Microorganisms studied or bioremediation function.
\r\n\t
",isbn:"978-1-80355-607-9",printIsbn:"978-1-80355-606-2",pdfIsbn:"978-1-80355-608-6",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!0,isSalesforceBook:!1,isNomenclature:!1,hash:"6cf0b844f6881c758c61cca10dc8b134",bookSignature:"Associate Prof. Gülşen Akın Evingür and Dr. Önder Pekcan",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/11830.jpg",keywords:"Elasticity, Toughness, Modulus, Compression, Extension, Optical Properties, Swelling, Drying, Diffusion, Release, Transmission Loss, Sound Absorption Coefficient",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"April 5th 2022",dateEndSecondStepPublish:"June 15th 2022",dateEndThirdStepPublish:"August 14th 2022",dateEndFourthStepPublish:"November 2nd 2022",dateEndFifthStepPublish:"January 1st 2023",dateConfirmationOfParticipation:null,remainingDaysToSecondStep:"15 days",secondStepPassed:!0,areRegistrationsClosed:!1,currentStepOfPublishingProcess:3,editedByType:null,kuFlag:!1,biosketch:"Dr. Evingür is a researcher in polymer composites and a lecturer at a maritime university. She has edited 2 books and has had 5 chapters published in international books, and 3 international and 5 national projects, respectively.",coeditorOneBiosketch:"Prof. Pekcan received their Ph.D. from the University of Wyoming, United States of America, in 1974. He has more than 362 SCI articles, 26 chapters, and 10 projects and is a member Science Academy in Turkey.",coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"180256",title:"Associate Prof.",name:"Gülşen",middleName:null,surname:"Akın Evingür",slug:"gulsen-akin-evingur",fullName:"Gülşen Akın Evingür",profilePictureURL:"https://mts.intechopen.com/storage/users/180256/images/system/180256.jpeg",biography:"Gülşen Akın Evingür graduated from Physics Department at the Yıldız Technical University (YTU, İstanbul, Turkey) in 1996. She completed her Master of Science degree in 2002 at the same department. The titled of her thesis was 'Electrical Properties of Polystyrene”. She received her PhD from Physics Engineering at İstanbul Technical University in 2011. The title of the thesis was 'Phase Transitions in Composite Gels”. She worked as an Assistant Professor between 2011 and 2018, and she is currently working as an Assosciate Professor at Pîrî Reis University, Istanbul, Turkey. She has been engaged in various academic studies in the fields of composites and their mechanical, optical, electrical, and acoustic properties. She has authored more than 60 SCI articles, 92 proceedings in national and international journals, respectively. She has edited \n 2 book, and has had 5 chapters published in international books, 3 international and 5 national projects, respectively.",institutionString:"Piri Reis University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"1",institution:{name:"Piri Reis University",institutionURL:null,country:{name:"Turkey"}}}],coeditorOne:{id:"27949",title:"Dr.",name:"Önder",middleName:null,surname:"Pekcan",slug:"onder-pekcan",fullName:"Önder Pekcan",profilePictureURL:"https://mts.intechopen.com/storage/users/27949/images/system/27949.jpeg",biography:"Prof. Pekcan received his MS Degree in Physics at the University of Chicago in June 1971, and then in May 1974 his PhD thesis on solid state physics was accepted at the University of Wyoming. \n\nHe started his career at Hacettepe University, Ankara, Turkey as Assistant Professor in 1974. Habilitation thesis on solid state physics was accepted in 1979. He became Associate Professor at Hacettepe University in 1979. \nHe visited ICTP Trieste, Italy as Visiting Scientist between June and August 1980. Between 1980 and 1981 he was a Visiting Scientist at the Technical University of Gdansk, Poland. \nHe worked as Visiting Professor at the Department of Chemistry, University of Toronto, Canada between 1981 and 1988. \nHe was appointed as full Professor at the Department of Physics, Istanbul Technical University, Turkey and worked there between 1988 and 2005. \nHe became an Elected Member of the Turkish Academy of Sciences (TÜBA) in January 1995. \nHe became the Dean of School of Arts and Sciences at the Istanbul Technical University in 1997. \nHe received the Science Award from the Scientific and Technological Research Council of Turkey (TÜBİTAK) in 1998. Prof. Pekcan was elected as Member of the Council of TÜBA in 2001 and Scientific Board of TÜBİTAK in 2003, respectively. \nHe was Head of the Department of Physics, and then became Dean of School of Arts and Sciences at the Işık University between 2005 and 2008.\nHe worked as Dean at the School of Art and Sciences, Kadir Has University (2008—2012). \nNow he is Professor at the Department of Bioinformatics and Genetics, Kadir Has University. Since 2012 he is a member of Science Academy. In the last few years Prof. Pekcan’s work covers mostly the area of biopolymers and nanocomposites.",institutionString:"Kadir Has University",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"2",totalChapterViews:"0",totalEditedBooks:"0",institution:{name:"Kadir Has University",institutionURL:null,country:{name:"Turkey"}}},coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"14",title:"Materials Science",slug:"materials-science"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"185543",firstName:"Maja",lastName:"Bozicevic",middleName:null,title:"Mrs.",imageUrl:"https://mts.intechopen.com/storage/users/185543/images/4748_n.jpeg",email:"maja.b@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. From chapter submission and review, to approval and revision, copyediting and design, until final publication, I work closely with authors and editors to ensure a simple and easy publishing process. I maintain constant and effective communication with authors, editors and reviewers, which allows for a level of personal support that enables contributors to fully commit and concentrate on the chapters they are writing, editing, or reviewing. I assist authors in the preparation of their full chapter submissions and track important deadlines and ensure they are met. I help to coordinate internal processes such as linguistic review, and monitor the technical aspects of the process. As an ASM I am also involved in the acquisition of editors. 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Contamination caused by petroleum hydrocarbon is a matter of worry because these are harmful for various life forms. Crude oil contamination is common due to its extensive use and its related dumping process and accidental spills. Complex mixture of a large range of high and low molecular weight hydrocarbons makes up the petroleum. The complex mixture of petroleum consists of saturated and branched alkanes, alkenes, and homo- and heterocyclic naphthenes; aromatics consisting of heteroatoms such as heavy metal complexes and N, S, and O; hydrocarbon consisting of different functional groups such as ethers, carboxylic acids, etc.; and large aromatic molecules such as asphaltenes, resins, and naptheno-aromatics.
Heavy metals are present in crude oil, and its heavy metal content is associated with porphyrins which is the pyrrolic structure. Lube oil waxes, light oil, asphaltenes, naphtha, diesel, kerosene, etc. are the several fractions in which the petroleum is refined. Light ends is the term that is used for the light fractions which are distilled at atmospheric pressure, and heavy ends is used for heavy fractions such as asphaltenes and lube oil. Due to different hydrocarbon compositions of light and heavy ends of petroleum, light ends consists of a lower percentage of aromatic compounds and lower molecular weight saturated and unsaturated hydrocarbons, while heavier ends consists of higher molecular weight saturated and unsaturated hydrocarbons, aromatic compounds with high molecular weight, and organometallic compounds. This part is relatively affluent in metals and nitrogen, sulfur, and oxygen-containing compounds [1].
Concentration of heavy metal is rising in the soil as a consequence of human action. There is a large impact of higher heavy metal and metalloid concentration in some areas [2].
This is caused mainly by accidents on oil platforms and ships used for hydrocarbon transportation but also by discharging water into the sea which is used to wash tanks of tanker vessels. Crude oil and petroleum products form a waterproof film on water that prevents the oxygen exchange between environment and water causing damages to plants, animals, and human beings. Nowadays during transport overseas, “double-hulled” tankers are used to avoid leaks in case of accidents. Best international practices are adopted with regard to oil platforms to face or eventually adequately deal with any type of inconvenience.
With the onset of industrialization, the use and buildup of organic compounds have increased. Major sources which are responsible for organic contaminants are anthropogenic activities including the use of fuels, solvents, and pesticides. Various organic compounds are harmful and are related to health concerns globally.
Diverse sources are responsible for the generation of hydrocarbons in sediments which are categorized below [3, 4]:
Anthropogenic sources
Petroleum inputs
Partial burning of fuels
Fires of forest and grass
Biosynthesis of hydrocarbons by marine or terrestrial organisms
Diffusing from the petroleum source rocks, reservoirs, or mantle
Organic pollutant is responsible for environmental and health-related problems; hence bioremediation provides an efficient explanation to this problem [5].
PAHs are considered to be ubiquitous contaminants. There are 100 diverse compounds of polycyclic aromatic hydrocarbons present. PAHs are seldom used for the industrial purpose, but only few are used for the manufacturing of pesticides, dyes, and plastics and for the production of medicines. Polycyclic aromatic hydrocarbons are produced on partial burning of organic matters [5]. PAHs due to carcinogenic and mutagenic nature are highly poisonous to organisms. The degradation of PAHs is predominantly slow with high molecular weights because due to low hydrophobicity and water solubility it has a tendency to accumulate in sediments [6]. PAHs have been classified as a priority pollutant by the USEPA which has classified 16 individual PAHs as pollutants due to its poisonous, carcinogenic, and mutagenic nature [7].
Polychlorinated biphenyls (PCBs) due to carcinogenicity, toxicity, and slow biodegradation in the nature are well thought-out to be the worst pollutants [8] of commercial PCBs of about hundreds of thousands of metric tons are persevere in aquatic sediments [9]. In adhesives and lubricants, dielectric fluids in flame retardants, transformers, hydraulic fluids, and plasticizers, PCBs are widely used. PCBs are released from disposal and spillage [10].
Polychlorinated dibenzo-p-dioxins and dibenzofurans (PCDD/Fs) are still present in deep sediment layers which are deposited decades ago. Toward biotic and abiotic degradation processes, PCDD/Fs are often well-thought-out to be recalcitrant [11]. PCDD/Fs are the most notorious pollutants present in nature [12].
Table 1 Microorganisms studied.
Pollutants | Organisms | Function | References |
---|---|---|---|
2,4,6-Trinitrotoluene (TNT) | Biotransformation | Boopathy and Kulpa [13] | |
Atrazine | Biodegradation | Newcombe and Crowley [14] | |
Chlorpyrifos | Biodegradation | Singh et al. [15] | |
Dibenzothiophene (DBT) | Biodegradation | Frassinetti et al. [16] | |
Hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX) | Biodegradation | Sherburne et al. [17] | |
PAHs | Biodegradation | Zhang and Hughes [18] | |
Phenanthrene, PAH | Biodegradation | Arun et al. [19] | |
Polychlorinated biphenyl (PCB) | Biodegradation | Aitken et al. [20] | |
Polycyclic aromatic hydrocarbon (PAH) | Biodegradation | Chung et al. [21] | |
Damaj and Ahmad [22] | |||
Fungi | Atagana [23] |
Microorganisms studied or bioremediation function.
Human sources are mainly responsible for the heavy metal contamination, but contamination due to natural and biological processes are also common which includes:
Mineral weathering over time.
Erosion and volcanic actions.
Forest fires and biogenic resource.
Vegetation causes release of particles.
Cellular binding sites of microbes are responsible for the absorption of heavy metals. By various mechanisms, heavy metals can be complexed with extracellular polymers of microbes. Organic contaminants can be mineralized by these microorganisms and convert into metabolic intermediates which can be utilized as primary substrates for growth of the cell. Heavy metals can be eliminated from the metal-polluted soil by microbes which can change the heavy metal oxidation state by immobilizing them [24]. Research on bioremediation of heavy metals by microbes has not been carried out extensively due to metal adsorption and incomplete knowledge of the genetics of the microbes.
Numerous sources such as pesticides, petroleum, or different harmful organic substances which are discharged into the water streams as effluents are responsible for the hydrocarbon pollution into the wastewater. Water contaminated with hydrocarbons is known to be carcinogenic, neurotoxin, and mutagenic to flora and fauna [25]. Contaminated lands, oil spillage, pesticides, automobile oils, and urban stormwater discharges are the major causes for the hydrocarbon contamination.
Oil spill is one of the major sources of hydrocarbon contamination. Oil spills caused mainly by accidents on oil platforms and ships are needed for transportation of hydrocarbon but also by disposal of water into the sea which is used to wash tanks of tanker vessels [2]. Underground oil storage tanks and leaking pipelines are also responsible for oil spilling in water [26, 27].
Increase use of vehicles and automobiles leads to increase in utilization of automobile oil, which is the major cause of hydrocarbon contamination in water. This type of contamination occurs when oil from the car drops onto the ground and leaks; it could be washed into water streams by runoffs [28].
Pesticides are another source of hydrocarbon contamination in water. Pesticides include herbicides, fungicides, and insecticides. Only small amount of pesticide is able to achieve the target, while the major proportion stays in the soil, and it can be washed away by the rain in the water stream [29]. Herbicides, out of all the pesticides, are most hazardous because it is directly applied on the soil in order to kill the weed and can be washed away during rainfall into the water streams.
Another source of hydrocarbon contamination in water is the land where some type of industrial action is being carried out. These lands contaminated by hydrocarbons or toxic organic compounds are washed due to rainfall into the water steams, thus causing pollution [30].
One of the main sources of hydrocarbon pollution is the discharge of urban stormwater. In urban communities, car parks and roads are frequently polluted by gasoline and oil from the vehicles, and during rainfall, these pollutants are washed into water streams and hence can contaminate them [30, 31].
Wastewater contaminated by hydrocarbons has an adverse effect in nature, animals, human beings, and plants. Lack of oxygen, decrease in crop yield, and effects on aquatic plants are various effects of hydrocarbon contamination in nature. There would be decrease in the crop yield and available food for household due to inappropriate crop’s growth when the farmland is irrigated by water contaminated with hydrocarbon [32, 33]. Soil fertility can be decreased to an extent due to the presence of oil in water due to the reason that most of the vital nutrients are no longer accessible for crop consumption which results in the decrease of the crop yield. The reduction in the yield of crop results in the decrease of the farmer’s earnings [34, 35].
Oxygen shortage is another environmental effect of hydrocarbon contamination. The main source of oxygen in nature is the economic trees which rely on rainfall or on the water steams for their growth. Oil spills can inhibit root penetration due to hydrocarbons which can block the pores of the soil, thereby removing water and air [36]. This results in the death of such plant or distortion in the growth and hence causes oxygen shortage for human utilization [37]. Hydrocarbon contamination in water avoids the penetration of light into the water and the exchange of gases for consumption by aquatic plants. This leads to the death of the plant because plant becomes incapable to photosynthesize and hence can affect the food chain. Plants consume the pollutants from the contaminated water which can be passed to humans and animals through the food chain [38].
Polycyclic hydrocarbons are toxic and found to have serious effects on human beings. The immune system, liver, respiratory system, reproductive system, circulatory system, kidney, etc. are the organs which are affected due to the hydrocarbon ingestion [33]. Individual’s susceptibility and level of exposure are the factors on which the degree of damage depends [2]. Cancer risk and hormonal problems that can disturb developmental and reproductive processes are the other effects of effluents polluted by hydrocarbons on human beings [39, 40, 41].
Discharge of wastewater contaminated with hydrocarbon into the water streams poses risk to animals through absorption, breathing, and ingestion. Sea birds are the most exposed to the hydrocarbon pollutant because it spends majority of its time near the water bodies [42]. There is unusual decrease in the temperature due to the destruction of the protective layer of the feathers in sea birds as a result of the presence of oil in water [43]. Scavengers such as ravens and vultures are also in danger when they consume preys and contaminated fish [44]. Water contaminated with hydrocarbon is consumed through gills of the fish during the respiration and accumulates in the gall bladder, liver, and stomach, and thus the fish becomes unhealthy for human utilization [45].
Polluted land or water systems have become a serious concern for human health. Over the past few decades, several methods have been developed and applied for the cleanups. The degradation either biological or chemical of petroleum which is a complex mixture of chemical substances is difficult because different treatments are required for different classes of compounds. Hence, remediation of oil-containing environment is not easy. Remediation strategies are decided after knowing the oil composition and physicochemical nature of the polluted site. Physical and chemical properties and pH of the polluted water/soil are the different factors on which the crude oil degradation depends. Oil-producing wells are generally situated near seashore, so due to this reason, water is contaminated mostly by oil spills during oil production operation. Oil spills are controlled by biological and chemical methods. Out of these two methods, chemical method is more frequently used. Bioremediation is gaining worldwide attention.
Contamination due to petroleum is widespread in the environment and contaminates surface and groundwater [46]. Several operations in petroleum exploration, leaking of underground storage tanks, and its production and transportation are responsible for affecting the environment [47]. Contamination causes threat to human health and safety and can affect nature by contaminating surface and groundwater [46].
Efforts are made both nationally and internationally in order to remediate the pollution caused by hydrocarbon contamination which can cause environmental and health risk. There are three methods involved in the remediation of sites contaminated due to hydrocarbon [2, 48]:
Phytoremediation
Bioremediation
Chemical remediation
Phytoremediation is the process which involves the use of plants for the degradation, extraction, and elimination of the contaminants from the air, water, and soil [40, 49, 50, 51]. It includes various mechanisms which can lead to degradation of contaminants, dissipation, immobilization, and accumulation [52, 53]. Various phytoremediation applications with examples are systematically given in Table 2.
Application | Media | Contaminants | Typical plants |
---|---|---|---|
Phytotransformation | Soil, groundwater, landfill leachate, land application of wastewater | Herbicides, aromatics, chlorinated aliphatics, nutrients, ammunition waste | Phreatophyte trees (popular, willow, cottonwood, aspen) Grasses (rye, Bermuda, sorghum, fescue) Legumes (clover, alfalfa, cowpeas) |
Rhizosphere bioremediation | Soil, sediments, land application of wastewater | Organic contaminants (pesticides, aromatics, and polynuclear aromatic hydrocarbons) | Phenolic releasers (mulberry, apple, Osage orange) Grasses with fibrous roots (rye, fescue, Bermuda) for contaminants 0.3 ft deep Phreatophyte trees for 0.10 ft Aquatic plants for sediments |
Phytostabilization | Soil, sediments | Metals (Pb, Cd, Zn, As, Cu, Cr, Se, U), hydrophobic organics (PAHs, PCNBs, dioxins, furans, pentachlorophenol, DDT, dieldrin) | Phreatophyte trees to transpire large amounts of water for hydraulic control Grasses with fibrous roots to stabilize soil erosion Dense root systems are needed to sorb/bind contaminants |
Phytoextraction | Soil, brown fields, sediments | Metals (Pb, Cd, Zn, Ni, Cu) with EDTA addition for Pb selenium (volatilization) | Sunflowers Indian mustard Rape seed plants Barley Hops Crucifers Serpentine plants Nettles Dandelions |
Rhizofiltration | Groundwater, water and wastewater in lagoons or created wetlands | Metals (Pb, Cd, Zn, Ni, Cu), radionuclides (137Cs, 90 Sr, U), hydrophobic organics | Aquatic plants: emergents (bulrush, cattail, coontail, pondweed, arrowroot, duckweed); submergents (algae, stonewort, parrot’s feather, Eurasian watermilfoil, hydrilla) |
Application of phytoremediation with examples.
Contaminated land and water are remediated more feasibly by using plants involving a variety of pollutant attenuation mechanisms than physical and chemical remediation techniques [54, 55, 56, 57, 58]. Plants due to their sedentary nature had developed various abilities for dealing with hazardous compounds. Plants serve as solar-driven pumping and filtering systems as they take up pollutants from the soil through the roots which is transported to various parts of the plant by the help of plant tissues where they can be volatilized, metabolized, or sequestered [57, 59]. Different types of mechanisms are used by the plant for removing the pollutants from the soil. They consist of biophysical and biochemical processes such as adsorption, translocation, and transport, as well as mineralization and transformation by plant enzymes are the mechanisms of phytoremediation [8]. Halogenated substances like TCE are degraded by plants using oxidative degradation pathways, and it includes plant-specific dehalogenases. After the death of the plant, the dehalogenase activity is still maintained [60]. Laccases, P450 monooxygenases, nitroreductases, dioxygenases, phosphatases, peroxidases, dehalogenases, and nitrilases are various contaminant-degrading enzymes which are present in plants [61, 62, 63]. The basic physiological mechanisms involved in phytoremediation in higher plants and related microorganisms, such as mineral nutrition, photosynthesis, transpiration, and metabolism. The root of the plant is responsible for the uptake of the organic and inorganic compounds from the soil, and it can bind and stabilize substance on its external surfaces on interaction with microorganism in the rhizosphere. Uptake or release of molecules occurs through exchanging gases from the aerial plant’s parts with the atmosphere [64]. For addressing different contaminants in different substrates, six phytotechnologies have been recognized by Interstate Technology and Regulatory Cooperation:
For organic contaminants, phytotransformation is ideal in all substrates.
Rhizosphere bioremediation is used in soil containing organic contaminants.
Phytostabilization is used in soil for organic and inorganic pollutants.
Phytoextraction is useful in substrates containing inorganic pollutants.
Phytovolatilization is used for volatile substances.
Hydraulic flow can be controlled in the contaminated environment by using evapotranspiration.
Bioremediation is a cost-efficient method used for the treatment of soil polluted with oil and wastes of petroleum consisting of biodegradable hydrocarbons and indigenous microbes.
The management of suitable levels of nutrient fertilizer addition, moisture control to optimize soil degradation by microorganisms, aeration and mixing, and pH amendment are required for the process of land treatment [65].
Enzymes attack on some inorganic compounds and on most of the organic compounds through the activities of living organisms. Bioremediation is the technique which involves the productive use of the biodegradative process for the elimination or detoxification of pollutants from the environment.
Oil spill causes contamination of soil which is considered as the chief worldwide concern. Pollution of soil due to petroleum causes a serious effect to human being, affects the groundwater, decreases the agricultural production of the soil, and causes economic loss and ecological problems. Plants, animals, microorganisms, and humans are affected by the toxicity of the petroleum hydrocarbons. Oil spill and accidents occur due to the transportation of crude oil which is generally through tankers on water or through land pipeline. Problems of the oil contamination occur mostly due to the reason that the main oil-producing countries are not the chief oil clients; hence petroleum is transported to the consumption area. Certain microorganisms are accountable for the petroleum hydrocarbon degradation and are used as the resource of carbon and energy for growth and maintenance. Soil contamination can be remediated by many ways including both physicochemical and biological techniques.
Biological techniques are more economical and proficient than physicochemical techniques. The degradation rate of petroleum products is increased by developing several remediation methods. Bioremediation through microorganism is considered to be the most effective method in comparison to other biological methods, but the high molecular weight hydrocarbons with low adsorption and solubility limit their accessibility to microorganisms.
Composite mixture of diverse chemical substances makes up the crude oil. Oil and its component are recognized by microbes using bioemulsifiers and biosurfactants, and then they join themselves; hydrocarbon is used as the resource of carbon and energy. High molecular weight hydrocarbons due to their low adsorption and solubility limit their accessibility to microorganisms. Oil biodegradation rates are improved by the biosurfactant’s addition which increases the elimination and solubility of these pollutants.
The oil constituents vary particularly in susceptibility, volatility, and volubility to biodegradation. A number of substances are easily degraded, some are non-biodegradable, and some oppose degradation. Diverse species of microbes preferentially attack diverse compounds due to this biodegradation of petroleum that occurs at different rates but concurrently. Enzymes produced by microorganisms in the presence of sources of carbon are accountable for attacking the hydrocarbon molecules. Hydrocarbon present in the petroleum is degraded by different enzymes and metabolic pathways. Hydrocarbon degradation is prevented by the lack of suitable enzyme [66].
Bioremediation process involves the utilization of natural microorganisms for the decontamination of atmosphere [67]. This process converts pollutants into useful or nontoxic substances by using bacteria, fungi, and yeast which are the naturally occurring microorganisms [40]. This is also a process in which microorganisms restore the quality of the environment by degrading and metabolizing the chemical substances [48]. Table 3 represents the main microorganisms which are included in the remediation of hydrocarbons.
Bacteria | Yeast and fungi |
---|---|
List of microorganisms for bioremediation.
Microbial species has efficient hydrocarbon degradation capability in natural environments. Various microbial species have been isolated from heavily polluted coastal areas, variety of oil spill, or soil contaminated by petroleum. These are isolated on the basis of their capability to metabolize different sources of carbon such as aliphatic and aromatic compounds and their chlorinated derivate. Enrichment culture procedures were used for obtaining the microorganisms, and for the selection criterion, maximum final cell concentration or maximum specific growth rate was used. Various microorganisms such as fungi, microalgae, bacteria, and yeast [68] are used for degrading the petroleum hydrocarbons. Out of these microorganisms, bacteria play a significant role for hydrocarbon degradation. Rapid degradation of low molecular weight alkanes is reported by various studies. The capability of microorganisms to use hydrocarbons to assure the growth of cell and energy requirements by degrading hydrocarbon is the driving force for the petroleum biodegradation. Biodegradation of petroleum is carried out more extensively by mixed cultures in comparison to pure culture [69]. Adequate indigenous microbial community in many ecosystems is capable of biodegradation of oil, but for oil degradation metabolic activity, environmental conditions should be favorable. Indigenous microorganisms have several advantages than adding microorganisms for hydrocarbon degradation.
For the biodegradation of hydrocarbons in soils, fungi play a more vital role than bacteria. Filamentous fungi which are found in aquatic structures are mostly related with surface films and sediments. The enzymatic processes used by mammalian organizations are also used by fungi in polycyclic aromatic hydrocarbons (PAHs). Two major types of cytochrome P450 monooxygenases have been well characterized in yeasts and filamentous fungi. Several fungi have the ability to oxidize polycyclic aromatic hydrocarbons to phenols, dihydrodiols, and other metabolites and conjugates, but only some fungi such as
Example:
The biodegradability of various yeasts decreases from n-alkanes > branched alkanes > low molecular weight aromatic hydrocarbons > cycloalkanes > high molecular weight aromatic and polar compounds.
Bioremediation process involves the detoxification of pollutants due to the various metabolic capabilities of microorganisms which is the developing method for elimination of contaminants from nature together with the yields of the petroleum industry [70]. Bioremediation technique is considered to be cost-effective and noninvasive. Petroleum and other hydrocarbon contaminants can be eliminated from the atmosphere by using microorganisms which is considered as primary mechanism, and it is the cheaper method in comparison to other remediation technologies. Microorganisms having suitable metabolic capabilities are the essential requirement.
Alkylaromatic degradation is carried out by various microorganisms such as
Fungi, bacteria, and yeast are accountable for the biodegradation of hydrocarbons in the environment. Six percent [71] to 82% [72] is the reported efficiency of biodegradation for soil fungi, 0.003–100% [73] for marine bacteria, and 0.13% [71] to 50% [72] for soil bacteria. Complex mixtures of hydrocarbons such as crude oil in freshwater, aquatic environments, and soil are degraded by mixed populations with overall wide enzymatic capacities [74].
Bioremediation involves two processes as follows:
Bioaugmentation
Biostimulation
Bioaugmentation process involves the degradation of the harmful hydrocarbons by the addition of microorganisms in order to achieve the pollutant reduction [67]. It is also the injection of polluted water with microorganisms capable of hydrocarbon degradation [48]. This process sometimes involves biodegradation of the hydrocarbon pollutants by adding the genetically engineered microorganisms into the polluted water [75]. Bioaugmentation process is not often used for the hydrocarbon degradation because microorganisms responsible for hydrocarbon degradation naturally exist in the environment. Bioaugmentation process is not so much effective to be used in oil spill remediation sites, and nonindigenous microorganisms used in this process can cause competition with the microbes already present in the environment [76].
Biostimulation is the process which involves degradation of the harmful compounds by adding the nutrients required by indigenous hydrocarbon-degrading microbes [67]. The growth of microorganisms responsible for the degradation of oil during oil spillage is activated by the increase in carbon. The tendency of the microorganisms to degrade the hydrocarbons is enhanced by addition of suitable concentration of supplemental nutrients. Due to this reason, microorganisms are competent of achieving their utmost rate of growth and consequently the utmost rate of contaminant uptake [77, 78]. The maximum biostimulation is achieved by obtaining the ideal nutrient concentration which is required for the utmost growth of the microorganisms and maintaining concentration as long as possible for microorganisms [79].
This process requires the use of chemicals. Contaminants can be treated by using various chemicals. Chemicals usually have the capability of altering the contaminant’s chemical and physical properties [80]. Dispersants, solidifiers, and chemical oxidants are the three categories in which the chemical remediations are grouped [2, 48, 52].
Slick of oil can be broken down into smaller droplets by surfactants which are present in dispersants, and these droplets undergo rapid dilution by transferring it into the water and can be effortlessly degraded [81]. Chemical dispersants can raise the oil droplet surface area which results in an increased rate of natural biodegradation, and this process makes the oil less sticky to the surface by slowing down the development of oil-water emulsions and allows fast treatment [82]. This method makes oil spills less harmful for living organisms and the marine life. This is achieved by converting oil slicks into droplets which in turn can be degraded by bacteria [2, 81]. Nokomis 3-F4, Slickgone NS, Finasol OSR 52, SPC 1000™, Neon AB3000, ZI-400, Corexit 9500, Corexit 8667, and Saf-Ron Gold are some of the examples of chemical dispersants [83].
In this method oil is removed by physical method which involves the interaction of dry granular materials with the oil and converts its liquid state into rubberlike solid state. Dry particulate and semisolid substances such as balls, pucks, sponge, etc. are the various forms in which the solidifiers can be applied. Solidification can be enhanced by using the solidifiers in the seas because mixing energy is provided by the seawater. Solidifiers are difficult to recover after solidification, and it is less efficient, which are the major drawbacks for the use of the solidifiers [82, 84].
This technique involves the usage of chemical agents which are capable of oxidizing the organic pollutants [85]. These chemical agents are introduced by the help of the mixing apparatus and injection in water or soil at the contaminated site. The usefulness of the process is found to depend upon oxidant quality, efficient contact between pollutant and oxidant, geological conditions, and oxidant’s residence time [86]. This process is rapid and can be applied in all weather situations which are some of the advantages of this process. Table 4 represents the details of other advantages and disadvantages.
Chemical treatment | Advantages | Disadvantages |
---|---|---|
Dispersants | Suitable in all weather condition and for wide range of oils | No oil recovery Not effective on highly viscous, non-spreading, and waxy oil |
Accelerates by degradation of the oil by natural processes Advanced formulations have reduced the previous concerns about toxicity Less man power needed Less expensive than mechanical methods | The localized and temporary increase in the amount of oil in water concentration that would have an effect on the surrounding marine life If dispersion is not achieved, other response method effectiveness may reduce on less disperse oil | |
Solidifiers | All weather conditions Quick | Lack of practical application Large amount required Selected oil Not effective No oil recovery |
Advantages and disadvantages of chemical treatment.
There are various techniques involved for the elimination of oil from the surface of the sea and to avoid the oil to reach the shoreline. The widely used methods are mechanical recovery and the application of dispersants. The crude oil spreads over the sea surface because it is lighter than water and the thickness of the oil film becomes very thin in a small time. Type of oil, temperature of atmosphere, tide, temperature of water, and wind are the factors on which the velocity of oil spreading depends.
If oil spills accidentally, then the spreading of the oil can be prevented by using skimmers and booms which can control the spill to a short area, and finally the oil can be collected into the container. Oil can be solubilized by applying biosurfactants which are generally not detrimental to nature.
For oil spill remediation, at times in situ oil burning is also used as an optional method; but in situ method is useful only when the spilled layer of oil is floating on the surface of the water, oil spill is fresh, or after the oil has been converted into a smaller area by the booms. The above technique has some drawback that aquatic system gets polluted by the by-products and smoke generated as a result of burning of oil. Weather, tides, and ocean currents are the factors on which the usefulness of the cleaning method depends. If the oil reaches the shoreline, different methods are applied to clean up the gravels and sand. Oil is absorbed sometimes by oil sorbents similar to sponge. Oil is removed from the oiled vegetation by washing with water, but the plants damaged severely should be detached completely.
When the amount of contaminated water is less than ex situ, remediation method is applied by pumping the contaminated water to the processing site. The shore sand and gravels are removed and cleaned in a different place from the contaminated site.
Pollution of soil occurs due to leakages from pipes and wellheads during offshore oil production and drilling operations, leakage from underground storage tanks of petroleum, overflow from gathering stations, petroleum yields, and inappropriate dumping of waste of petroleum. During the excavation, transport, and handling of polluted material, significant risk may be created by this method. For the final disposal of the substance, it is very hard to locate new landfill sites. There is continuous requirement of monitoring and maintenance of separation barriers since the pollutant remains on the site, and hence cap and containment technique is the temporary solution.
Methods for the treatment of soil contamination are as follows:
In situ
Ex situ
This method involves physicochemical processes including air sparging, soil air extraction, or by combinations of these two methods applied to the soil at the contaminated site. Vertical & horizontal fossil fuel drilling equipment’s are used
The growth of aerobic bacteria on oxygen feeding is accelerated by the help of this method. Air sparging can be also performed under the water table if the contamination takes place in the groundwater through extraction wells or to the surface by gravity segregation. The oil can be extracted from the oil saturated ground water or partially saturated soil by using a process called as slurping.
The volatile components which are trapped in the soil are extracted by injecting steam into the contaminated soil.
This technique involves the elimination and transportation of polluted soil to off-site remediation ability. Various processes are used to perform the ex situ remediation which is as follows:
Land farming process is used in which soil polluted with oil is excavated and spread above a bed where it once in a while is tilled until the contaminants are degraded. Fifteen to 35 cm of soil surface is treated with the help of this technique. Composting involves the increase in the development of the microbial species by mixing polluted soil with harmless organic compounds to contaminated soil. Bioreactors are used for the bioprocessing of polluted soil, sediment, and water in which the three phases, gas, soil, and liquid, are mixed continuously in order to enhance the biodegradation rate. Before loading the contaminated soil to the bioreactors, the soil is pretreated. Contaminants undergo chemical reaction and convert harmful compounds into nontoxic compounds. Dechlorination or UV is used for the catalyzation of the oxidation reactions. These techniques have a few limitations such as high cost due to the complication of the method required, while bioremediation due to natural biological action is a choice which provides the chance to degrade the hydrocarbon contaminants.
Ecologically sound, natural process; there is an increase in the number of the existing microorganisms when the contaminants are present, and the microbial population decreases naturally when the contaminants are degraded. The residues such as water, carbon dioxide, and fatty acids obtained as a result of the biological treatment are usually nonhazardous product, and the obtained CO2 can be used for the photosynthesis process by the plants.
Bioremediation is responsible for destroying the target chemicals in place of transferring the contaminants from one place to another.
Other techniques which are used for the cleanup of harmful waste are more costly than bioremediation. For example, through the cleanup of the Exxon Valdez spill, the cost of 1-day physical washing is more than bioremediating 120 km of shoreline.
Bioremediation deals with in situ treatment and does not involve the transfer of a large amount of the polluted wastes off-site, and the risk due to the transportation can be overcome.
Microbe efficiency can be enhanced by using nutrient formulation in the bioremediation process.
The residues such as CO2, fatty acids, water, etc. obtained from the biological treatment are generally nonhazardous.
It is a less costly technique than other techniques which are used for cleaning up of the toxic waste.
Hydrocarbons due to their different solubility from polar compounds such as methanol have lower polarity and hence have low solubility. Degradation of hydrocarbons is not only determined by solubilization. Many microorganisms are responsible for increasing the surface area of the substrate by excreting emulsifiers including
Hydrocarbon pollutants have a widely applicable consequence on land, aquatic, as well as atmospheric ecosystem. This has been a problem ever since the use of fossil fuels and industrial revolution started. The unparalleled growth in populations with frequent oil spills, leakages in pipelines, and rampant use of pesticides contribute to substantial increase in pollution. These together are threatening the lives of animals and native microbiological population in land, air, and water surfaces and subsurfaces. Thus environmental remediation is the most important aspect of human survival. This book not only highlights the causes but also explains the techniques used in pollution rectifications. The various remediations described in this chapter are (i) phytoremediation, (ii) bioremediation, and (iii) chemical remediation.
The task of my earliest work in pathology was to find out whether there was a soluble serum precursor for amyloidosis (This spacious scientific field has been reviewed pain part recently) [1, 2]. In experimental murine amyloidosis induced by septic conditions [3], morphologically significant signs are visible in Figure 1 showing large amounts of hepatic amyloid (white areas), now recognized as amyloid A (AA). This amyloid was first deposited at the sites where the blood stream entered from the triangle of Glisson into the liver capillaries. The entire branches of blood vessels entering the liver parenchyma (left large vessel) are decorated with amyloid and, on the other hand, the branches that allow the blood to leave the liver are devoid of amyloid (right large vessel). This implies that the amyloidogenic protein is being deposited immediately when it reaches the liver upon assumed changing conditions (still unknown) by which amyloid is deposited from a soluble precursor. With time, the deposits grow by apposition toward the central liver vein (darker areas) until most of the liver is transformed into amyloid in a fatal amyloidosis. This behavior requires a consistent, steady and very fast transformation of an assumed precursor to amyloid by entering the liver capillaries. The amyloid is deposited under pressure and visible as the rough liver surface (at the top), which is usually sleek.
Photomicrograph of murine AA amyloidosis. Tissue section showing hepatic capillary amyloid deposits (white areas) induced by septic multi-microbial exposure after 25 days. The amyloid is deposited under pressure visible as the rough liver surface (at the top), which is usually sleek. Formalin-fixation, 4–6 μm paraffin section, HE-staining, magnification 24.1× [
When the assumed precursor is present in blood, as suggested by morphologic evidence, it should cross the anastomosis between artificial Siamese twins (parabiosis) with one partner induced to develop amyloidosis through septic conditions. However, this transmission does not always occur. The septic partner developed amyloid in 92.5% of pairs and the untreated partner in only 13.4%, and the latter was statistically not different to that seen in control pairs without any treatment [4]. The failure of crossing the anastomosis was excluded by 51Cr-tagged erythrocytes [5]. Since the anastomosis was fully permeable, this type of parabiotic barrier was not an absolute one but a relative one caused by a short half-life of the agent that was removed from the bloodstream before it could cross the permeable anastomosis. The results of quantitation of the blood flow by 51Cr erythrocytes, including a mathematical model of the exchange rate, shows that half of the blood was exchanged between the partners in 22.3 min. Therefore, a short half-life far below 22.3 min indicates a protein with a rapid clearance in minutes or even seconds, a property that is addressed today as an
The half-life of SAA1 and SAA2 in plasma of normal mice was reported for SAA-HDL as a T1/2 of 75–80 min and both isotypes were similar. However, when trace amounts of SAA were given, they were rapidly cleared [6]. Another report measured the clearance of the complex SAA-HDL for SAA1 T1/2 of 75 min and SAA2 T1/2 of 30 min, respectively. The clearance was delayed when both isotypes were bound to high-density lipoprotein (HDL) [7]. Both reports did not measure SAA under acute-phase conditions (APC). However, the report of Hoffman and Benditt [6] found a rapid clearance with trace amounts of SAA devoid of HDL and confirmed our data that are performed under a septic acute-phase condition that was to be observed when SAA was separated from HDL (see below).
Amyloids of different clinical settings (also in animals, see Figure 1) represent characteristic fibrils under electron microscopy [8]. Therefore, for chemical identification of the amyloid, these fibrils had to be extracted in pure form followed by chromatographic isolation of the major amyloid protein for its chemical analysis by amino acid sequence analysis. The method of isolation of the pure amyloid fibrils was pioneered by Pras et al. [9]. The first amino acid sequence of an amyloid protein was published by Glenner et al. [10], which was derived from a monoclonal immunoglobulin κ-light chain and was named ALκ. The first sequence identifying the chemical nature of inflammation-induced amyloid in monkey and human amyloid was published by Benditt et al. [11], which was named amyloid A (AA). The first anti-AA antibodies were prepared in rabbits where a serum protein in patients suffering from inflammations was detected immunochemically. This protein had an α1-electrophoretic mobility and was in serum approximately 180 KDa by calibrated gel filtration [12] and thus ready to monitor the isolation of the soluble with anti-AA reactive precursor. This isolation of serum protein began in summer 1972 and was monitored with another rabbit anti-AA antibody. Its chromatographic separation from serum yielded a native 200 ± 20 kDa AA reactive protein, which was further chromatographically isolated in 5 M guanidine-HCl. The AA reactive protein had an α2-electrophoretic mobility and a molecular size of 12.5 kDa. Since this new protein had the same N-terminal amino acid sequence as AA, it was named serum amyloid A (SAA) [13]. Since SAA was larger than AA, a limited proteolytic cleavage had to be presumed in order for the former to generate AA. During the isolation of SAA and its purification to one size by gel filtration, by isoelectric focusing, however, eight SAA bands of different isoelectric point named A-H were identified with anti-AA antibodies (with AAE as the major SAA species for the planned radioimmunoassay), thus indicating the first signs of a polymorphism of SAA [13]. In addition, in plasma, SAA is bound to HDL [14].
When examining a patient’s acute-phase serum (APS) with elevated SAA in immunodiffusion (ID) at different temperatures and different times using a polyclonal AA antiserum in comparison with isolated control AA, this resulted in the three different precipitation patterns presented in Figure 2. In (a), one recognizes a line of identity of AA with all four patients’ sera as if the SAA (probably SAA1 and SAA2) reaction were done with pure SAA. At 4°C in (b), however, there is no reaction with SAA-HDL in serum. This is due to the hiding of the AA-reactive parts of SAA through HDL. However, when the temperature was switched to room temperature after the reaction in (b) at 4°C the SAA containing serum resulted in a strong line after releasing the SAA from HDL in (c) as seen in (a). However, different from the pattern in (a), the precipitation line of AA-anti-AA is somewhat independent of the SAA-anti-AA line, thus indicating that the homologous AA-anti-AA line seems to be more stable than the SAA-anti-AA line. These results show that SAA-HDL is stable in full APS at 4°C where the AA-reactive sites are covered by HDL. When at room temperature (in ID buffer), where SAA is released from HDL and is now accessible to antibodies for precipitation, it is reactive. Therefore, the separation of SAA from HDL is temperature dependent [15]. These results became only fully explainable through Section 3.2, where the separation of SAA from HDL became clear [14].
Immunochemical comparison of SAA-HDL, SAA and AA. Immunodiffusion (ID) at different temperatures [
In addition, we prepared recombinant SAA2 and, when added to normal human serum, it was possible to repeat exactly that behavior reported in Figure 2. This shows that SAA alone can reproduce this phenomenon [16].
Temperature-dependent molecular weight determination of AA-antigenic proteins of acute-phase serum (APS) has been performed using an ACA-34 gel filtration column in PBS with the enzyme inhibitor phenylmethylsulfonylfloride (PMSF) under various temperatures as shown in Figure 3. The size grading was done by the serum proteins IgM, IgG, albumin and, in addition, cytochrome C and the salt marker N-ε-DNP-lysine. The proteins were identified by way of the size position in the column by immunodiffusion as SAA-HDL at a size of ca. 180–200 kDa or SAA at 12.5 kDa. The different temperatures were kept with a temperature-controlled glass jacket, that is at 37°C in column run A, at 38°C in B, at 40°C in C and at 42°C in D. E was run as D, but without enzyme protection by PMSF, thus showing some degradation of SAA [18].
Size separation of SAA-HDL at febrile temperatures. SAA-HDL in a patient’s acute-phase serum with a common cold was separated in A at 37°C, B at 38°C, C at 40°C and D at 42°C by gel filtration. All individual fractions (20–70) were examined and semi-quantified by ID using polyclonal rabbit anti-AA antibodies [
At a normal body temperature of 37°C, AA-containing proteins are at a single position as that of the SAA-HDL stable complex in A (fractions 34–37). However, already at 38°C, the stable complex SAA-HDL begins to dissociate as shown in Figure 3, run B. AA antigenic proteins appear at three positions, that is first of all at the void volume at fractions 19–20 (which has not been further analyzed, but could be related to aggregated SAA and/or its derivatives), secondly at the position of the stable SAA-HDL complex at fractions 34–36 and thirdly at the position of the HDL-free SAA at 53–56, as determined by the antigenic differentiation as seen in Figure 2. This size differentiation may also indicate functional heterogeneity, as the different affinities of SAA to HDL. This dissociation begins at 38°C and progresses with diminution of the SAA-HDL complex until run C. SAA-HDL disappeared at a “threshold of life” in run D at 42°C and above where the SAA species was maximized and the broadest was seen at fraction 53–56. This shows a temperature-induced gradual dissociation of SAA from HDL at the different febrile temperatures, which was shown here in vitro. This may also occur under systemic and local, acute-phase conditions, with the release of different SAA isotypes at different temperatures, for functions to be discovered. Finally, the SAA monomers released at different temperatures differ in size. SAA in B is somewhat smaller than SAA in C. In addition, both appear at 42°C in D together as a broad combination of the two SAAs in B and D. In conclusion, SAA separated from HDL at 38°C in B has a lower affinity to HDL and is smaller, and SAA with a higher affinity for HDL is larger. Different isotypes and sizes of SAA are known [1, 2, 13]. The acute-phase SAAs, aSAA1 and aSAA2, are each 12.5 kDa with 104 amino acids and the constitutive SAA (cSAA), which is 14 kDa and has 112 amino acids. Since SAA1 has the lowest affinity for HDL and is the most amyloidogenic SAA, it could have separated from HDL in run at 38°C in B already, while SAA4, which is somewhat larger than the aSAAs, could be a component in the C. These indications can be solidified using isoelectric focusing or SAA-isotype-specific antibodies [1, 2].
While these experiments above were done stepwise, one by one, a more precise dissociation of the SAA-HDL separation was performed by electrophoresis in 1.5% agarose across a continuous temperature gradient in a single flat gel, as shown in Figure 4. The two sides between the agarose gel were kept at a constant temperature of 15°C in T1 and of 65°C in T2 [17].
Electrophoresis of SAA-HDL across a continuous temperature gradient in agarose [
The results in Figure 4 show two horizontal bands of samples of one patient in the form of dots across the temperature gradient. The SAA-HDL band of α1-electrophoretic mobility is marginally stained due to the concealing of the AA-antigenic determinants of SAA within the SAA-HDL complex at low temperatures. The hiding of the antigenic determinants disappeared gradually from 38°C (the 5th sample) until it is completely above 42°C with the appearance of large amounts of SAA (intensive staining of the band with α2-mobility). By gradually increasing the temperature, the SAA release increases gradually while the SAA-HDL fades away up to the extreme exposure at 42°C and beyond, in agreement with the stepwise separation of SAA from HDL shown in Figure 3. Also important during this gradual temperature-induced separation from HDL seems to be that the morphology of the dots is different. They changed by their shape in the longitudinal direction, which is consistent with the fact that SAA is not uniform and consists of a group of homologous, but chemically different, SAAs demonstrating different isoelectric points (13 reviewed by [1, 2]). Another observation concerns the AA-antigenic species below 37°C in the first four samples. These slow, arc-like uniform samples could represent an SAA species, which is always active as a monomer regardless of temperature. This species seems to be less acidic. It could be a type of SAA species for the general protection under normal condition. In sample 5, this “arc SAA” is overlaid by a more acidic SAA released from the acute-phase proteins (APPs) SAA1 or SAA2, thus changing the spots to a more longitudinal pattern. With increasing temperature, the SAA spots become thicker and increase more in the longitudinal direction. This “arc SAA” needs to be analyzed since it does not seem to be part of the intact SAA-HDL complex (we did not check for SAA4). Finally, far above a temperature of 42°C, the SAA species seems to be stable. Parallel to the gradual release of SAA, at the same time, the SAA-HDL complex while losing SAA is gaining more negative charges with increased temperatures. Moreover, the trailing of SAA in samples 5–8 possibly indicates the gradual separation of differently charged SAA species.
Taken together [15, 17, 18, 21], it is clear that the mechanism of separation of SAA from HDL in vitro is also strictly regulated in vivo by body temperatures above 37°C. Therefore, this is a key mechanism that can be induced and activated basically by two different manifestations. The most common is the orthologic APR activation [36] of SAA. This occurs with a maximal SAA concentration of up to 1000 times within a day as a systemic “biochemical thunderstorm” with a myriad of activating and inhibiting events simultaneously, which are not understood in detail today [1, 2]. During these events, the cause of the APR will be eradicated and the APR becomes curative. With this beneficial outcome, the normal immune homeostasis returns in a foreseeable future. However, when the APR cannot overcome its initial cause, it will become a pathologic APR [36] with a “persistent biochemical thunderstorm” and lacking a self-driven cure. The consequences can be summarized in an exhaustion of the resources of the organism and decline of the metabolic activity through a multitude of clinically challenging conditions exemplified by severe viral and bacterial chronic inflammations, systemic inflammatory response syndrome (SIRS) or uncontrolled chronic infections, sepsis and septic shock [1, 2]. Moreover, when the infection remains limited, a local APR will take care of it.
The functions of the four human isotypes, SAA1, SAA2, (SAA3 in humans is only transcribed in some cells) and SAA4 have not been fully analyzed. They have arisen through gene duplications, thus indicating important individual functions either alone or in combination. As described before, the human acute-phase A-SAA has two very similar isotypes, A-SAA1 and A-SAA2, in the APR mostly synthesized in the liver and expressed in most body cells (see below) and the constitutive C-SAA4 and some allotypes in SAA1 and SAA2. For a review of the SAA heterogeneity and its known functions, see the reviews [1, 2].
Another discovery was the discontinuous separation of SAA from HDL described above at different temperatures, meaning that not all SAA molecules are being separated from HDL at a single temperature except for the temperature of 42°C (Figures 3 and 4). In fact, these figures show that the separation of SAA is spreading out over the whole febrile temperature range starting from 38°C to 42°C and above. In addition, based on these observations in Figure 4, it is possible that SAA isotypes and allotypes are separated from HDL at different febrile temperatures and thereafter fulfill their different functions locally or systematically as individual SAA species as is also to be derived from Figure 3. Another indication for the differential release of the SAA species can be detected in Figure 4 in the different shapes of the protein blots of the SAAs devoid of HDL, thus indicating possible SAAs with distinct isoelectric points (IP). In Figure 4, there are free dots before 37°C named (for convenience) “arc SAA,” the least acidic SAA. The SAA species released from HDL after 37°C (“38 SAA”) are probably the more acidic ones. In this sense, the dot changes also occur later on 39°C-, 40°C-released SAA, etc. Analyzing the spots for the identity of the various SAA species could show whether these indications did discover a mechanism by which the different SAA species can be released from HDL and thereby are being activated at specific temperatures alone or with other SAAs for special purposes, which need to be analyzed. These points may also be of therapeutical interest. This proposed temperature selection of SAA isotypes could specify the needed APR function for a specific purpose. The increase of the organism’s temperature is being induced by the organism as a response to various stimuli, exemplified by bacterial invasion. It could represent some sort of a “gear shift” for providing a graded response in order to release special SAAs to provide adequate amounts, which are necessary “tools” for survival. This could occur in concert with other agents including other APPs and cytokines of the APR network. The possible therapeutical manipulation of the body’s temperature (“the gear shift”) in vivo needs the precise analysis of this phenomenon in vivo first.
In a collaborative study, each of the eight species-specific polyclonal AA antibodies against eight species (including humans) was immunohistochemically tested against the AA amyloids of eleven different species, including those of humans. The results showed a strong reactivity only with the homologous species and with only some cross-reaction with a related species. The reactivity was in general species specific, but a universal generic AA antibody could not be obtained in these eight polyclonal antibodies [37].
The next step was to produce murine monoclonal antibodies against AA and SAA [20]. Their value and merit have been documented by the inventors Köhler and Milstein [38]. Monoclonal antibodies are represented by one amino acid sequence and have the value of a chemical reagent. We selected 20 stable clones (see Table 1), which were epitope mapped [31] and immunohistochemically tested on AA amyloids in 10 different mammals, many humans and 9 different birds. Some cross-reactivity with some monoclonals was detected. Most of the 19 AA amyloids tested could be identified with the two monoclonals mc4 and mc29, showing that most of these AA amyloids have some peptides in common and these antibodies recognize the same or very similar epitopes of AA in different species. In addition, antibodies of all clones were tested for binding with 15 synthetic SAA peptides in only 4 clones the epitope could be identified. These included the known clones mc4 and mc29 (see above), and the two new ones, mc1 and mc20 (see Table 1). In APS, two different charge variants of SAA have been detected with these monoclonals [22].
For notes | Clone no | Internal lab K-Nr. | Isotype | Quality | References (selected) | ||
---|---|---|---|---|---|---|---|
Epitope and SAA peptides | Usage IHC | Usage EM | |||||
mc 1* | 17 | IgG 2a κ | 5–16 7–15 | +++ | +++ | [16, 18, 22, 25, 27, 28, 29, 42, 44, 45] | |
mc 2 | ++ | [22] | |||||
mc 3 | 33 | + | |||||
mc 4 | 34 | IgG 1 κ | 19–31 | +++ | +++ | [16, 18, 22, 25, 27, 28, 29, 46, 48] | |
mc 8 | 38, 57 | IgG 3 κ | 25–76 | ++ | 0 | [22, 25, 29] | |
mc 9 | 39, 41, 53 | IgG 1 κ | +++ | 0 | [22, 24, 25, 29] | ||
mc 12 | 40, 42 | IgG 2b κ | 25–76 | ++ | 0 | [22, 24, 25, 29] | |
mc 13 | 43, 54 | IgG 1 κ | +++ | ++ | [22, 25, 28, 29] | ||
mc 15 | 45 | + | |||||
mc 17 | 47 | + | |||||
mc 20 | 50, 28 60 | IgG 2a κ | 60–75 25–76 | ++ | +++ | [16, 18, 22, 24, 25, 29] | |
mc 21 | 65 | IgG 1 κ | 33-42 | +++ | [32] | ||
mc 22 | 70 | IgG 2b κ | + | 0 | [25] | ||
mc 23 | 63 | IgG 1 κ | + | ||||
mc 25 | 55, 124, 125, 126 | ++ | |||||
mc 27 | 77, 127 | IgM κ | ++ | ||||
mc 28 | 58, 128 | +++ | + | ||||
mc 29 | 129 | IgG 1 κ | 28–40 25–76 | +++ | +++ | [16, 18, 24, 28, 29, 36, 37, 41, 42, 43, 44, 45, 46, 48] | |
mc 30 | 130 | IgG 1 κ | +++ | ||||
mc 31 | 131 | IgG 1 κ | + | 0 | [25] |
Monoclonal AA and SAA antibodies [20].
Available from Dako, Denmark.
Explanations: IHC, immunohistochemistry; EM, immunoelectron histochemistry.
The cause of the failing reactivity of most of the synthetic peptides with most of the monoclonals may be due to the presence of more discontinuous epitopes. This could also be deduced from the fact that SAA shows multiple short peptides that alternate between the invariable (red) and the variable (white) peptides, as shown in Figure 5 (see also below).
Structure of SAA and epitope-mapped AA monoclonal antibodies. The structure of SAA 1–104 and its fragments AA 1-76 and SL-77-104 with invariant (in red) and variant (white in between the red) peptides and epitope mapped of five monoclonal AA/SAA antibodies. There are three species-independent (mc4, mc21 and mc29), and two variant as well as species-specific (mc1 and mc20) monoclonal antibodies against AA and SAA. The positions of epitopes on the α-helical coils 1–4 and the contribution of the invariable (red) and variable peptides are also visible.
Moreover, since mc21 was negative with the linear peptides, but reacted very strongly with AA amyloid in tissues, it was epitope mapped differently. It was mapped with endoproteinase Asp-N-generated peptides from a pure and partially amino acid-sequenced human AA (KIR) protein of 8.4 kDa. Of the 11 distinct peptides separated by RP-HPLC, mc21 reacted only with a single peptide, which was aa 33–42 of SAA [32]. This peptide is almost identical with the largest invariant peptide of SAA (see Figure 5). Two other monoclonals mc9 and mc13 did not show any reaction with these 11 distinct HPLC peaks [32] although they were reactive with AA in tissue sections. Here again, in linear SAA peptides, the discontinuous epitopes of SAA may not be preserved.
Therefore, another strategy for the epitope mapping has been worked out that is the cooperative precipitation with either the antigens AA or SAA in 1.5% agarose gel. Applied were various combinations of two different monoclonals on one antigen, respectively. A precipitation showed that the two given monoclonals react with two epitopes. This approach resulted in precipitations and the epitope could be estimated roughly in some of the antibodies (unpublished). This has been expected since all the AA/SAA antibodies were selected by reactivity with amyloid in tissues. Finally, precipitation with SAA but not with AA pointed to a monoclonal against the SL peptide (see Figure 5, aa 77–104). Similarly, SAA isotype-specific monoclonals could have been selected by a similar approach.
Monoclonals (see Table 1) are being applied for classification of AA amyloid in tissue sections when a recent amyloidosis was diagnosed in a patient or in an animal. Every amyloid has to be classified for therapeutic and prognostic purposes. This is exemplified in exploiting the generic monoclonals mc4 and mc29 (in Refs. [23, 24]) by either the immunohistochemical classification (IHC) on paraffin section of animal AA amyloidosis [23, 24] or by the immunoelectron microscopic classification (EM) of human AA amyloid on ultrathin sections [25].
The SAA1 and SAA2 proteins are presented in Figure 5 as a continuous string with 1–104 amino acids. SAA consists of two parts, the N-terminal AA 1–76 polypeptide, which causes AA amyloidosis in humans [11] and animals under unfavorable inflammatory conditions [23, 24], and the C-terminal SL 77–104 polypeptide, whose function is stabilizing the two double coils [39, 40]. Figure 5 was constructed using data from the USCS Genome Browser (GRCH38hg38) Assembly, as reported by 2.
The structure of SAA consists of four α-helical coils, 1–4, with 1–27, 32–47, 50–69 and 73–88 aa in length, respectively, followed by a tail after the 4th coil. These four coils are arranged in two antiparallel double coils, whereby 1 joins 3 and 2 joins 4 [39]. Each α-helix and its tail contain alternating blocks of twenty invariable peptides (Figure 5, in red, numbered 1–20). The variable peptides that can be species specific are the white, unstained sites in between the invariable peptides. Variables are also the peptides joining the coils, which represent the turns. In addition, the tail is winding around these double coils for stabilization [39, 40]. This conformation of SAA with the short-distance, alternating peptides in red and white would need more exact three-dimensional analyses for identifying the proposed discontinuities of peptides based on the partial un-reactivity of the monoclonals with linear peptides (see above).
The monoclonal antibodies can be divided into three categories by the kind of epitope onto which they bind. In (a), they bind to species-specific epitopes and could perhaps also be detected with polyclonal antibodies [37]; in (b), they bind to AA amyloid in tissue section, but not to synthetic linear peptides, and are probably reacting with discontinuous epitopes of the SAA, and in (c), they bind to species independent, i.e., the invariant peptides and epitopes of AA and SAA, which are almost identical throughout the vertebrates (reviewed in [1, 2]). These special antibodies can also be called “generic” AA/SAA antibodies. Generic SAA antibodies are mc4, mc21 and mc29 (the latter contains also an additional specificity; see later). The two monoclonals that functionally bind to variable epitopes are mc1 and mc20 and belong to a category in (a). All monoclonals and their known binding synthetic peptides are listed in Table 1, together with their binding to patients’ and animals’ AA amyloid in formalin-fixed paraffin tissue sections [20, 23, 24] and ultrathin sections for EM [25].
The binding sites of the monoclonals to SAA are shown in Figure 5. The invariant parts of SAA contain ancient peptide clusters preserved during their evolution from the lampreys (over 500 Mio years without hardly any changes, Wikipedia) to the mammals, including humans. Again, we as humans have the invariable peptides of SAA in common with all vertebrates and the lamprey. Therefore, these special peptides have to be of utmost importance for mechanisms related to the proteostasis of many systems. They become extremely activated when in imbalance, exemplified by injuries and inflammation or bacterial infection, and in the event that their activation cannot be resolved. This can result in a sepsis. Thus, one can assume with some likelihood that a single amino acid exchange in these 19 invariant areas must not have been accepted throughout evolution. Indications are in the literature that natural SAA behaves differently as compared to recombinant SAA or SAA with a single amino acid change or exchange [1, 2]. The importance of the proteins of the SAA family for survival can therefore hardly be overestimated and the phrase that SAA is “the hub in the interaction network” [40] can express this eminent role of the SAA.
This monoclonal antibody mc1 (see Table 1 and Figure 5) is of interest since it binds to the most N-terminally positioned human-specific epitope on SAA (aa 5–16), but only when it is devoid of HDL. Thus, SAA can be distinguished from SAA-HDL through the failure of mc1 to bind to the complex of SAA-HDL, since HLD conceals the mc1 epitope of SAA [15]. Recombinant SAA shows the same binding to HDL and the same temperature release of SAA from HDL in vitro [21]. When separated from HDL under febrile temperatures, it can rebind again to HDL at body (or lower) temperatures. The binding is therefore reversible except when the temperature is above 41°C for some time, when it probably aggregates irreversibly [34]. The temperature-dependent mechanism has been proposed for activating the SAAs (see Figures 2–4). When fever is systemic, the free SAA load is part of the systemic APR. When local febrile temperatures are induced by local injuries or infection, a local APR is induced with local SAA. This can also apply for local tumors (see below). How this acts is not fully known. Where is the mc1 epitope located, considering that three invariant peptides are located within the 5–16 peptide stretch? Since the specificity is human specific, these peptides should be among the 2–3 variant areas; those are probably the white areas of the 5–16 peptide stretch; see Figure 5. In addition, this mc1 epitope (aa 5–16) has an overlap of 7 [5, 6, 7, 8, 9, 10, 11] of the 11 aa residues with the presumptive lipid-binding site (aa 1–11) (established by Turnell et al. [41]). Finally, mc1 binds very reliably to human (and some primate) AA in fixed paraffin sections and in ultrathin sections for EM [25], and not to SAA-HDL in serum at lower body temperatures (see above). Therefore, this murine monoclonal anti-AA mc1 has become a standard for examining human AA and SAA (available from Dako).
In tissue sections, this monoclonal (see Table 1 and Figure 5) reliably binds to human AA amyloid and is being used for diagnostic purposes. It binds to the synthetic peptide aa 60–75 of SAA, which is located at the longest variable peptide stretch of SAA and located at the C-terminal half of the third α-helical coil, and, to a minor extent, at the small N-terminal part of the fourth coil, which contains the first invariable peptide no. 12. We do not know whether this mini peptide is part of the mc20 paratope.
These antibodies demonstrated immunohistochemical, species-independent binding to most AA-type amyloids of the vertebrates (see above). They were therefore directed against the invariant peptides of SAA, which are located on the first and second α-helical coils. Their extent and their differences are depicted in Figure 5. The clone mc4 reacts largely with the invariant peptide no. 4–6 on coil 1. This clone binds differently as compared to mc21 and mc29, both of which bind to the 7th peptide of coil 2, the largest invariant peptide of SAA. While mc21 seems to be only reacting with peptide no. 7, the monoclonal mc29 extends to the variant joining peptide area (aa 28–32) that is between coil 1 and coil 2. This may explain the additional, partial binding of mc29 to the variable peptides. In addition, it binds to most of the animal AA amyloids tested (see below).
This series of monoclonal antibodies has been probed and exerted to establish a monoclonal micro-ELISA for quantification of SAA [42].
Various functions of SAA have been reported, including the systemic and local elevation of SAA in inflammations in an APR due to the systemic and local cytokine increase. SAA is involved in very many functions as being an opsonin of Gram-negative bacteria, a chemoattractant, an inducer of chemokines and cytokines, a stimulator of angiogenesis, important in cholesterol transport and a modulator in the migration of white blood cells. SAA acts concentration dependently on polymorphonuclear cells and the degradation of SAA (by matrix degradation enzymes?), which can release the AA 1–76 fragment and can thereby induce the fatal AA amyloidosis in humans and animals. Other fragments of SAA and other APPs may, in vivo, influence this still not understood complex network of the SAA family, which has been reviewed in [1, 2, 43, 44]. Here, some of these vital functions of SAA have been identified by blocking these functions by way of monoclonal AA/SAA antibodies. At the same time, the SAA binding motives have been localized at the surface of SAA (see Figure 5). Alternatively, these ligands for the SAA binding motives can, in part, be blocked with the respective synthetic peptides of SAA [44, 45].
The HDL binding site of SAA was identified as the peptide aa 5–17 with the monoclonal mc1 (see Section 4). The presumptive estimate by Turnell et al. [41] was aa 1–11.
Strong binding of isolated, acute-phase human SAA (and recombinant SAA2, not presented) were shown with human neutrophils [33] assuming the existence of an SAA receptor, which may have regulatory functions [1, 2]. The FMLP-induced oxidative burst of normal human neutrophils could be reduced, concentration dependently, by SAA at concentrations of 0.1 μg/ml and 1.0 μg/ml. This inhibitory reduction of SAA could be blocked by the monoclonal antibody mc29 (see Table 1 and Figure 5), which binds to the synthetic peptide aa 28–40 of SAA, thus proving that this blocked area is responsible for this inhibitory effect of SAA [33]. This was the first time that a function of SAA was blocked by a monoclonal AA antibody. Moreover, at the same time, the responsible peptide of SAA was identified, which was the invariant peptide no. 7 of coil 2. The monoclonal antibody mc29 used probably also blocks the laminin-like domain (aa 29–33) and may also be participating partially with the RGD-like domain (aa 39–41). In addition, human neutrophils were exposed to full human APS at different temperatures [34]. At 41°C, the inhibition of the oxidative burst was much stronger than at 37°C, indicating the role of SAA freed from HDL and in its active state (see Section 3.4; see Figures 3 and 4). However, when the acute-phase serum was preheated to 41°C for 15 min and assayed at 37°C, the SAA-containing serum did not return to the 37°C value, but stayed with the increased 41°C inhibiting effect at 37°C. This indicated an irreversible structural change of SAA (or its fragments) during high fever, which is blocking SAA’s return to the reversible binding to HDL. (This febrile temperature that induced the aggregation of AA-antigenic proteins has also been noticed in vitro and documented in Figure 3 at 38°C and 40°C). The possibly unfavorable consequences of these aggregates in humans or animals are unknown today.
The anti-inflammatory potential of SAA on neutrophils [33] has been confirmed for SAA at reported serum concentrations [46]. Oxidative burst, migration and the neutrophil myeloperoxidase release were also inhibited. SAA peptides (aa 1–14, 15–101 and 83–104) also contributed to this inhibitory effect. However, at higher concentrations of more than 50 μg/ml, SAA was stimulating. In addition, O2 release was inhibited up to 0.1 μg/ml, but the O2 release was increased above that. Thus, SAA plays a dual role, it downregulates inflammatory processes in lower concentration, but, during the full APR, the action of SAA can be promoting.
SAA functions can be identified by SAA-generic antibodies [33, 34, 46] but they can also be blocked by synthetic peptides of SAA [45]. This was shown through the use of a 14mer synthetic peptide (aa 29–42) of SAA. This peptide inhibited the binding of T lymphocytes and mouse M4 melanoma cells to adhesive glycoproteins of the extra cellular matrix. This SAA 14mer peptide contained the laminin-like (aa 29–33) and fibronectin-like (aa 13–15) domains of the extracellular matrix. Finally, by extending these data of the 14mer SAA peptide, by comparing to the binding of our generic antibodies mc21 and mc29, it is to be said that these antibodies bind to a similar peptide of SAA, which is the largest invariable peptide (no. 7 of coil 2) as shown in Figure 5.
Phagocytosis was examined on fixed bacteria by normal and stimulated blood monocytes at the SAA concentration that were inhibitory to human neutrophil activation [33]. There was no difference in phagocytosis in the presence or in the absence of SAA [47].
Human platelet adhesion was shown to immobilize SAA and the mechanism of binding was examined [35]. Among the many receptors on platelets, the receptors for laminin and fibronectin were chosen to be examined because SAA has laminin-like and fibronectin-like motives in its sequence. Immobilized SAA binds platelets as do fibronectin and, to a lesser degree, fibrinogen. This binding of SAA to platelets was completely abolished by anti-SAA (mc29), which binds to the laminin-like motive on SAA (aa 29–33) that is part of the mc29-binding peptide. Also, a 29–42-containing peptide could inhibit the binding of platelets to SAA. In addition, an antibody against an integrin receptor also inhibited the binding as well the RGD-containing peptide GRGDSP. Also, the anti-SAA (mc29) did not inhibit the RGD-dependent binding motive to a significant extent, thus indicating that the overlap of two amino acids (aa 39–40) of the peptide (see Figure 5) did not lead to an efficient paratope subsite of mc29 for the method applied. Finally, all controls were in line with the conclusion that SAA was binding to platelets via the laminin-like and fibronectin-like motives. Since the related binding motives are not chemically identical with laminin or fibronectin, they could have a lower affinity, which may be exerted differently at lower concentrations as compared with higher concentrations, i.e., during the APR.
Thus, SAA may play a role in inhibiting and modulating platelet adhesion at vascular injury sites by sharing platelet receptors with other platelet-adhesive proteins. In addition, depending on the kind of disease, the window between bleeding and thrombosis may sometimes be very narrow; how can it be widened? Finally, systemic and local thrombosis are not rare, which are life-threatening sequels of many conditions. These are related to arteriosclerosis, heart conditions, nutrition-related ailments, deranged lipid metabolism, smoking and other drugs, cancer, injuries, bacterial infections and sepsis, mostly in a more advanced age as well as in cases of vascular injury. The role of platelets is central in these and many other diseases, and the concentration-dependent role of SAA and its antidotes (humanized monoclonals and others) in vivo needs to be explored and then further developed.
Intracellular SAA of colon tissue with cancer of progressing stages of anaplasia was examined on formalin-fixed paraffin sections from 26 patients with colon cancer (after SAA plasma levels were shown by others to be elevated in carcinomas, assuming that the elevated SAA is of hepatic origin) [26]. SAA was detected immunohistochemically by using the monoclonal antibodies mc1 and mc29 (specificity, see Figure 5 and Table 1). On normal cells, no reaction or only traces were detected. However, stronger reactions were found in carcinoma cells. The staining intensity increased gradually from dysplasia to the stage of malignant neoplasia. The metastases also showed the presence of SAA, but weaker. In addition, cells, other than colon cells in these sections, also showed the presence of SAA as lymphoid cells of the intestinal wall, inflammatory cells, ganglion cells and endothelial cells. The presence of SAA has been confirmed by in situ hybridization and reverse transcriptase polymerase chain reaction (RT-PCR). The genes of SAA1 and SAA4 in the colon carcinomas were activated. Although the role of SAA in colon carcinoma is unknown, the close association of the increasing grade of malignancy with the increased SAA synthesis may indicate a role of SAA in tumorigenesis. SAA can serve as an adhesive ligand for tumor-cell homing; it induces inflammation, which may be neoplastic. It also induces migration and can be involved in metastasis, or it can be inhibitory to attachment [26].
The colon carcinoma cell line HT-29 showed plasminogen activity (PA) enhanced by SAA measured with a chromogenic substrate. This activity could be inhibited using monoclonal antibodies against SAA (mc1 + mc29). The cell line also produced endogenous SAA1 by itself, which could be augmented by exogenous SAA and also by cytokines IL-1b and IL-6. This activity was also inhibited in part by the monoclonal antibodies against SAA [36]. The concomitant overexpression and co-localization of SAA and PA in colon cancer cells raises the possibility of a functional relationship between these two systems. The authors suggest that SAA produced in the malignant tissue may contribute to increased matrix degeneration and tumor spread [36].
Increased levels of SAA were reported in a wide range of malignancies, as well as another unspecific tumor marker, with an increase in metastatic tumors and regression when therapy is successful [26]. Here, the presence of SAA in serum (with CRP and CA-123) and expressed locally in tissues was examined and compared with different stages of tumor growth. Compared were normal ovarian tissues, benign, borderline, carcinoma and metastatic tissues of patients using immunohistochemistry with monoclonal antibodies against AA (mc1 and mc29, see Table 1 and Figure 5) and in situ hybridization. In some patients (and in cell line OVCR-3), RT-PCR was applied, and SAA1 and SAA4 were detected. The result shows a continuous increase of SAA (CRP and CA-125) in serum during the gradual increase of the malignant nature of the ovarian tissue proliferation. In addition, and most important, the SAA expression in tissue increases, in the same manner, with a steep increase in the SAA-synthesizing cells from the normal cells, without (or with only a trace of) SAA, over the borderline tumors with weak expression to the maximal expression of the distinct carcinomas and metastases. Therefore, it is likely that the serum level of SAA in these malignancies may, in part, originate from the ovarian tumor itself.
The data show that the quantity of local intracellular expression of SAA correlates directly with the grade of malignancy of the ovarian epithelial neoplasias and runs in parallel with the serum value of SAA, CRP and CA-125. Therefore, SAA may have a role in ovarian tumorigenesis [27].
Ovarian reproduction includes a kind of inflammatory process [28]. Therefore, the cellular expression and localization of SAA in all stages of follicular development was examined in in vitro fertilization (IVF) patients applying nonradioactive in situ hybridization and immunochemistry with the monoclonal anti-AA (mc1 and mc29) antibodies. In parallel, SAA of follicular fluids and SAA in serum were examined using micro-ELISA. Expression of SAA mRNA was found in all follicular cells (granulosa, thecal and luteal) of all stages of development, from primordial, primary and secondary follicles to corpora lutea and even in oocytes.
The concentration of SAA in serum and in the matched follicular fluid was very closely associated (R2 = 0.80), although both values could vary considerably by a factor of ca. 30× for blood SAA and by 100× for the follicular fluid. In addition, elevated follicular SAA values have a strong correlation with the patients’ body mass index. Values over 30 are associated with a reduced pregnancy rate. Taken together, SAA is locally produced by all follicular cells and is a constituent of the follicular fluid. Therefore, it has a role in ovarian development and in the rate of pregnancy, which is reduced when SAA values are too high in overweight female patients with a BMI of over 30.
Finally, since human ovarian epithelial tissues reproduce SAA during reproduction (see above), the neoplastic degenerated cells in ovarian carcinoma continue their SAA synthesis [26].
In order to analyze the different steps necessary to overcome an infection by the hepatic APR, an experimental mouse model was applied and shown as an “anti-sepsis circle” (see Figure 6) [26]. Using polymicrobial sepsis induced by cecal ligation and puncture (CLP), the various actions begin with mice exposed to a bacterial overload that leads to the IL-6 induction, which is the dominant interleukin and major inductor of the APR. IL-6-deficient mice can still mount an APR, since IL-6 represents one member of a larger group of interleukins with redundant actions. The action of IL-6 is to initiate the intracellular signaling via the hepatic IL-6 receptor gp130 and further induction of STAT3, which is inevitable for developing the full hepatic APR in hepatic cells, including the synthesis of the dominant APP SAA. However, when mice with a deletion of gp130 or STAT3 are treated with CLP, the hepatic synthesis of SAA is not induced and these mice cannot mount an APR anymore and are thus defenseless, and mortality is greatly increased. The missing APR and the missing defense can be reversed by adding myeloid-derived suppressor cells (MDSCs), which are induced by a hepatic APR including SAA. SAA induces and activates the proliferation of bone marrow cells, which include MDSCs. These cells are accepted to be able to also act against the microbial infection. MDSCs are anti-inflammatory in cancer, cancer spread and metastases [27]. They home-in on different organs. In septic mice, they have been examined from spleen and increase their numbers when pg130 and STAT deficiency are overcome by an injection of SAA, cxc1 (KC) or SAA/KC. MDSC can be regarded as a second anti-inflammatory wave induced by SAA and the other components of the APPs when the first wave of anti-inflammatory phagocytes is beginning to wane while becoming exhausted [1, 2, 27].
Closing the sepsis loop to the “anti-sepsis circle” schematically.
When very important functions of SAA (which need to be more clarified) are being blocked by the monoclonal antibodies mc4 and mc29 in CLP mice, the essential MDSCs cannot be produced to the necessary amount and function to cope with the bacterial load so that the mice become defenseless and display a significantly accelerated death rate. This unfavorable situation can be reverted by the injection of SAA, thereby resulting in the former defense with the proliferation of MDSCs, so that the mice survived like CLP-treated mice in this sepsis model [29, 30, 48]. The APP KC has a similar, but not identical, effect. When KC was added to SAA, the recovery from the CLP fate of mice with a murine SAA inactivated by antibodies may even be slightly improved, thus indicating that SAA, although the major and dominant APP, can be assisted by KC against the bacterial load.
This demonstrates a cooperative defense of SAA and KC [29]. Cooperation can also be expected from other APPs and constituents in the APP network, including from the greater SAA family. The AA antibodies mc4 and mc29 bind to invariant and therefore very important peptides of SAA as described in detail in Section 4.2, in Table 1 and Figure 5. With these antibodies, life-saving biological functions have been detected and their functions localized to invariant peptides of SAA. This approach could be extended to analyze all the invariant peptides of the SAA family. This can be regarded as a starting point for a possible therapy of a long list of such maladies as severe chronic inflammations and severe chronic infections including sepsis with (induced in vivo or recombinant) SAA isotypes (and their inhibitors as humanized generic SAA antibodies), and with other APPs and constituents of the network of the SAA family, which are able to fortify the “anti-sepsis circle” (Figure 6).
Some essential elements of the cooperative defense against the experimental multi-microbial infections became apparent as shown in Figure 6. The pathway from infection procedures passes, through IL-6, gp130 and STAT3, to the APR with the dominant SAA family and its network. This loop has been closed to a circle through the action of at least the SAA1 that assisted in inducing the growth of the MDSCs in the bone marrow. These cells are also shown to be essential in fighting bacterial infection. However, when gp130 or SAA was not available in this model and the “circle” was interrupted, with fatal consequences, the addition of the missing agents restored the circle with its function [29]. It should be an important goal to examine the SAA isotypes in different inflammatory states and diseases in relation to febrile temperatures (Figures 3 and 4) and to analyze the functions of all 20 invariant peptides (Figure 5) and the epitopes of the AA/SAA antibodies (Table 1) in order fortify it.
It is also important to define the febrile temperatures by which the individual SAAs separate from HDL (proven in vitro, Figures 3 and 4) and get activated to execute their function. A novel idea could be: therapeutical hypothermia below 37°C could inactivate SAA through binding to HDL, which can be called “hypothermic deactivation of SAA.” This option could be considered (after complying with the strict rules for a novel therapy) in severe inflammatory states exemplified by sepsis, septic shock, genetic hyperthermia syndromes and similar diseases summarized in SIRS (systemic inflammatory response syndrome). Inversely, a temperature-dependent conformational change of SAA at above 38°C causing SAA release from HDL can induce a “hyper-thermic activation of SAA,” which could be beneficial for patients having clinical syndromes with body temperatures of 36°C and below.
The presented view summarizes peptides of SAA that are decisive for innate humoral functions in different systems. This view can be applied to many possible possible inflammatory and infectious diseases, including sepsis. These SAA peptides provide a functional innate humoral “stop and go” mechanisms located on SAA (“SAA checkpoints”) related to survival. Stop, with generic (humanized) AA/SAA monoclonal antibodies or equivalent agents, and go, with the bio-identical SAA preparations, including SAA isotypes or related peptides with special SAA functions (Figure 5), which need to be further explored to find out their additional role in the SAA network. This examination can also be extended to other APPs.
Due to its novelty within the field of innate immunity and the possibly far-reaching impact in medicine, in particular, in inflammatory diseases including sepsis, these discoveries by three inventors were in agreement with the two other inventors patented by the author [49, 50].
This chapter is dedicated to Professor Dr. Konrad Beyreuther, Heidelberg and Professor Dr. Robert Huber, Martinsried, Germany.
For help with the figures, I thank Ms. Anne Linke, Zürich, Switzerland.
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Zouaghi"},{id:"147368",title:"Dr.",name:"Fetheddine",middleName:null,surname:"Melki",slug:"fetheddine-melki",fullName:"Fetheddine Melki"}]},{id:"30707",doi:"10.5772/29917",title:"Radon as Earthquake Precursor",slug:"radon-as-earthquake-precursor",totalDownloads:3768,totalCrossrefCites:12,totalDimensionsCites:21,abstract:null,book:{id:"2051",slug:"earthquake-research-and-analysis-statistical-studies-observations-and-planning",title:"Earthquake Research and Analysis",fullTitle:"Earthquake Research and Analysis - Statistical Studies, Observations and Planning"},signatures:"Giuseppina Immè and Daniela Morelli",authors:[{id:"79901",title:"Dr.",name:"Daniela",middleName:null,surname:"Morelli",slug:"daniela-morelli",fullName:"Daniela Morelli"},{id:"81874",title:"Prof.",name:"Giuseppina",middleName:null,surname:"Immè",slug:"giuseppina-imme",fullName:"Giuseppina Immè"}]},{id:"43258",doi:"10.5772/55439",title:"Speedy Techniques to Evaluate Seismic Site Effects in Particular Geomorphologic Conditions: Faults, Cavities, Landslides and Topographic Irregularities",slug:"speedy-techniques-to-evaluate-seismic-site-effects-in-particular-geomorphologic-conditions-faults-ca",totalDownloads:3040,totalCrossrefCites:8,totalDimensionsCites:20,abstract:null,book:{id:"3059",slug:"engineering-seismology-geotechnical-and-structural-earthquake-engineering",title:"Engineering Seismology, Geotechnical and Structural Earthquake Engineering",fullTitle:"Engineering Seismology, Geotechnical and Structural Earthquake Engineering"},signatures:"F. Panzera, G. Lombardo, S. D’Amico and P. Galea",authors:[{id:"52181",title:"Dr.",name:"Sebastiano",middleName:null,surname:"D'Amico",slug:"sebastiano-d'amico",fullName:"Sebastiano D'Amico"},{id:"58678",title:"Dr.",name:"Pauline",middleName:null,surname:"Galea",slug:"pauline-galea",fullName:"Pauline Galea"},{id:"167864",title:"Prof.",name:"Giuseppe",middleName:null,surname:"Lombardo",slug:"giuseppe-lombardo",fullName:"Giuseppe Lombardo"},{id:"167865",title:"Dr.",name:"Francesco",middleName:null,surname:"Panzera",slug:"francesco-panzera",fullName:"Francesco Panzera"}]}],mostDownloadedChaptersLast30Days:[{id:"64562",title:"Electrical Resistivity Tomography: A Subsurface-Imaging Technique",slug:"electrical-resistivity-tomography-a-subsurface-imaging-technique",totalDownloads:3183,totalCrossrefCites:7,totalDimensionsCites:10,abstract:"Electrical resistivity tomography (ERT) is a popular geophysical subsurface-imaging technique and widely applied to mineral prospecting, hydrological exploration, environmental investigation and civil engineering, as well as archaeological mapping. This chapter offers an overall review of technical aspects of ERT, which includes the fundamental theory of direct-current (DC) resistivity exploration, electrode arrays for data acquisition, numerical modelling methods and tomographic inversion algorithms. The section of fundamental theory shows basic formulae and principle of DC resistivity exploration. The section of electrode arrays summarises the previous study on all traditional-electrode arrays and recommends 4 electrode arrays for data acquisition of surface ERT and 3 electrode arrays for cross-hole ERT. The section of numerical modelling demonstrates an advanced version of finite-element method, called Gaussian quadrature grid approach, which is advantageous to a numerical simulation of ERT for complex geological models. The section of tomographic inversion presents the generalised standard conjugate gradient algorithms for both the l1- and l2-normed inversions. After that, some synthetic and real imaging examples are given to show the near-surface imaging capabilities of ERT.",book:{id:"8361",slug:"applied-geophysics-with-case-studies-on-environmental-exploration-and-engineering-geophysics",title:"Applied Geophysics with Case Studies on Environmental, Exploration and Engineering Geophysics",fullTitle:"Applied Geophysics with Case Studies on Environmental, Exploration and Engineering Geophysics"},signatures:"Bing Zhou",authors:null},{id:"37864",title:"Role of the NE-SW Hercynian Master Fault Systems and Associated Lineaments on the Structuring and Evolution of the Mesozoic and Cenozoic Basins of the Alpine Margin, Northern Tunisia",slug:"role-of-the-ne-sw-hercynian-master-fault-systems-and-associated-lineaments-on-the-structuring-and-ev",totalDownloads:8225,totalCrossrefCites:17,totalDimensionsCites:26,abstract:null,book:{id:"2227",slug:"tectonics-recent-advances",title:"Tectonics",fullTitle:"Tectonics - Recent Advances"},signatures:"Fetheddine Melki, Taher Zouaghi, Mohamed Ben Chelbi, Mourad Bédir and Fouad Zargouni",authors:[{id:"39860",title:"Dr.",name:"Taher",middleName:null,surname:"Zouaghi",slug:"taher-zouaghi",fullName:"Taher Zouaghi"},{id:"147368",title:"Dr.",name:"Fetheddine",middleName:null,surname:"Melki",slug:"fetheddine-melki",fullName:"Fetheddine Melki"}]},{id:"43258",title:"Speedy Techniques to Evaluate Seismic Site Effects in Particular Geomorphologic Conditions: Faults, Cavities, Landslides and Topographic Irregularities",slug:"speedy-techniques-to-evaluate-seismic-site-effects-in-particular-geomorphologic-conditions-faults-ca",totalDownloads:3040,totalCrossrefCites:8,totalDimensionsCites:20,abstract:null,book:{id:"3059",slug:"engineering-seismology-geotechnical-and-structural-earthquake-engineering",title:"Engineering Seismology, Geotechnical and Structural Earthquake Engineering",fullTitle:"Engineering Seismology, Geotechnical and Structural Earthquake Engineering"},signatures:"F. Panzera, G. Lombardo, S. D’Amico and P. Galea",authors:[{id:"52181",title:"Dr.",name:"Sebastiano",middleName:null,surname:"D'Amico",slug:"sebastiano-d'amico",fullName:"Sebastiano D'Amico"},{id:"58678",title:"Dr.",name:"Pauline",middleName:null,surname:"Galea",slug:"pauline-galea",fullName:"Pauline Galea"},{id:"167864",title:"Prof.",name:"Giuseppe",middleName:null,surname:"Lombardo",slug:"giuseppe-lombardo",fullName:"Giuseppe Lombardo"},{id:"167865",title:"Dr.",name:"Francesco",middleName:null,surname:"Panzera",slug:"francesco-panzera",fullName:"Francesco Panzera"}]},{id:"64060",title:"Advance Wave Modeling and Diffractions for High-Resolution Subsurface Seismic Imaging",slug:"advance-wave-modeling-and-diffractions-for-high-resolution-subsurface-seismic-imaging",totalDownloads:1175,totalCrossrefCites:2,totalDimensionsCites:2,abstract:"Seismic modeling and Imaging for the small-scale feature in a complex subsurface geology such as salt deposit, fracture reservoir, and Carbonate is not casual because of propagated wave affected by many objects once it hits the geologic structure in the subsurface. The principal goal of newly developed seismic modeling & imaging is to get a subsurface image of structural features with greatest sharpness or resolution. Using model dataset the Sigsbee and Marmousi, we illustrate the accuracy of conventional and advance wave modeling techniques. However, in conventional a Finite difference (FD) algorithm is used to generate the data and in advanced wave modeling, the low-rank (LR) approximation is used to acquire zero-offset configuration data. A field dataset from Malaysian basin is re-processed and imaged using diffraction imaging which shows an enhancement in structural interpretation. Furthermore, the results gained from the proposed modeling and imaging approach significantly enhance the bandwidth of the imaged data. Finally, a frequency spectrum shows a recovery of low-frequency from 0 to 60 Hz which is an optimal resolution of seismic imaging.",book:{id:"8361",slug:"applied-geophysics-with-case-studies-on-environmental-exploration-and-engineering-geophysics",title:"Applied Geophysics with Case Studies on Environmental, Exploration and Engineering Geophysics",fullTitle:"Applied Geophysics with Case Studies on Environmental, Exploration and Engineering Geophysics"},signatures:"Yasir Bashir and Deva Prasad Ghosh",authors:null},{id:"37858",title:"Geodynamic and Tectonostratigrafic Study of a Continental Rift: The Triassic Cuyana Basin, Argentina",slug:"geodynamic-and-tectonostratigrafic-study-of-a-continental-rift-the-triassic-cuyana-basin-argentina",totalDownloads:3434,totalCrossrefCites:0,totalDimensionsCites:14,abstract:null,book:{id:"2227",slug:"tectonics-recent-advances",title:"Tectonics",fullTitle:"Tectonics - Recent Advances"},signatures:"Silvia Patricia Barredo",authors:[{id:"147305",title:"Dr.",name:"Silvia",middleName:null,surname:"Barredo",slug:"silvia-barredo",fullName:"Silvia Barredo"}]}],onlineFirstChaptersFilter:{topicId:"654",limit:6,offset:0},onlineFirstChaptersCollection:[],onlineFirstChaptersTotal:0},preDownload:{success:null,errors:{}},subscriptionForm:{success:null,errors:{}},aboutIntechopen:{},privacyPolicy:{},peerReviewing:{},howOpenAccessPublishingWithIntechopenWorks:{},sponsorshipBooks:{sponsorshipBooks:[],offset:0,limit:8,total:null},allSeries:{pteSeriesList:[],lsSeriesList:[],hsSeriesList:[],sshSeriesList:[],testimonialsList:[]},series:{item:{id:"10",title:"Physiology",doi:"10.5772/intechopen.72796",issn:"2631-8261",scope:"Modern physiology requires a comprehensive understanding of the integration of tissues and organs throughout the mammalian body, including the cooperation between structure and function at the cellular and molecular levels governed by gene and protein expression. While a daunting task, learning is facilitated by identifying common and effective signaling pathways mediated by a variety of factors employed by nature to preserve and sustain homeostatic life. \r\nAs a leading example, the cellular interaction between intracellular concentration of Ca+2 increases, and changes in plasma membrane potential is integral for coordinating blood flow, governing the exocytosis of neurotransmitters, and modulating gene expression and cell effector secretory functions. Furthermore, in this manner, understanding the systemic interaction between the cardiovascular and nervous systems has become more important than ever as human populations' life prolongation, aging and mechanisms of cellular oxidative signaling are utilised for sustaining life. \r\nAltogether, physiological research enables our identification of distinct and precise points of transition from health to the development of multimorbidity throughout the inevitable aging disorders (e.g., diabetes, hypertension, chronic kidney disease, heart failure, peptic ulcer, inflammatory bowel disease, age-related macular degeneration, cancer). With consideration of all organ systems (e.g., brain, heart, lung, gut, skeletal and smooth muscle, liver, pancreas, kidney, eye) and the interactions thereof, this Physiology Series will address the goals of resolving (1) Aging physiology and chronic disease progression (2) Examination of key cellular pathways as they relate to calcium, oxidative stress, and electrical signaling, and (3) how changes in plasma membrane produced by lipid peroxidation products can affect aging physiology, covering new research in the area of cell, human, plant and animal physiology.",coverUrl:"https://cdn.intechopen.com/series/covers/10.jpg",latestPublicationDate:"June 20th, 2022",hasOnlineFirst:!0,numberOfPublishedBooks:11,editor:{id:"35854",title:"Prof.",name:"Tomasz",middleName:null,surname:"Brzozowski",slug:"tomasz-brzozowski",fullName:"Tomasz Brzozowski",profilePictureURL:"https://mts.intechopen.com/storage/users/35854/images/system/35854.jpg",biography:"Prof. Dr. Thomas Brzozowski works as a professor of Human Physiology and is currently Chairman at the Department of Physiology and is V-Dean of the Medical Faculty at Jagiellonian University Medical College, Cracow, Poland. His primary area of interest is physiology and pathophysiology of the gastrointestinal (GI) tract, with the major focus on the mechanism of GI mucosal defense, protection, and ulcer healing. He was a postdoctoral NIH fellow at the University of California and the Gastroenterology VA Medical Center, Irvine, Long Beach, CA, USA, and at the Gastroenterology Clinics Erlangen-Nuremberg and Munster in Germany. He has published 290 original articles in some of the most prestigious scientific journals and seven book chapters on the pathophysiology of the GI tract, gastroprotection, ulcer healing, drug therapy of peptic ulcers, hormonal regulation of the gut, and inflammatory bowel disease.",institutionString:null,institution:{name:"Jagiellonian University",institutionURL:null,country:{name:"Poland"}}},editorTwo:null,editorThree:null},subseries:{paginationCount:4,paginationItems:[{id:"10",title:"Animal Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/10.jpg",isOpenForSubmission:!0,editor:{id:"202192",title:"Dr.",name:"Catrin",middleName:null,surname:"Rutland",slug:"catrin-rutland",fullName:"Catrin Rutland",profilePictureURL:"https://mts.intechopen.com/storage/users/202192/images/system/202192.png",biography:"Catrin Rutland is an Associate Professor of Anatomy and Developmental Genetics at the University of Nottingham, UK. She obtained a BSc from the University of Derby, England, a master’s degree from Technische Universität München, Germany, and a Ph.D. from the University of Nottingham. She undertook a post-doctoral research fellowship in the School of Medicine before accepting tenure in Veterinary Medicine and Science. Dr. Rutland also obtained an MMedSci (Medical Education) and a Postgraduate Certificate in Higher Education (PGCHE). She is the author of more than sixty peer-reviewed journal articles, twelve books/book chapters, and more than 100 research abstracts in cardiovascular biology and oncology. She is a board member of the European Association of Veterinary Anatomists, Fellow of the Anatomical Society, and Senior Fellow of the Higher Education Academy. Dr. Rutland has also written popular science books for the public. https://orcid.org/0000-0002-2009-4898. www.nottingham.ac.uk/vet/people/catrin.rutland",institutionString:null,institution:{name:"University of Nottingham",institutionURL:null,country:{name:"United Kingdom"}}},editorTwo:null,editorThree:null},{id:"11",title:"Cell Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/11.jpg",isOpenForSubmission:!0,editor:{id:"133493",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",profilePictureURL:"https://mts.intechopen.com/storage/users/133493/images/3091_n.jpg",biography:"Prof. Dr. Angel Catalá \r\nShort Biography Angel Catalá was born in Rodeo (San Juan, Argentina). He studied \r\nchemistry at the Universidad Nacional de La Plata, Argentina, where received aPh.D. degree in chemistry (Biological Branch) in 1965. From\r\n1964 to 1974, he worked as Assistant in Biochemistry at the School of MedicineUniversidad Nacional de La Plata, Argentina. From 1974 to 1976, he was a Fellowof the National Institutes of Health (NIH) at the University of Connecticut, Health Center, USA. From 1985 to 2004, he served as a Full Professor oBiochemistry at the Universidad Nacional de La Plata, Argentina. He is Member ofthe National Research Council (CONICET), Argentina, and Argentine Society foBiochemistry and Molecular Biology (SAIB). His laboratory has been interested for manyears in the lipid peroxidation of biological membranes from various tissues and different species. Professor Catalá has directed twelve doctoral theses, publishedover 100 papers in peer reviewed journals, several chapters in books andtwelve edited books. Angel Catalá received awards at the 40th InternationaConference Biochemistry of Lipids 1999: Dijon (France). W inner of the Bimbo PanAmerican Nutrition, Food Science and Technology Award 2006 and 2012, South AmericaHuman Nutrition, Professional Category. 2006 award in pharmacology, Bernardo\r\nHoussay, in recognition of his meritorious works of research. Angel Catalá belongto the Editorial Board of Journal of lipids, International Review of Biophysical ChemistryFrontiers in Membrane Physiology and Biophysics, World Journal oExperimental Medicine and Biochemistry Research International, W orld Journal oBiological Chemistry, Oxidative Medicine and Cellular Longevity, Diabetes and thePancreas, International Journal of Chronic Diseases & Therapy, International Journal oNutrition, Co-Editor of The Open Biology Journal.",institutionString:null,institution:{name:"National University of La Plata",institutionURL:null,country:{name:"Argentina"}}},editorTwo:null,editorThree:null},{id:"12",title:"Human Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/12.jpg",isOpenForSubmission:!0,editor:{id:"195829",title:"Prof.",name:"Kunihiro",middleName:null,surname:"Sakuma",slug:"kunihiro-sakuma",fullName:"Kunihiro Sakuma",profilePictureURL:"https://mts.intechopen.com/storage/users/195829/images/system/195829.jpg",biography:"Professor Kunihiro Sakuma, Ph.D., currently works in the Institute for Liberal Arts at the Tokyo Institute of Technology. He is a physiologist working in the field of skeletal muscle. He was awarded his sports science diploma in 1995 by the University of Tsukuba and began his scientific work at the Department of Physiology, Aichi Human Service Center, focusing on the molecular mechanism of congenital muscular dystrophy and normal muscle regeneration. His interest later turned to the molecular mechanism and attenuating strategy of sarcopenia (age-related muscle atrophy). His opinion is to attenuate sarcopenia by improving autophagic defects using nutrient- and pharmaceutical-based treatments.",institutionString:null,institution:{name:"Tokyo Institute of Technology",institutionURL:null,country:{name:"Japan"}}},editorTwo:{id:"331519",title:"Dr.",name:"Kotomi",middleName:null,surname:"Sakai",slug:"kotomi-sakai",fullName:"Kotomi Sakai",profilePictureURL:"https://s3.us-east-1.amazonaws.com/intech-files/0033Y000031QtFXQA0/Profile_Picture_1637053227318",biography:"Senior researcher Kotomi Sakai, Ph.D., MPH, works at the Research Organization of Science and Technology in Ritsumeikan University. She is a researcher in the geriatric rehabilitation and public health field. She received Ph.D. from Nihon University and MPH from St.Luke’s International University. Her main research interest is sarcopenia in older adults, especially its association with nutritional status. Additionally, to understand how to maintain and improve physical function in older adults, to conduct studies about the mechanism of sarcopenia and determine when possible interventions are needed.",institutionString:null,institution:{name:"Ritsumeikan University",institutionURL:null,country:{name:"Japan"}}},editorThree:null},{id:"13",title:"Plant Physiology",coverUrl:"https://cdn.intechopen.com/series_topics/covers/13.jpg",isOpenForSubmission:!0,editor:{id:"332229",title:"Prof.",name:"Jen-Tsung",middleName:null,surname:"Chen",slug:"jen-tsung-chen",fullName:"Jen-Tsung Chen",profilePictureURL:"https://mts.intechopen.com/storage/users/332229/images/system/332229.png",biography:"Dr. Jen-Tsung Chen is currently a professor at the National University of Kaohsiung, Taiwan. He teaches cell biology, genomics, proteomics, medicinal plant biotechnology, and plant tissue culture. Dr. Chen\\'s research interests include bioactive compounds, chromatography techniques, in vitro culture, medicinal plants, phytochemicals, and plant biotechnology. He has published more than ninety scientific papers and serves as an editorial board member for Plant Methods, Biomolecules, and International Journal of Molecular Sciences.",institutionString:"National University of Kaohsiung",institution:{name:"National University of Kaohsiung",institutionURL:null,country:{name:"Taiwan"}}},editorTwo:null,editorThree:null}]},overviewPageOFChapters:{paginationCount:45,paginationItems:[{id:"82135",title:"Carotenoids in Cassava (Manihot esculenta Crantz)",doi:"10.5772/intechopen.105210",signatures:"Lovina I. Udoh, Josephine U. Agogbua, Eberechi R. Keyagha and Itorobong I. Nkanga",slug:"carotenoids-in-cassava-manihot-esculenta-crantz",totalDownloads:6,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"Carotenoids - New Perspectives and Application",coverURL:"https://cdn.intechopen.com/books/images_new/10836.jpg",subseries:{id:"13",title:"Plant Physiology"}}},{id:"82112",title:"Comparative Senescence and Lifespan",doi:"10.5772/intechopen.105137",signatures:"Hassan M. Heshmati",slug:"comparative-senescence-and-lifespan",totalDownloads:8,totalCrossrefCites:0,totalDimensionsCites:0,authors:[{name:"Hassan M.",surname:"Heshmati"}],book:{title:"Mechanisms and Management of Senescence",coverURL:"https://cdn.intechopen.com/books/images_new/10935.jpg",subseries:{id:"11",title:"Cell Physiology"}}},{id:"81796",title:"Apoptosis-Related Diseases and Peroxisomes",doi:"10.5772/intechopen.105052",signatures:"Meimei Wang, Yakun Liu, Ni Chen, Juan Wang and Ye Zhao",slug:"apoptosis-related-diseases-and-peroxisomes",totalDownloads:11,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"The Metabolic Role of Peroxisome in Health and Disease",coverURL:"https://cdn.intechopen.com/books/images_new/10837.jpg",subseries:{id:"11",title:"Cell Physiology"}}},{id:"81723",title:"Peroxisomal Modulation as Therapeutic Alternative for Tackling Multiple Cancers",doi:"10.5772/intechopen.104873",signatures:"Shazia Usmani, Shadma Wahab, Abdul Hafeez, Shabana Khatoon and Syed Misbahul Hasan",slug:"peroxisomal-modulation-as-therapeutic-alternative-for-tackling-multiple-cancers",totalDownloads:4,totalCrossrefCites:0,totalDimensionsCites:0,authors:null,book:{title:"The Metabolic Role of Peroxisome in Health and Disease",coverURL:"https://cdn.intechopen.com/books/images_new/10837.jpg",subseries:{id:"11",title:"Cell Physiology"}}}]},overviewPagePublishedBooks:{paginationCount:11,paginationItems:[{type:"book",id:"7264",title:"Calcium and Signal Transduction",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/7264.jpg",slug:"calcium-and-signal-transduction",publishedDate:"October 24th 2018",editedByType:"Edited by",bookSignature:"John N. Buchholz and Erik J. Behringer",hash:"e373a3d1123dbd45fddf75d90e3e7c38",volumeInSeries:1,fullTitle:"Calcium and Signal Transduction",editors:[{id:"89438",title:"Dr.",name:"John N.",middleName:null,surname:"Buchholz",slug:"john-n.-buchholz",fullName:"John N. Buchholz",profilePictureURL:"https://mts.intechopen.com/storage/users/89438/images/6463_n.jpg",biography:"Full Professor and Vice Chair, Division of Pharmacology, Loma Linda University, School of Medicine. He received his B.S. Degree in Biology at La Sierra University, Riverside California (1980) and a PhD in Pharmacology from Loma Linda University School of Medicine (1988). Post-Doctoral Fellow at University of California, Irvine, College of Medicine 1989-1992 with a focus on autonomic nerve function in blood vessels and the impact of aging on the function of these nerves and overall blood vessel function. Twenty years of research funding and served on NIH R01 review panels, Editor-In-Chief of Edorium Journal of Aging Research. Serves as a peer reviewer for biomedical journals. Military Reserve Officer serving with the 100 Support Command, 100 Troop Command, 40 Infantry Division, CA National Guard.",institutionString:null,institution:{name:"Loma Linda University",institutionURL:null,country:{name:"United States of America"}}}]},{type:"book",id:"6925",title:"Endoplasmic Reticulum",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/6925.jpg",slug:"endoplasmic-reticulum",publishedDate:"April 17th 2019",editedByType:"Edited by",bookSignature:"Angel Català",hash:"a9e90d2dbdbc46128dfe7dac9f87c6b4",volumeInSeries:2,fullTitle:"Endoplasmic Reticulum",editors:[{id:"196544",title:"Prof.",name:"Angel",middleName:null,surname:"Catala",slug:"angel-catala",fullName:"Angel Catala",profilePictureURL:"https://mts.intechopen.com/storage/users/196544/images/system/196544.jpg",biography:"Angel Catalá studied chemistry at Universidad Nacional de La Plata, Argentina, where he received a Ph.D. in Chemistry (Biological Branch) in 1965. From 1964 to 1974, he worked as an Assistant in Biochemistry at the School of Medicine at the same university. From 1974 to 1976, he was a fellow of the National Institutes of Health (NIH) at the University of Connecticut, Health Center, USA. From 1985 to 2004, he served as a Full Professor of Biochemistry at the Universidad Nacional de La Plata. He is a member of the National Research Council (CONICET), Argentina, and the Argentine Society for Biochemistry and Molecular Biology (SAIB). His laboratory has been interested for many years in the lipid peroxidation of biological membranes from various tissues and different species. Dr. Catalá has directed twelve doctoral theses, published more than 100 papers in peer-reviewed journals, several chapters in books, and edited twelve books. He received awards at the 40th International Conference Biochemistry of Lipids 1999 in Dijon, France. He is the winner of the Bimbo Pan-American Nutrition, Food Science and Technology Award 2006 and 2012, South America, Human Nutrition, Professional Category. In 2006, he won the Bernardo Houssay award in pharmacology, in recognition of his meritorious works of research. Dr. Catalá belongs to the editorial board of several journals including Journal of Lipids; International Review of Biophysical Chemistry; Frontiers in Membrane Physiology and Biophysics; World Journal of Experimental Medicine and Biochemistry Research International; World Journal of Biological Chemistry, Diabetes, and the Pancreas; International Journal of Chronic Diseases & Therapy; and International Journal of Nutrition. He is the co-editor of The Open Biology Journal and associate editor for Oxidative Medicine and Cellular Longevity.",institutionString:"Universidad Nacional de La Plata",institution:{name:"National University of La Plata",institutionURL:null,country:{name:"Argentina"}}}]},{type:"book",id:"6924",title:"Adenosine Triphosphate in Health and Disease",subtitle:null,coverURL:"https://cdn.intechopen.com/books/images_new/6924.jpg",slug:"adenosine-triphosphate-in-health-and-disease",publishedDate:"April 24th 2019",editedByType:"Edited by",bookSignature:"Gyula Mozsik",hash:"04106c232a3c68fec07ba7cf00d2522d",volumeInSeries:3,fullTitle:"Adenosine Triphosphate in Health and Disease",editors:[{id:"58390",title:"Dr.",name:"Gyula",middleName:null,surname:"Mozsik",slug:"gyula-mozsik",fullName:"Gyula Mozsik",profilePictureURL:"https://mts.intechopen.com/storage/users/58390/images/system/58390.png",biography:"Gyula Mózsik MD, Ph.D., ScD (med), is an emeritus professor of Medicine at the First Department of Medicine, Univesity of Pécs, Hungary. He was head of this department from 1993 to 2003. His specializations are medicine, gastroenterology, clinical pharmacology, clinical nutrition, and dietetics. His research fields are biochemical pharmacological examinations in the human gastrointestinal (GI) mucosa, mechanisms of retinoids, drugs, capsaicin-sensitive afferent nerves, and innovative pharmacological, pharmaceutical, and nutritional (dietary) research in humans. He has published about 360 peer-reviewed papers, 197 book chapters, 692 abstracts, 19 monographs, and has edited 37 books. He has given about 1120 regular and review lectures. He has organized thirty-eight national and international congresses and symposia. He is the founder of the International Conference on Ulcer Research (ICUR); International Union of Pharmacology, Gastrointestinal Section (IUPHAR-GI); Brain-Gut Society symposiums, and gastrointestinal cytoprotective symposiums. He received the Andre Robert Award from IUPHAR-GI in 2014. 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