Measurement of frequency decrease in Aβ40 aggregation by V-D2 on performing QCM 60 min later.
\r\n\t
",isbn:"978-1-83969-164-5",printIsbn:"978-1-83969-163-8",pdfIsbn:"978-1-83969-165-2",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"918540a77975243ee748770aea1f4af2",bookSignature:"Dr. Aakash Goyal",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/9651.jpg",keywords:"GWAS, Cereals, Breeding, Disease Resistance, Wheat, Rice, Maize, Drought Tolerance, Genetics, Production, Quality, Yield",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"October 21st 2020",dateEndSecondStepPublish:"December 4th 2020",dateEndThirdStepPublish:"February 2nd 2021",dateEndFourthStepPublish:"April 23rd 2021",dateEndFifthStepPublish:"June 22nd 2021",remainingDaysToSecondStep:"3 months",secondStepPassed:!0,currentStepOfPublishingProcess:4,editedByType:null,kuFlag:!1,biosketch:"Elected fellow member of the International College of Nutrition (FICN) and Society of Applied Biotechnology (FSAB) with research experience at Agriculture and Agri-Food Canada, Bayer Crop Science, ICARDA, InnoTech Alberta, and Palm Gardens Inc.",coeditorOneBiosketch:null,coeditorTwoBiosketch:null,coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"97604",title:"Dr.",name:"Aakash",middleName:null,surname:"Goyal",slug:"aakash-goyal",fullName:"Aakash Goyal",profilePictureURL:"https://mts.intechopen.com/storage/users/97604/images/system/97604.jpg",biography:"Aakash Goyal was born in India, and graduated from MDU, Ajmer (Biology) in 1999, then obtained Master’s in Biotechnology in 2002 from GJU, Hissar specialization in Plant biotechnology & molecular breeding, and PhD. in Genetics and Plant Breeding in 2007 from CCSU, Meerut India, specialization in Wheat Breeding. After completion of PhD, he obtained NSREC Visiting Fellowship (in 2008) and thus, joined the wheat and triticale breeding program at Lethbridge Research Center, Agriculture and Agri Food Canada (AAFC), Lethbridge, AB., Canada. In 2012, he achieved a position as a Wheat Breeder for Bayer Crop Science, Saskatoon, Canada. In 2014 he had the honor to obtain Senior Research Scientist position with International Center of Agriculture Research in Dry Areas (ICARDA). In 2017, he moved back to Canada and joined as Native Plant Research Scientist with InnoTech Alberta. In November 2019 he joined as an Agriculture Specialist with Palm Gardens Inc. to help in breeding and cultivation of Cannabis. In this time (2002-2020), he has published nine Books and 50 research papers, reviewed articles, book chapters and book reviews. He is also an elected fellow member of International College of Nutrition (FICN) and Society of Applied Biotechnology (FSAB).",institutionString:"Palm Gardens Inc. Canada",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"2",totalChapterViews:"0",totalEditedBooks:"3",institution:null}],coeditorOne:null,coeditorTwo:null,coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"5",title:"Agricultural and Biological Sciences",slug:"agricultural-and-biological-sciences"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"259492",firstName:"Sara",lastName:"Gojević-Zrnić",middleName:null,title:"Mrs.",imageUrl:"https://mts.intechopen.com/storage/users/259492/images/7469_n.png",email:"sara.p@intechopen.com",biography:"As an Author Service Manager my responsibilities include monitoring and facilitating all publishing activities for authors and editors. 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by",editors:[{id:"19816",title:"Prof.",name:"Alexander",surname:"Kokorin",slug:"alexander-kokorin",fullName:"Alexander Kokorin"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"57",title:"Physics and Applications of Graphene",subtitle:"Experiments",isOpenForSubmission:!1,hash:"0e6622a71cf4f02f45bfdd5691e1189a",slug:"physics-and-applications-of-graphene-experiments",bookSignature:"Sergey Mikhailov",coverURL:"https://cdn.intechopen.com/books/images_new/57.jpg",editedByType:"Edited by",editors:[{id:"16042",title:"Dr.",name:"Sergey",surname:"Mikhailov",slug:"sergey-mikhailov",fullName:"Sergey Mikhailov"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"51790",title:"Vitamin D Affects Neuronal Peptides in Neurodegenerative Disease: Differences of V-D2 and V-D3 for Affinity to Amyloid-β and Scrapie Prion Protein In Vitro",doi:"10.5772/64508",slug:"vitamin-d-affects-neuronal-peptides-in-neurodegenerative-disease-differences-of-v-d2-and-v-d3-for-af",body:'\nRecently, involvement of Vitamin D (V-D) in cognitive impairment is reported.
\nV-D is a secosteroid and occurs in two distinctive major forms: Vitamin D2 (V-D2) and Vitamin D3 (V-D3). V-D3 is a 27-carbon derivative of cholesterol, and V-D2 is a 28-carbon derivative from plant ergosterol. The structure of V-D2 differs from V-D3 by containing an extra methyl group and a double bond between carbon 22 and 23 (Figure 1). Both V-D derivatives appear to have similar biological effects in humans [1, 2]. V-D3 is about four times as potent as V-D2 [3]. Interestingly, V-D2 is a naturally occurring V-D form derived from a fat extract of yeast by the exposure to UV light, and the metabolites were not detectable in the blood of vertebrates such as humans, unless administered from an external source [3, 4]. Thus, V-D2 is not synthesized in vivo and is regarded as a supplement. The metabolites derived from V-D2 are not equivalent to those for V-D3 [5]. In contrast to V-D2, V-D3 is the naturally synthesized within the skin and oils of fur. Although both microsomal and mitochondrial 25-hydroxylases act on V-D3, they do not act on V-D2 [4, 6, 7], and furthermore the V-D binding protein shows lower affinity for V-D2 than V-D3 and its metabolites [8]. Currently, clinical applications of V-D for immunosuppression and reduction of pro-inflammatory immune pathways demonstrate that V-D is a prosteroid hormone rather than a vitamin [9, 10]. V-D cross blood-brain barrier by passive diffusion and enter the cerebrospinal fluid and brain. The beneficial effects in reducing the relapse risk in multiple sclerosis through its immune-regulatory effects were reported [11].
\nStructural differences between Vitamin D2 and Vitamin D3.
Recent epidemiologic studies report V-D3 deficiency as a risk factor of cardiovascular disease including cardiac hypertrophy, myocardial remodeling developed to heart failure (HF) [12, 13] and some prospective studies report the relationship between hypovitaminosis-D and an increased risk of cognitive decline in elderly population [14] and suggested that supplementation of V-D could prevent the cognitive disorders [15–17], and its effects for the clearance of aggregated amyloid-β (Aβ) in AD brain [18].
\nIn this chapter, we present the different binding affinity of V-D2 and V-D3 to amyloidogenic protein in brain: Aβ and prion protein.
\nAD and prion diseases are neurodegenerative diseases in brain and cause dementia. AD is the most common case of senile dementia and the number of AD patients is increasing and recent study shows that 46.8 million of AD patients live in the world and it is estimated to reach 131.5 million by 2050 [19]. It is featured by memory loss, deterioration of cognitive and behavioral process, and diminished social life. These symptoms do not improve and progress with life time.
\nThe main pathological hallmark with AD patients is the senile plaque in the brain [20]. Extracellular accumulation of insoluble Aβ protein is the main component of the plaque that induces synaptic dysfunction and neuronal loss resulting in progressive dementia [21]. The Aβ is composed of 39–43 amino acids, naturally produced by proteolytic cleavage of integral membrane protein, 100–135 kDa amyloid precursor protein [22]. The majority of the secreted Aβ alloform includes the C-terminal Aβ40 and Aβ42. Quantitative analyses have shown that, on average, 60% of all plaques contain Aβ42 and 31% contain Aβ40 [23]. The misfolding and aggregation of Aβ and tau proteins are two principal aggregating proteins in AD brain [24, 25]. Growth of the fibrils occurs by assembly of the Aβ seeds into intermediate protofibrils, and self-associates to form mature fibers [26]. This multistep process may be influenced at various stages by factors that promote Aβ fiber formation and aggregation, and the seeding of Aβ40 oligomers is the initial step of the process [27, 28].
\nThe emergence of a prion disease in cattle is known as bovine spongiform encephalopathy (BSE) and a possible transmission to humans by the exposure to BSE has been suggested [29, 30]. Gerstmann-Straussler-Scheinker disease and Creutzfeldt-Jacob are well-known naturally occurring prion diseases in human and they are transmissible and fatal. The main event contributing to the pathogenesis of prion disease is the conversion of the cellular prion protein (PrPc) into scrapie prion protein (PrPsc), which is a protease-resistant, insoluble protein [31, 32]. PrPc is predominantly expressed in neurons, and attached to extracellular space of plasma membrane through a glycophosphatidylinositol. It is a sialoglycoprotein with a molecular weight of approximately 33–35 kDa [33, 34]. Studies have shown that PrPc(90–231), which is N-terminal truncated fragments of PrPc and corresponds to the core of the protease K (PK) resistant prion protein, preserve the pathogenic features of PrPsc [35, 36]. Gerstmann-Straussler-Scheinker disease and Creutzfeldt-Jacob disease are caused by mutations in the PrP gene [37] and the mutations directly link to conformational conversion from PrPc to PrPsc and amplification of PrPsc without exogenous PrPsc [38, 39], and the infectivity can be explained by the direct PrPsc-PrPc interaction [40]. In vitro generation of infectious PrPsc has demonstrated the protein-only hypothesis of prion propagation [41, 42]. Many reports have suggested that the multistep process of conversion from PrPc into PrPsc includes an oligomerization/polymerization step [43, 44]. The oligomerization or molten-globule state is a preliminary step required for the formation of insoluble protein in the brain like that of Aβ aggregates in AD brain, and soluble oligomers appear to be more cytotoxic than mature aggregates [45].
\nQuartz-crystal microbalance (QCM) measurement is a highly sensitive mass-measuring system [46, 47]. The instrument is equipped with a 27 MHz QCM plate at the bottom with a stirring bar. Changes of frequency are calculated by Sauerbrey’s equation [48] as below.
\nWe applied Sauerbrey’s equation for the QCM in the air phase:
where ΔF is measured frequency change (Hz), Δm is mass change, F0 is fundamental frequency of the quartz-crystal, A is an electrode area, ρq is density of quartz-crystal, and μq is the shear modulus of quartz-crystal.
\nThe equation indicates that a 0.61 ng/cm2 increase in mass means a −1 Hz decrease in frequency. The change of frequency is proportional to that of mass.
\nThe change of mass in Aβ40 with V-D2 or V-D3 was determined [49]. A significant decrease in frequency started after 15 min upon addition of Aβ40 to the V-D2 solution, and found that the frequency decrease depends on both V-D2 concentration and incubation time. Aβ40-V-D2 complex formation occurs in solution and accelerated after 15–60 min later (Figure 2a). After 60 min, the calculated Aβ40 molecules aggregated by an Aβ40 was 4.21394 e19 at 0.1 M of V-D2, 6.74725 e19 at 0.5 μM of V-D2, and 8.85697 e19 at 1.0 μM of V-D2 (Table 1). In case of V-D3, however, no considerable decrease in frequency upon Aβ40 addition was observed (Figure 2b). These results show a different potential of V-D2 and V-D3 for Aβ40 oligomerization in vitro.
\nQuartz-crystal microbalance pattern for Aβ40 aggregation with V-D derivatives. Typical real-time monitoring of Aβ40 (12 μM) aggregation with V-D2 at the concentrations of 0, 0.1, 0.5, and 1 μM (a) or with V-D3 at the concentrations of 0, 0.5, and 1 μM (b) in quartz-crystal microbalance measurements. The changes of frequency of Aβ40 with V-D2 or V-D3 for 60 min are shown. The data are representative of three experiments. Total amount of Aβ40 aggregates with V-D2 (a). V-D2 induced potential dose-dependent Aβ40 aggregates. Total amount of Aβ40 aggregates with V-D3 (b). V-D3 did not induce Aβ40 aggregation after 60 min.
V-D2 (μM) | \n−ΔF (Hz) | \nΔm (ng/cm2)a | \nΔn (atoms/cm2)b | \n
---|---|---|---|
Control* | \n3111 ± 44 | \n190 | \n2.63507 × 1019 | \n
0.1 | \n498 ± 6 | \n304 | \n4.21394 × 1019 | \n
0.5 | \n798 ± 332 | \n487 | \n6.74725 × 1019 | \n
1 | \n1048 ± 252 | \n639 | \n8.85697 × 1019 | \n
Measurement of frequency decrease in Aβ40 aggregation by V-D2 on performing QCM 60 min later.
* Direct binding of Aβ40 peptide to the Au electrode without V-D2.
a A 1 Hz decrease in frequency results in a 0.61 ng/cm2 increase in mass.
b Calculation using a molecular weight of 4331 for Aβ40.
Data are presented as mean ± SD values for three independent experiments.
Aβ40 in artificial cerebrospinal fluid without V-D as a control induced weak self-oligomerization and V-D3 induced no enhancement to the control, however V-D2 enhanced potent oligomerization for Aβ40 as Figure 3(a–c) [49].
\nElectron microscopic observation for Aβ40 without or with V-D2 or V-D3. Aβ40 without V-D as a control (a), Aβ40 with V-D2 (b), and Aβ40 with V-D3 (c). Aβ40 in the photo indicates 100 nm for (a), (b), and (c).
Amyloid fibers are ordered β-sheet-rich proteins. Benzothiazole dye, Thioflavin-T (Th-T) is used to probe amyloid fibril formation due to specific noncovalent interactions that yield strong fluorescence upon binding [50]. Aβ40 showed a peak at 490 nm, indicating β-sheet formation [51]. V-D2 increased peak intensity at 490 nm dose-dependently, indicating that V-D2 facilitates β-sheet formation in Aβ40. The V-D3 do not increase peak fluorescent intensity at 490 nm, indicating that V-D3 facilitate no β-sheet formation in Aβ40 peptide (Figure 4) [49].
\nTh-T fluorescence monitored β-sheet formation of Aβ40 in the presence of V-D2, V-D3. (a) V-D2 facilitates strong β-sheet formation in Aβ40 and (b) V-D3 induced weak β-sheet formation in Aβ40. Y-axis indicates relative fluorescence units (RFUs). Data represent the mean ± SD values (bar) for three independent experiments. *p < 0.01, **p < 0.001 vs. without V-D derivatives.
In silico docking analysis at the tertiary structure level by Molecular Operating Environment (MOE) software indicates the different interactions between V-D2 or V-D3 and Aβ40 peptide. The calculated minimum energy for V-D2 was −40.36 kcal/mol and for V-D3, −12.46 kcal/mol; for cholesterol, the calculated minimum energy was −25.89 kcal/mol. The result showed that both V-D2 and V-D3 bind common amino acid residues 7–8, 11–12, and 15–16 of Aβ40, and the C22–C23 double bond in V-D2 stacks with the benzene ring of Phe19 in Aβ40, whereas V-D3 has no double bonds and showed no stacking (Figure 5) [49].
\nDocking simulation between Aβ40 and V-D2 or V-D3. Purple indicates hydrophilic residues and green indicates hydrophobic residues in Aβ40 (backbone). The double bonds (red arrow) of V-D2 stack on the benzene ring of Phe19 in Aβ40. The minimum energy between Aβ40 and V-D2 was −40.36 kcal/mol, that between Aβ40 and V-D3 was −12.46 kcal/mol.
Affinity of V-D to PrP, as measured using the Biacore system. (a) The interaction between PrPc(90–231) and V-D2 showed high binding affinity, with a Ka of 6.17 e8 and a Kd of 1.62 e-9. (b) The interaction between PrPc(90–231) and V-D3 showed no binding affinity. (c) The interaction between PrPc(90–231) and V-D2, after saturating with the anti-3F4 mAb.
A Biacore assay indicates a high affinity of V-D2 for human recombinant cellular prion protein (Hu-rPrPc)(90–231), and after saturating PrPc(90–231) with the anti-3F4 antibody, specific for amino acid fragment 109–112 of PrPc, V-D2 binding to PrPc(90–231) was decreased (Figure 6a and c), indicating that within the 3F4 epitope, PrPc(90–231) was responsible for the interaction with V-D2. However, V-D3 showed no affinity for PrPc(90–231) (Figure 6b), The binding kinetics of V-D2 to Hu-rPrPc(90–231) was shown in Table 2 [52].
\nLigand | \nAnalyte | \n\nK\na (1/M) | \n\nK\nd (M) | \n
---|---|---|---|
\n | V-D2 | \n6.17 e8 | \n1.62 e-9 | \n
PrPc(90–231) | \nV-D3 | \nND* | \nND* | \n
\n | 3F4 + V-D2 | \n1.12 e8 | \n8.95 e-9\t | \n
Binding kinetics of V-D2 and V-D3 to Hu-rPrPc(90–231).
* ND, not detected.
Reactivity of mAbs against PrPc with V-D2 by ELISA. The 3F4 epitope on PrPc was affected by V-D2 in a dose-dependent manner. The blue line indicates signals for PrPc(90–231) and the red line f PrPc(101–130).
The responsible fragment within Hu-rPrPc(90–231) that was affected by V-D2 was determined by ELISA. The reactivity of the 3F4 antibody to PrPc(90–231) that was incubated with V-D2 showed decreasing signals toward PrPc(90–231) bound with V-D2 in a dose-dependent manner (Figure 7) [52]. These results confirm the observation by Biacore assay (Figure 6).
\nThe Aβ hydrophobic core 16–20 (KLVFF) was the minimum sequence required in a binding screen of full-length and trimeric to decameric peptides spanning the entire Aβ40 sequence. Alanine substitution demonstrated that Lys16, Leu17, and Phe20 are critical for this interaction [53]. The stereospecific binding of KLVFF to the homologous Aβ sequence was later confirmed as the product of specific hydrophobic and electrostatic interactions. Controlling amyloid β-peptide fibril formation with protease-stable ligands was reported [53]. The sequences of Aβ (9–14): GYEVHH and Aβ (17–21): LVFFA, are responsible to pH-shifts [54] and thermal-induced structural transformation from α-helix/random coil to β-sheet in Aβs were Aβ (16–23) and Aβ (17–24) [55]. The conformational transition from Aβ40 monomer to oligomers may occur in response to small chemical compounds and may be dependent on specific Aβ40 sequences. The key amino acid of Aβ40 for interaction with V-D2 is the Phe at a position 19, and it is around the sequences responsible to pH shifts and thermal stress [54, 55].
\nIn case of PrPc(90–231), the sequence of PrPc(107–112): TNMKHM is pH dependent [56], and it contains PrPc(109–112), the responsible sequence for the interaction with V-D2.
The C22–C23 double bond contained in V-D2 structure may influence the conformational flexibility of the molecule through allylic strain and rigidity of the double bond against rotation [57, 58]. Therefore, we hypothesize that conformational restriction by the double bond in the V-D2 side chain facilitated binding of V-D2 to the recognition site of Aβ40 and PrPc(90–231).
\nWe detected V-D2-induced Aβ40 oligomerization by QCM, and electron microscopic observation demonstrated the potential of V-D2 for Aβ40 oligomerization through β-sheet formation as revealed by Th-T study. V-D2-mediated Aβ40 oligomerization occurs through interaction between the Phe19 benzene ring of Aβ40 and the C22–C23 double bond of V-D2. In case of prion, the fragment of V-D2 binding to PrPc(90–231) is around 3F4 epitope, 109–112 amino acid in PrPc(90–231). These fragments are involved in the sensitive fragments to pH shifts and thermal stress. The binding of V-D2 to amyloidogenic peptides in brain might give some insights to oligomerization of these peptides in the brain.
\nMedications are chemical substances used to treat, cure, prevent, or diagnose a disease or to promote well-being. An adverse drug reaction is defined by WHO as a response to a drug which is noxious and unintended, and which occurs at doses normally used in man for the prophylaxis, diagnosis, therapy of diseases or for the modification of physiological function. Several medications can cause adverse effects in the periodontium. The most common are the gingival enlargement, inflammation, pigmentations, gingival bleeding and osteonecrosis [1]. Gingival overgrowth (GO) or enlargement is a condition is characterized by an increase in the size of gingiva subsequent to the increase in extracellular tissue volume. Gingival overgrowth is a side effect of several medications used by patients have the capability to cause adverse effects in the oral cavity and periodontal tissues [2]. Though many medications have marked effects on the periodontal tissues and these adverse reactions are well documented, many have been described only as isolated case series or reports [2]. It is important for the clinician to obtain a complete record of the medications the patient takes, including prescription drugs and over-the-counter drugs. This will help the clinician to diagnose and manage the adverse effects in the periodontal tissues.
\nThe main drugs associated with GO can be divided into three categories such as anticonvulsants, calcium channel blockers, and immunosuppressants. Few isolated incidences of GO associated with antibiotics and sulphonamides were also reported. Though these drugs have different pharmacologic effect and targets, all of them seem to act similarly on the gingival connective tissue as a secondary target, leading to common clinical and histopathological changes. The gingival overgrowth (GO) is consequent to the alteration of the host tissue response, resulting in an increase in collagen synthesis and cellular changes within the connective tissue. The prevalence of gingival overgrowth varies with different medications, with a reported rate of 50% for phenytoin (anticonvulsant), 25–30% for cyclosporine (immunosuppressant), 5–20% for nifedipine and 3% for amlodipine (CCBs) [2]. The drug associated gingival overgrowth is three times more prevalent among men and can be attributed to the effect of testosterone on fibroblast proliferation and collagen stimulus [3].
\nThe GO appears normally within 1–3 months after administration of these medications (Table 1). The gingival enlargement may appear inflamed or more fibrotic depending on the degree of inflammation. Normally the GO is confined to the attached gingiva which might occasionally extend coronally. The enlarged gingiva produces esthetic changes and its clinical symptoms include tenderness, bleeding, interference with speech, dental occlusion problems, and enhanced susceptibility to periodontal diseases [4, 5, 6].
\nDrugs/groups | \nIncidence/prevalence | \nReferences | \n
---|---|---|
Anticonvulsants | \n||
Phenytoin | \n13% | \n[17] | \n
\n | 50.3% | \n[18] | \n
\n | 57% | \n[19] | \n
\n | 40% | \n[20] | \n
\n | 50–60% | \n[21] | \n
\n | 53% | \n[22] | \n
Sodium valproate | \nRare | \n[22] | \n
Vigabatrin | \nRare | \n[23, 24] | \n
Carbamazepine | \nNone | \n[22] | \n
Immunosuppressants | \n||
Cyclosporines | \n10–85% | \n[25] | \n
\n | 30% | \n[26] | \n
\n | 8–70% | \n[27] | \n
\n | 25–81% | \n[8] | \n
\n | 22.4% | \n[28] | \n
Tacrolimus | \n14.1% | \n[28] | \n
Calcium channel blockers | \n||
Nifedipine | \n6.3% | \n[29] | \n
\n | 50.8% | \n[30] | \n
\n | 83% | \n[31] | \n
Diltiazem | \n20% | \n[31] | \n
Verapamil | \n4–19% | \n[32, 33] | \n
Amlodipine | \n3% | \n[34, 35] | \n
Felodipine | \nRare | \n[36] | \n
Medications causing drug induced gingival overgrowth (DIGO).
Histologically, the drug-induced gingival overgrowth is indistinguishable from other types of gingival enlargement. The enlargement of the gingival tissue occurs as a result of accumulation of extracellular matrix (ECM), although the pathogenesis remains multifactorial. Age, genetic predisposition, pharmacokinetic variables, drug-induced alterations in gingival connective tissue homeostasis, inflammatory changes, drug-induced action on growth factors, etc. are some of the factors that influences the occurrence and severity of the gingival overgrowth.
\nGenetic factors are important in the pathogenesis of drug associated gingival overgrowth. The drugs are metabolized by cytochrome p450 enzymes, which are characterized by high genetic variability. Research on genes responsible for HLA leukocyte antigen coding confirmed the theory of HLA-DR2 antigen influence, which is found much more commonly in patients with moderate or severe drug-induced gingival overgrowth than HLA-DR1 [7]. The drug variables such as dosage, duration of therapy and concentration of drug in plasma and local fluids, like gingival crevicular fluid and saliva, play an important role in DIGO [8].
\nThe exact mechanism behind the pathogenesis of drug-induced gingival overgrowth is not yet fully understood. Each medication has got separate impacts on the range of cytokines and growth factors involved in connective tissue metabolism. Studies revealed that the molecular markers and clinical features of gingival overgrowth differ depending on the drugs. The cytokine and growth factor balances are altered in tissues with GO, including connective tissue growth factor (CTGF), a member of the interesting CCN (cysteine-rich angiogenic protein 61) family of factors [3, 9, 10].
\nCytokine dependent alterations in extracellular matrix metabolism appear to be of functional importance to gingival overgrowth. Abnormal differentiation of cells, resulting in accumulation of fibroblasts with a pathologic range of proliferative and synthetic phenotypes, could result from deregulated cytokines. The unique metabolic aspects of gingival extracellular matrix metabolism; and a greater understanding of interactions between and among medications, the innate and acquired immune response, cytokines and growth factors, and gingival epithelial and connective tissue cells providing more detailed molecular and mechanistic information need to be elucidated [3, 11].
\nHistologically, slight to moderate hyperkeratosis, thickening of the spinous layer, fibrosis of underlying connective tissue with fibroblastic proliferation, increase in the number of capillaries with slight chronic perivascular inflammation is seen. Excessive accumulation of extracellular matrix like collagen with varying amounts of inflammatory infiltrates, predominantly plasma cells are seen. Fibroblastic proliferation may not be evident. Plasma cells are the principal type of infiltrating inflammatory cell. Parakeratinized epithelium of variable thickness covers the connective tissue stroma. The epithelial ridges may penetrate deep into the connective with columns of interspersed collagen fibers [12].
\nThe management of medication induced gingival overgrowth depends on the degree of progression of the disease. Withdrawal or substitution of medication is one of the methods that might resolve the gingival overgrowth. However, not all patients respond to this mode of treatment especially those with long standing gingival enlargement. Professional debridement with scaling and root planning as needed has been shown to offer some remission of the gingival overgrowth in patients. Since the anterior labial gingiva is frequently involved, surgery is commonly performed for esthetic reasons. The classical surgical approach has been the external bevel gingivectomy. However, a total or partial internal gingivectomy approach has been suggested as an alternative. This approach has the benefit of limiting the large denuded connective tissue wound and thereby minimizing postoperative pain and bleeding [13].
\nThe surgical methods include traditional scalpel gingivectomy and periodontal flap surgery. Electrocautery may be used in difficult cases, children, or where the gingiva is fragile and likely to bleed. Excision using laser provides a superior incision margin and improved wound healing due to a coagulated layer along the incision, as well as a reduced incidence of scarring. CO2 laser is very effective in surgery of soft tissues with high water content like the gingiva. Blood vessels up to a diameter of 0.5 mm can be sealed effectively and provides a dry field for better visibility of the surgical field. A laser is preferred over the scalpel as it has strong bactericidal and hemostatic effects [14, 15]. A combined non-surgical and surgical therapy with drug substitution is the most common treatment approach in the management of medication induced gingival overgrowth [16]. In most cases, conservative methods such as professional oral hygiene maintenance, topical anti-inflammatory and antibacterial drugs and a meticulous oral hygiene measures by the patient. Surgical excision is used in cases of where the gingival overgrowth interferes with food intake, causing difficulties in speech and maintaining oral hygiene. Surgical excision is more reliable as it eliminates the hyperplastic tissue and promotes plaque control as well as improves the esthetics.
\nPhenytoin is an anticonvulsant prescribed for the control of epilepsy and neuralgias. In the present day, phenytoin is not usually prescribed as a first line drug for the management of epilepsy due to the availability of a wide range of newer, more effective anticonvulsant drugs with fewer side effects. The prevalence of drug-induced gingival overgrowth in patients taking phenytoin is reportedly between 15% and 60% [17]. Phenytoin, or its metabolites, probably acts directly on high activity fibroblasts leading to the high levels of production of collagen in the presence of inflammation. This results in gingival enlargement, characteristically originating principally from the interdental papillae (Figure 1). The amount or degree of severity of the overgrowth is not related to the dose of the drug. Presence of plaque and gingival inflammation, serum concentrations of the drug are factors which increases the risk of phenytoin-induced gingival overgrowth [37].
\nA case of phenytoin induced gingival overgrowth.
The management of this overgrowth is based on obtaining optimal control of plaque. Where the enlargement is unsightly and disfiguring, or even interfering with chewing, the over-growths should be removed. Gingivectomy appears to be the simplest and best way of achieving good gingival contour as a post-operative result. But optimal plaque control post-operatively is the most important determinant of success. Recent research work suggests that the use of chlorhexidine, especially brushing daily using the gel, can be of valuable assistance in controlling plaque and hence in controlling the overgrowths in the post-surgical phase.
\nCyclosporin (CsA) is a cyclic polypeptide with potent immunosuppressive activity used widely to prevent organ transplant rejection and also in the treatment of autoimmune diseases [38, 39]. CsA selectively suppresses helper T-cell function and modulates the network of inflammatory cytokines. However, cyclosporin is associated with several untoward effects like nephrotoxicity, hepatotoxicity, hirsutism and gingival overgrowth [40, 41]. Gingival overgrowth is one of the common side effects of CsA treatment, observed in 13–81% of the patients [6, 39]. The prevalence of gingival overgrowth associated with CsA averages around 30%, with reported rates ranging from 10 to 85% [25]. Studies have shown certain degree of association between GO and potential risk factors, such as age, genetic susceptibility, pharmacokinetic variables, plaque-related inflammation and immunological changes [42, 43, 44]. Epidemiological studies have reported wide variation of its occurrence and it accounts for more than 70% of the transplant recipients [4, 45]. The severity of gingival overgrowth is often associated with its prolonged use and further influenced by bacterial plaque and local irritants (Figure 2) [46]. The use of other medication, such as calcium channel blockers along with CsA increases the prevalence of gingival overgrowth and subsequently the risks [11]. The condition can interfere with the mastication, speech and oral hygiene maintenance and has a psychological impact in the affected individual [5].
\nA case of cyclosporin A induced gingival overgrowth.
The most prominent pathologic manifestation of the gingival overgrowth is an excessive accumulation of extracellular matrix, predominantly type I collagen. Many studies have shown increased transcriptional and translational levels of type I collagen in both tissue and fibroblast cultures derived from CsA-induced gingival overgrowth [9, 10, 47]. Though the exact mechanism is not clearly understood, studies also have shown increased expression of specific cytokines, especially transforming growth factor-beta (TGF-β), in drug-induced gingival overgrowth. This suggests that TGF-β, an inflammatory mediator that regulates cell proliferation and differentiation, plays a role in enlarging the extracellular matrix in hyperplastic gingival tissue [48].
\nThe management of cyclosporin associated gingival overgrowth includes removal of local irritants and plaque and maintenance of adequate oral hygiene. Invasive procedures, such as gingivectomy is done in severe cases [49]. Currently the use of antibiotics has shown reduction in the GO associated with the drug usage. Azithromycin, a semi synthetic antibiotic, derived from the macrolide erythromycin has shown reduction in gingival overgrowth [50]. Roxithromycin, a macrolide antibiotic with similar characteristics of azithromycin, is also found to be effective in the reduction of gingival overgrowth in renal transplant recipients on CsA [25]. Gingival overgrowth can be prevented by intensive plaque-control practices including meticulous brushing, although critically ill patients receiving CsA may not be the ideal candidates for such intensive procedures. A combination of chlorhexidine or normal saline mouth rinses and mechanical cleaning was found to be effective in controlling the management of such patients [51, 52].
\nDrugs including diuretics, alpha and beta blockers, angiotensin converting enzyme inhibitors, angiotensin II type 1 receptor blockers and calcium channel blockers (CCBs) have been used to manage hypertension [53]. They are administered either alone or in combination, depending on the needs of the patient. The calcium channel blockers are the most frequently prescribed antihypertensive agents which is comprised of two subclasses, dihydropyridines and non-dihydropyridines. Although their mechanism of action is the same, they have varied pharmacological effects. While the dihydropyridines are potent vasodilators, the non-dihydropyridines produce more negative inotropic effects. The dihydropyridines such as nifedipine, amlodipine and felodipine are significantly associated with gingival overgrowth. The non-dihydropyridines such as diltiazem and verapamil are less commonly associated with gingival enlargement [54].
\nNifedipine, a drug that belongs to a pharmacological agent group known as calcium channel blocker was introduced in 1972 and has been used widely in the management of hypertension and angina pectoris. Lederman et al. [55] was the first to describe nifedipine-induced gingival overgrowth in patients treated with this drug. The prevalence of nifedipine-induced gingival overgrowth is between 30 and 50% and was found to be 3 times likely to develop in males [29]. The overgrowth appears 1–9 months after administration of the drug and the most common sites affected included the labial anterior gingiva of both jaws [56, 57]. A multifactorial pathogenesis has been suggested including environmental, genetic, immunological and inflammatory factors [58]. The interdental papilla becomes more grossly enlarged followed by the marginal and the attached gingiva (Figure 3). Presence of gingival periodontal disease and dental plaque has been reported as significant risk factors in the development of gingival enlargement. Several hypotheses have been put forward to explain the phenomena of the gingival overgrowth. The interaction between nifedipine and gingival fibroblasts contain increased sulfated mucopolysaccharides which are precursors of ground substance, leading to the overproduction of collagen and extracellular ground substance [59]. A genetically specific predetermined subpopulations of fibroblasts are identified which are sensitive to nifedipine and cause an increase in the production of collagen [60]. The dose of nifedipine is important and it was found that its presence in gingival crevicular fluid is 15–316 times higher than plasma. The higher concentration of nifedipine in the gingival crevicular fluid could increase the severity of gingival enlargement.
\nA case of nifedipine induced gingival overgrowth.
Amlodipine is a third-generation dihydropyridine calcium channel blockers (CCB) that is used in the management of both hypertension and angina. The prevalence of gingival overgrowth associated with amlodipine is between 1.7% and 3.3% [35]. Though the etiopathology of this adverse reaction is not clearly understood, mechanisms such as inflammatory and non-inflammatory pathways have already been hypothesized. The non-inflammatory mechanisms involves a defective collagenase activity due to decreased uptake of folic acid, blockage of aldosterone synthesis in the adrenal cortex and consequent increase in Adrenocorticotropic hormone level, and up-regulation of keratinocyte growth factor [61]. The inflammatory pathway develops as a result of direct toxic effects of concentrated drug in gingival crevicular fluid and bacterial plaques leading to the up-regulation of several cytokine factors such as transforming growth factor-beta (TGF-β) [62].
\nThe gingival overgrowth normally begins at the interdental papillae and is more frequently found in the anterior segment of the labial surfaces. Subsequently gingival lobulations that develop might appear as inflamed or fibrotic in nature depending on the degree of contributing factors (Figure 4). Normally the fibrotic enlargement is confined to the attached gingiva which might advance coronally and interfere with esthetics, mastication, or speech [63]. Management of amlodipine induced gingival overgrowth includes substitution of the drug and controlling the other risk factors with meticulous mechanical and chemical plaque control. Surgical management of the overgrowth is advised in cases to accomplish an esthetic and functional outcome [64].
\nA case of gingival overgrowth in a patient on amlodipine.
Verapamil is an effective preventive agent in both episodic and chronic cluster headache. Gingival overgrowth is an infrequent adverse effect of Verapamil and a prevalence rate of around 4.2% has been reported [33]. Histologically, verapamil induced gingival enlargement shows a highly vascular connective tissue, acanthotic and thickened epithelium with long rete pegs containing dyskeratotic pearls, and varying amounts of subepithelial inflammatory infiltrate which is similar to other group of drugs [65]. The histological appearance is similar to that caused by phenytoin, cyclosporin, and other calcium channel antagonists. Discontinuation of the drug usually results in complete regression of the gingival overgrowth.
\nMinocycline, a semi-synthetic broad-spectrum antimicrobial agent, is mainly used for the treatment of acne, chronic respiratory diseases, and rheumatoid arthritis. It is lipid soluble and therefore can easily penetrate into body fluids, such as saliva and gingival crevicular fluid, and into various body tissues including bone and soft tissues [66]. Minocycline-induced pigmentation of oral mucous membranes including the buccal mucosa, gingiva, palatal area, lips and tongue has been reported [67, 68, 69]. The pathophysiology of minocycline staining is not clearly understood. It has been suggested that either a minocycline-metabolite complex or melanin, iron and calcium-containing granules are the source of the pigment [70]. The pigmentation of oral soft tissues appears as distinctive blue-gray or brown in color and occurs as a result of pigmented black bone visible through the thin overlying mucosa without any actual involvement of the soft tissue itself (Figure 5) [71]. The pigmentation appears to be related to the duration of minocycline therapy or the cumulative dose, and resolves once the drug is discontinued [69, 72]. Intraoral pigmentation can be managed with lasers [71].
\nDiscoloration of the gingiva and teeth in a patient on minocycline therapy.
A higher prevalence of gingival inflammation, loss of attachment and gingival enlargement in woman taking hormone based oral contraceptives [73, 74]. The gingival inflammation seems to be associated to high concentrations of sex hormones present in oral contraceptives (Figure 6) [75]. Oral contraceptives (OCs) enhance periodontal breakdown by reducing the resistance to dental plaque and can induce gingival enlargement in otherwise healthy females [76, 77]. Oral contraceptives have pronounced effects on gingival microvasculature and it has been shown that human gingiva contains receptors for progesterone and estrogen. The dosage and duration of intake are the possible factors which influence the effect of oral contraceptives on the periodontal condition. A continued exposure of oral contraceptives for longer duration results in higher risk of periodontal disease development due to increased production of pro-inflammatory cytokines and prostaglandins as a result of elevated levels of the hormones [78, 79]. However, the currently used combined oral contraceptives showed little influence on the periodontal health, possibly related to their lower concentration of progesterone and estrogen compared to the earlier formulations [74, 80]. A critical review supports the conclusion that there is no impact of modern oral contraceptives on the periodontal and gingival tissues. Hence, it is concluded that oral contraceptives can no longer be considered to constitute a risk factor for gingivitis or periodontitis [81].
\nGingival changes in a patient on oral contraceptives.
Bisphosphonates are used widely in the management of primary and metastatic bone cancer, as well as osteoporosis. Bisphosphonates improve bone mineral density, reduce fracture risk, and reduce hypercalcemia of malignancy. Incidents of osteonecrosis of the jaw have been reported in people on bisphosphonates and undergoing invasive dental treatment procedures, including tooth extractions, dental implants, and surgical and nonsurgical periodontal treatment [82]. The risk for bisphosphonate-induced osteonecrosis may be influenced by the route of administration of the drug, the potency and the duration of use. Jaw osteonecrosis appears more associated with the intravenous use of bisphosphonates. A review showed that 94% of the published cases of osteonecrosis correlated with administration of intravenous, nitrogen-containing bisphosphonates [83].
\nBisphosphonates inhibit bone resorption by acting on osteoclasts to reduce their activity or to increase the rate of apoptosis [84]. The inhibitory effect on osteoclast function, bone formation coupled with resorption results in an overall reduction in the rate of bone remodeling [85]. Moreover, bisphosphonates may antagonize the action of several matrix metalloproteinase involved in breakdown of structural components of periodontal connective tissue [86]. In view of the antiresorptive properties of bisphosphonates and the ability to inhibit cytokines of periodontal tissue destruction, there has been interest in the possible use of bisphosphonates as an adjunct to scaling and root planning in the management of periodontitis [87, 88]. Although bisphosphonates claim its effectiveness in controlling periodontal destruction, clinical use warrants further evidence. A systematic review concluded that bisphosphonates may be used topically as an adjunct to scaling and root planing [89].
\nStatins, or inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMG-CoA reductase), are a group of drugs, used mainly to treat hyperlipidemia. In addition to their cholesterol lowering properties they also have strong anti-inflammatory properties and may stimulate bone growth [90]. Statins have anabolic effects on the bone by augmenting bone morphogenetic protein-2 expression and thereby contributing towards the differentiation and activity of osteoblasts [91]. Due to their activity on bone formation statins have been considered as potential agents in improving periodontal treatment outcomes [92]. Limited data is available on the impact of stains on periodontal tissues suggesting a reduction in periodontal destruction and tooth loss [93]. Experimental studies on rats support the potential protective effect of statins on periodontal bone loss. Although these basic data are interesting, further research could extrapolate the use of statins as a potential adjunctive therapeutic agent in periodontal disease and bone regeneration.
\nAnti-platelet drugs are widely used for the treatment of established cardiovascular disease, the prevention of atherothrombotic events and the treatment of myocardial infarction. The most commonly prescribed antiplatelets drugs are aspirin and clopidogrel which are often used in combination. Both of these drugs have been reported to cause increased gingival bleeding. Patients on these medications carry a risk of an increased tendency to bleeding during or following periodontal surgery and this risk is far greater when the drugs are used in combination [94].
\nSeveral systemic factors are known to contribute to periodontal diseases or conditions and among those are the intake of drugs. The gingival overgrowth associated with medications occur as a side effect of systemic medications. These medications include the anti-seizure drug phenytoin, the immune suppressor cyclosporin A, and certain anti-hypertensive dihydropyridine calcium-channel-blockers, most notably nifedipine. It is crucial that health professionals understand the complications that medications can have on the oral health of their patients. In order to properly diagnose and treat patients, a complete medical history including prescription medications, over the counter drugs and dietary supplements must be recorded which will enable the healthcare team to identify the causative agents.
\nNone declared.
This is a brief overview of the main steps involved in publishing with IntechOpen Compacts, Monographs and Edited Books. Once you submit your proposal you will be appointed a Author Service Manager who will be your single point of contact and lead you through all the described steps below.
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