Laboratory results of oil recovery applications by nanosurfactant.
\\n\\n
More than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\\n\\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\\n\\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\\n\\nAdditionally, each book published by IntechOpen contains original content and research findings.
\\n\\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\\n\\n\\n\\n
\\n"}]',published:!0,mainMedia:null},components:[{type:"htmlEditorComponent",content:'
Simba Information has released its Open Access Book Publishing 2020 - 2024 report and has again identified IntechOpen as the world’s largest Open Access book publisher by title count.
\n\nSimba Information is a leading provider for market intelligence and forecasts in the media and publishing industry. The report, published every year, provides an overview and financial outlook for the global professional e-book publishing market.
\n\nIntechOpen, De Gruyter, and Frontiers are the largest OA book publishers by title count, with IntechOpen coming in at first place with 5,101 OA books published, a good 1,782 titles ahead of the nearest competitor.
\n\nSince the first Open Access Book Publishing report published in 2016, IntechOpen has held the top stop each year.
\n\n\n\nMore than half of the publishers listed alongside IntechOpen (18 out of 30) are Social Science and Humanities publishers. IntechOpen is an exception to this as a leader in not only Open Access content but Open Access content across all scientific disciplines, including Physical Sciences, Engineering and Technology, Health Sciences, Life Science, and Social Sciences and Humanities.
\n\nOur breakdown of titles published demonstrates this with 47% PET, 31% HS, 18% LS, and 4% SSH books published.
\n\n“Even though ItechOpen has shown the potential of sci-tech books using an OA approach,” other publishers “have shown little interest in OA books.”
\n\nAdditionally, each book published by IntechOpen contains original content and research findings.
\n\nWe are honored to be among such prestigious publishers and we hope to continue to spearhead that growth in our quest to promote Open Access as a true pioneer in OA book publishing.
\n\n\n\n
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\r\n\r\n\tThe book will further detail other small bowel diseases such as celiac disease, malabsorption diseases, and small bowel neoplasms in a separate chapter.
\r\n\r\n\tThe future options of small bowel endoscopy shall be covered in the final chapter. The book will be written by experts in the field and prove to be a valuable resource to all the training and practicing gastroenterologists, physicians and surgeons who are looking for a composite overview of endoscopy in small bowel diseases.
",isbn:"978-1-83968-780-8",printIsbn:"978-1-83968-779-2",pdfIsbn:"978-1-83968-781-5",doi:null,price:0,priceEur:0,priceUsd:0,slug:null,numberOfPages:0,isOpenForSubmission:!1,hash:"a7c515b4add9ecf0a5de381a72d145e5",bookSignature:"Dr. Mahesh Goenka, Dr. Usha Goenka and Dr. Gajanan Rodge",publishedDate:null,coverURL:"https://cdn.intechopen.com/books/images_new/10309.jpg",keywords:"Capsule Endoscopy, Enteroscopy, CT Enterography, MR Enterography, Ulcerative Colitis, Crohn's Disease, Malena, Hematochezia, Celiac Disease, Malabsorption, Motorised Spiral Enteroscopy, Device-assisted Enteroscopy",numberOfDownloads:null,numberOfWosCitations:0,numberOfCrossrefCitations:null,numberOfDimensionsCitations:null,numberOfTotalCitations:null,isAvailableForWebshopOrdering:!0,dateEndFirstStepPublish:"September 11th 2020",dateEndSecondStepPublish:"October 9th 2020",dateEndThirdStepPublish:"December 8th 2020",dateEndFourthStepPublish:"February 26th 2021",dateEndFifthStepPublish:"April 27th 2021",remainingDaysToSecondStep:"3 months",secondStepPassed:!0,currentStepOfPublishingProcess:4,editedByType:null,kuFlag:!1,biosketch:"A world-renowned gastroenterologist and a perfect blend of an extraordinary clinician, enthusiastic academician, and a skillful endoscopist. He has performed more than >1,00,000 endoscopic procedures with expertise in advance therapeutic endoscopy such as Spyglass Cholangioscopy, Cellvizio & POEM. Dr. Goenka is appointed as a member of the International Committee of American Society of Gastrointestinal Endoscopy. He has written 135 publications in various medical journals and 55 books.",coeditorOneBiosketch:"Dr. Usha Goenka is a senior interventional radiologist and specializes in vascular & nonvascular interventional radiology. She has completed her post-graduation M.D. in Radiology from the prestigious Postgraduate Institute of Medical Education and Research (PGIMER), India. She has more than 35 publications in various national and international journals.",coeditorTwoBiosketch:"Dr. Gajanan Rodge is a young gastroenterologist and has a special interest in the field of endoscopy. He also has experience as a clinical associate in the Gastroenterology department at Lilavati Hospital. He has recently been awarded the Poster of Distinction Award at the APDW 2019.",coeditorThreeBiosketch:null,coeditorFourBiosketch:null,coeditorFiveBiosketch:null,editors:[{id:"292494",title:"Dr.",name:"Mahesh",middleName:null,surname:"Goenka",slug:"mahesh-goenka",fullName:"Mahesh Goenka",profilePictureURL:"https://mts.intechopen.com/storage/users/292494/images/system/292494.jpg",biography:"PRESENT DESIGNATION :\n\nDirector, Institute of Gastrosciences and Liver, Apollo Gleneagles Hospital, Kolkata.\n\nPROFESSIONAL SOCIETY\t\t\t \n\nPresident, Asio-Pacific Digestive Week (2019)\nGovernor (Indian region), American College of Gastroenterology (2017-2020)\nPresident, Society of Gastrointestinal Endoscopy of India (2016-17) \nMember, International Committee, American Society of GI Endoscopy (ASGE)- 2013-16\n\n \nQUALIFICATION\n\nMNAMS\t: Gastroenterology 1995 (awarded by National Academy of \n\t\t Medical Sciences, New Delhi)\n\nD.M\t\t: Gastroenterology\n\t\t June 1989, Postgraduate Institute of Medical Education and \n\t\t Research (PGIMER) Chandigarh, India.\n\nM.D\t\t: Medicine \n\t\t June 1987, Postgraduate Institute of Medical Education and \n\t\t Research (PGIMER) Chandigarh, India.\n\nM.B.B.S\t: June 1981, Calcutta Medical College, Calcutta, India.\n\nF.A.C.G \t: Fellow, American College of Gastroenterology, 1996.\n\nF.A.S.G.E : Fellow, American Society of Gastrointestinal Endoscopy, 2007\n\nA.G.A.F\t: Fellow of the American Gastroenterological Association, 2016\n\nF.R.C.P\t: Fellowship of Royal College of Physicians, Glasgow 2017\n\n\nEXPERIENCE:\n\n8/96 onwards: Organised the Dept. at Apollo Gleneagles Hospital, AMRI & \n \t Eko Endoscopy Centre, Kolkata\n\n1/96 - 3/96: Fellow - Department of Endoscopic surgery, - Hamburg University, \n Germany. \n\n4/91 - 7/96: Assistant Professor (Gastroenterology) Postgraduate Institute of\n Medical Education and Research (PGIMER) Chandigarh, India.\n\n1/90 - 4/91: Pool Officer, Dept. of Gastroenterology, Postgraduate Institute of\n Medical Education and Research (PGIMER) Chandigarh, India. \n\n7/87 - 12/89: Senior Residency in Gastroenterology, (PGIMER) Chandigarh, India\n\n7/84 - 6/87: Residency in Medicine, (PGIMER) Chandigarh, India.\n\nINTERNATIONAL RECOGNITION\n\n1.\tAppointed as Clinical Professor of Medicine Gastroenterology at Medical College of Wisconsin USA for 2019 to 2024.\n2.\tElected as Governor (Indian region). American College of Gastroenterology for 3yrs. (2017-2020)- Initiated and Organised Best of American College of Gastroenterology, Kolkata, Bangalore and New Delhi on 17, 18, 19th Jan 2020.\n3.\tAdjunct Professor of Medicine at University of Wisconsin School, USA\n4.\tAppointed as member of International Committee of American Society of Gastrointestinal Endoscopy (2014-18)\n5.\tAppointed as Adjunct Associate Professor in Dept. of Medicine at University of Queensland, Australia for 3 yrs. (2011-2014)\n6.\tInvited as Faculty for Asio-Pasific Digestive Week (APDW) held at Kobe, Japan in Nov 2016. and HongKong 2017, Korea 2018\n7.\tInvited as a Guest Speaker to the 12th World congress at Paris organized by International agency for Research of Cancer and World Health Organization (WHO) at UNESCO Headquarters in August 2013. Delivered two lectures. \n8.\tInvited to visit Department of Gastroenterology at Zhongshan Hospital, Fudan University at Sanghai, China in July 2013.\n9.\tInvited faculty for Asia Pacific Digestive week (APDW) 2011 held at Singapore from 1st to 4th Oct 2011.\n10.\tVisiting Professorship awarded by University of Alabama at Birmingham, USA. Invited to the Basil I Hirschowitz Endoscopy Center of Excellence & delivered talks on ERCP and Small Bowel Endoscopy on 4th Oct’2010\n11.\tMember of Asia Pacific Panel Recommendations for Optimal Management of Hepatitis B “APPROACH group”(Headed by Prof M Omata of Japan) to draw guide line on treatment of Hepatitis B- sole member respesenting India. (Work published subsequently in Hepatology International)\n12.\tDelivered a guest lecture on “Small bowel Endoscopy” at Dubai in April’2010 during Annual meeting of Middle- East Chapter of Indian Society of Gastroenterology\n13.\tAdvisory Editorial Board member of Journal of Bioscience & Medicine, official Journal of International Association for Biological and Biomedical Science.\n14.\tReviewer for Malaysian Journal of Medical sciences & Journal of Gastroenterology & Hepatology, Gastrointestinal Endoscopy, World Journal of Gastroenterology, World J of GI Endoscopy.\n15.\tInvited in 2013 by World Journal of Gastroenterology and World Journal of Hepatology to write state of Art Review Articles on Capsule Endoscopy and Hilar Cholangiocarcinoma respectively. \n16.\tGuest faculty at Digestive Diseases week, Annual meeting of American Gastroenterology Association during 2014 and 2015. Delivered guest lectures at Chicago and Washington respectively\n\n\nNATIONAL RECOGNITION\n\n1.\tPresident of Society of Gastrointestinal Endoscopy of India (SGEI 2016-17), a scientific national body of GI endoscopists (about 1500 members)\n2.\tAppointed Fellow of West Bengal Academy of Science & Technology (2011)\n3.\tAwarded Adjunt Professorship by Apollo Hospitals Education and Research Foundation July 2012\n4.\tReviewer for Tropical Gastroenterology, Indian J of Gastroenterology\n5.\tEditor of Apollo Medicine Journal\n6.\tMember of National Task Force by Indian Association for study of liver on Hepatocellure carcinoma, Hepatitis C, & by Indian society of Gastroenterology on GI Bleed and Inflammatory Bowel Disease \n7.\tEditor-In-Chief, Journal of Digestive Endoscopy, official journal of Society of Gastrointestinal Endoscopy of India (2015 onwards)\n\nAWARDS AND SCHOLARSHIPS\n\n1.\tApollo Distinguished Academician award 2019 by Apollo Hospitals, Chennai.\n\n2.\tAcademic achievement award 2016 by Apollo Hospital Group in 2016.\n\n3.\tJ. Mitra Award 2005-06 given by Indian Society of Gastroenterology in the year 2006 for contribution to G. I. Endoscopy.\n\n4.\tSISCO PENTAX ORATION for 2002 awarded by Society of G. I. Endoscopy for contribution in the field of G. I. Endoscopy.\n\n5.\tResearch fellowship awarded by Indian Association for Study of the Liver (1993) for research contribution in the field of hepatology.\n\n6.\tAwarded Academic achievements awards by Apollo Hospital Educational and Research Foundation for original research publication in 2011\n\n7.\tSilver Medal (first order) for securing 1st position in M.D. (Medicine) at PGIMER, Chandigarh.\n\n8.\tFirst in the first MBBS examination of Calcutta University (awarded Maharaja Gwalior Prize).\n\n9.\tHonours in Chemistry, Anatomy, Physiology, Ophthalmology and E.N.T. from the Calcutta University.\n\n10.\tCollege merit scholarship during the 2nd, 3rd, 4th and final years of MBBS from the Calcutta University.\n\n11.\tSilver Medal for the best student of 1st year class in MBBS.\n\n12.\tGold medal for the best student in Anatomy in 2nd year MBBS.\n\n13.\tSilver Medal for the best student in Anatomy in 1st year MBBS.\n\n14.\tAnandlal Sanyal Prize in Mid – Wifery (1978 – 1979).\n\n15.\tSenior Prosector’s Prize in Anatomy (1975 – 1976).\n\n\nTEACHING EXPERIENCE\n\n1.\tPresently Heading the Dept. of Gastroenterology at Apollo Gleneagles Hospitals, Kolkata which imparts National Board Postgraduate Degree in Gastroenterology, called Diplomate in National Board (DNB)- actively involved in teaching of Postgraduate Students since last 7 yrs.\n\n2.\tFive & half years (1991-1996) as Assistant Professor (Gastroenterology) at Postgraduate Institute of Medical Education and Research (PGMER) Chandigarh, India. This institute imparts MD (Postgraduate) and DM (Super specialty) degrees\n\n3.\tOne and half year (1990-91) as Pool Officer, Dept. of Gastroenterology, Postgraduate Institute of Medical Education and Research (PGIMER) Chandigarh, India.\n\n4.\tTwo years (1987-1989) as Senior Residency in Gastroenterology, (PGIMER) Chandigarh, India (Teaching postgraduate, MD students)",institutionString:"Institute of Gastrosciences and Liver",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"0",institution:null}],coeditorOne:{id:"292497",title:"Dr.",name:"Usha",middleName:null,surname:"Goenka",slug:"usha-goenka",fullName:"Usha Goenka",profilePictureURL:"https://mts.intechopen.com/storage/users/no_image.jpg",biography:"Dr. Usha Goenka is a senior interventional radiologist and specialises in vascular & nonvascular interventional radiology. She is currently working as the Director and Head, Department of clinical imaging and interventional radiology at Apollo Gleneagles Hospital, Kolkata. She has been a merit holder and university topper through her MBBS graduation. She has completed her post-graduation M.D. in Radiology from the prestigious Postgraduate Institute of Medical Education and Research (PGIMER), India. She has more than 35 publications in various national and international journals. She has a keen interest in teaching and has delivered more than 50 lectures in national and international conferences.",institutionString:"Apollo Gleneagles Hospital",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"0",institution:null},coeditorTwo:{id:"292496",title:"Dr.",name:"Gajanan",middleName:null,surname:"Rodge",slug:"gajanan-rodge",fullName:"Gajanan Rodge",profilePictureURL:"https://mts.intechopen.com/storage/users/no_image.jpg",biography:null,institutionString:"Apollo Gleneagles Hospital",position:null,outsideEditionCount:0,totalCites:0,totalAuthoredChapters:"1",totalChapterViews:"0",totalEditedBooks:"0",institution:null},coeditorThree:null,coeditorFour:null,coeditorFive:null,topics:[{id:"16",title:"Medicine",slug:"medicine"}],chapters:null,productType:{id:"1",title:"Edited Volume",chapterContentType:"chapter",authoredCaption:"Edited by"},personalPublishingAssistant:{id:"9699",firstName:"Iva",lastName:"Lipović",middleName:null,title:"Ms.",imageUrl:"https://mts.intechopen.com/storage/users/9699/images/4740_n.png",email:"iva.l@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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Venkateswarlu",coverURL:"https://cdn.intechopen.com/books/images_new/371.jpg",editedByType:"Edited by",editors:[{id:"58592",title:"Dr.",name:"Arun",surname:"Shanker",slug:"arun-shanker",fullName:"Arun Shanker"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"878",title:"Phytochemicals",subtitle:"A Global Perspective of Their Role in Nutrition and Health",isOpenForSubmission:!1,hash:"ec77671f63975ef2d16192897deb6835",slug:"phytochemicals-a-global-perspective-of-their-role-in-nutrition-and-health",bookSignature:"Venketeshwer Rao",coverURL:"https://cdn.intechopen.com/books/images_new/878.jpg",editedByType:"Edited by",editors:[{id:"82663",title:"Dr.",name:"Venketeshwer",surname:"Rao",slug:"venketeshwer-rao",fullName:"Venketeshwer Rao"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}},{type:"book",id:"4816",title:"Face Recognition",subtitle:null,isOpenForSubmission:!1,hash:"146063b5359146b7718ea86bad47c8eb",slug:"face_recognition",bookSignature:"Kresimir Delac and Mislav Grgic",coverURL:"https://cdn.intechopen.com/books/images_new/4816.jpg",editedByType:"Edited by",editors:[{id:"528",title:"Dr.",name:"Kresimir",surname:"Delac",slug:"kresimir-delac",fullName:"Kresimir Delac"}],productType:{id:"1",chapterContentType:"chapter",authoredCaption:"Edited by"}}]},chapter:{item:{type:"chapter",id:"41438",title:"Molecular Basis of Insulin Resistance and Its Relation to Metabolic Syndrome",doi:"10.5772/54620",slug:"molecular-basis-of-insulin-resistance-and-its-relation-to-metabolic-syndrome",body:'The metabolic syndrome is an agglomeration of interrelated risk factors that is associated with nearly 5-fold increased risk for type 2 diabetes mellitus (DM) and a 2-fold increased risk of coronary artery disease (CAD) [1]. Reaven first suggested this cluster of metabolic abnormalities in 1988. It is characterized by insulin resistance, visceral adiposity, dyslipidemia and a systemic pro-inflammatory and pro-coagulant state [2]. Insulin resistance is defined as reduced insulin action in metabolic and vascular target tissues, hence higher than normal concentration of insulin is required to maintain normoglycemia. On a cellular level, it indicates an inadequate strength of insulin signaling from the insulin receptor downstream to the final substrates of insulin action involved in multiple metabolic and mitogenic aspects of cellular function [3].
The development of insulin resistance leads to many of the metabolic abnormalities associated with this syndrome. Patients with insulin resistance tend to have impaired fasting plasma glucose levels, which increase the prevalence of more atherogenic, small dense low-density lipoprotein (LDL) particles. The growing incidence of insulin resistance and metabolic syndrome (MS) is seriously threatening human health globally. Individuals with MS have a 30%–40% probability of developing diabetes and/or CVD within 20 years, depending on the number of components present [4].
In the United States (US), the prevalence of the MS in the adult population was estimated to be more than 25%. Similarly, the prevalence of MS in seven European countries was approximately 23%. It was estimated that 20%–25% of South Asians have developed MS and many more may be prone to it [5,6]. The main reason why MS is attracting scientific and commercial interest is that the factors defining the syndrome are all factors associated with increased morbidity and mortality in general and from CVD in particular [7].
Though, Insulin resistance has been recognized as a basis of CVD and diabetes type II, its etiology still remains elusive. Recent studies have contributed to a deeper understanding of the underlying molecular mechanisms of Insulin resistance. This review provides a detailed understanding of these basic pathophysiological mechanisms which may be critical for the development of novel therapeutic strategies to treat/ prevent metabolic syndrome.
Insulin action is initiated by an interaction of insulin with its cell surface receptor [8]. The insulin receptor (IR) is a heterotetramer consisting of two α subunits and two β subunits that are linked by disulphide bonds. Insulin binds to the extracellular α subunit of the insulin receptor and activates the tyrosine kinase in the β subunit {figure 1). Binding of insulin to IR effects a series of intramolecular transphosphorylation reactions, where one β subunit phosphorylates its adjacent partner on a specific tyrosine residue. Once the tyrosine kinase of insulin receptor is activated, it promotes autophosphorylation of the β subunit itself, where phosphorylation of three tyrosine residues (Tyr-1158, Tyr-1162, and Tyr-1163) is required for amplification of the kinase activity [9]. It then recruits different substrate adaptors such as the Insulin Receptor Substrate (IRS) family of proteins. Although IRs are present on the surface of virtually all cells, their expression in classical insulin target tissues, i.e. muscle, liver and fat, is extremely high [10]. Tyrosine phosphorylated IRS then displays binding sites for numerous signaling partners. Phosphorylated IRS proteins serve as multisite docking proteins for various effector molecules possessing src homology 2 (SH2) domains, including phosphatidylinositol 3-kinase (PI 3-kinase) regulatory subunits (p85, p55 p50, p85, and p55PIK), the tyrosine kinases Fyn and Csk, the tyrosine protein phosphatase SHP-2/Syp, as well as several smaller adapter molecules such as the growth factor receptor binding proteins Grb-2, Crk, and Nck [11]. Activation of these SH2 domain proteins initiates signaling cascades, leading to the activation of multiple downstream effectors that ultimately transmit the insulin signal to a branching series of intracellular pathways that regulate cell differentiation, growth, survival, and metabolism. Four members of the IRS family have been identified that are considerably similar in their general architecture [12-15]. IRS proteins share a similar structure characterized by the presence of an NH2-terminal pleckstrin homology (PH) domain adjacent to a phosphotyrosine-binding (PTB) domain followed by a variable-length COOH-terminal tail that contains a number of Tyr and Ser phosphorylation sites. The PH domain is critical for IR-IRS interactions. Plasma membrane phospholipids, cytoskeletal elements, and protein ligands mediate these interactions [16, 17]. In contrast, the PTB domain interacts directly with the juxtamembrane (JM) domain of the insulin and IGF-I receptors [18, 19], and hindrance of these interactions (by Ser/Thr phosphorylation) negatively affects insulin signaling [19]. A third domain, the kinase regulatory loop binding (KRLB) is found only in IRS-2 [20, 21]. This domain interacts with the phosphorylated regulatory loop of the IR, whereas the phosphorylation of two Tyr residues within the KRLB are crucial for this interaction [22].
PI3 kinase is a target of the IRS proteins (IRS-1 and IRS-2) which phosphorylates specific phosphoinositides to form phosphatidylinositol 4,5 bisphosphate (PIP2) to phosphatidylinositol 3,4,5 triphosphate; in turn, this activates ser/thr kinase, i.e. phosphoinositide-dependent kinase-1 (PDK1) [23, 24]. Known substrates of the PDKs are the protein kinase B (PKB) and also atypical forms of protein kinase C (PKC) [25].
Downstream from PI 3-kinase, the serine/threonine kinase Akt (also called PKB) triggers insulin effects on the liver. Phosphatidylinositol-dependent kinase (PDK) and PKB/Akt have a pleckstrin homology domain that enables these molecules to migrate toward the plasma membrane [26]. Activated Akt induces glycogen synthesis, through inhibition of GSK-3; protein synthesis via mTOR and downstream elements; and cell survival, through inhibition of several pro-apoptotic agents (Bad, Forkhead family transcription factors, GSK-3). Insulin stimulates glucose uptake in muscle and adipocytes via translocation of GLUT4 vesicles to the plasma membrane [27- 29]. This suggests that the impairment of insulin activity leading to insulin resistance is linked to insulin signalling defects.
Recently, an alternative PI 3-kinase independent mechanism to enhance GLUT4 translocation and glucose uptake was described. According to this model, binding of insulin to its receptor finally activates the small G-protein TC10 via the scaffolding protein CAP (Cbl-associated protein) resulting in GLUT4 translocation and enhanced glucose uptake [30]. Insulin signaling also has growth and mitogenic effects, which are mostly mediated by the Akt cascade as well as by activation of the Ras/MAPK pathway. A negative feedback signal emanating from Akt/PKB, PKCΖ, p70 S6K and the MAPK cascades results in serine phosphorylation and inactivation of IRS signaling [31, 32]. Insulin signalling molecules involved in metabolic and mitogenic action have been demonstrated to play a role in cellular insulin resistance. A few recent reports indicate that some PKC isoforms may have a regulatory effect on insulin signalling. The expression levels and activity of a few PKC isoforms are found to be associated with insulin resistance [33-35].
Recent data from PKB knockout animal models provide an insight into the role of PKB in normal glucose homeostasis. While disruption of PKB/Akt1 isoform in mice have not shown to cause any significant perturbations in metabolism, mice with a knock out of the PKB(Akt2) isoform show insulin resistance ending up with a phenotype closely resembling Type 2 diabetes in humans [36-37]. Subsequent studies [38- 40] in insulin-resistant animal models and humans have consistently demonstrated a reduced strength of insulin signaling via the IRS-1/PI 3-kinase pathway, resulting in diminished glucose uptake and utilization in insulin target tissues. Recent studies on inherited insulin post-receptor mutations in humans have detected a missense mutation in the kinase domain of PKB (Akt2) in a family of severely insulin resistant patients. The mutant PKB was unable to phosphorylate downstream targets and to mediate inhibition of phosphoenolpyruvate carboxykinase (PEPCK), a gluconeogenic key enzyme [41]. Another recent study, involving the stimulation of PI3K and Akt-1, -2, and -3 by insulin and epidermal growth factors (EGFs) in skeletal muscles from lean and obese insulin-resistant humans showed that Insulin activated all Akt isoforms in lean muscles, whereas only Akt-1 was activated in obese muscles. Insulin receptor substrate (IRS)-1 expression was reduced in obese muscles, and this was accompanied by decreased Akt-2 and -3 stimulation. In contrast, insulin- or EGF-stimulated phosphotyrosine-associated PI3K activity was not different between lean and obese muscles. These results showed that a defect in the ability of insulin to activate Akt-2 and -3 may explain the impaired insulin-stimulated glucose transport in insulin resistance [42].
This suggests that the impairment of insulin activity leading to insulin resistance is linked to insulin signalling defects. These insulin signalling pathways are shown in figure1.
Two separate, but likely, complementary mechanisms have recently emerged as a potential explanations for Insulin resistance. First, changes in IRS-1 either due to mutations or serine phosphorylation of IRS proteins can reduce their ability to attract PI 3-kinase, thereby minimizing its activation. A number of serine kinases that phosphorylate serine residues of IRS-1 and weaken insulin signal transduction have been identified. Additionally, mitochondrial dysfunction has been suggested to trigger activation of several serine kinases, leading to a serine phosphorylation of IRS-1. Second, a distinct mechanism involving increased expression of p85α has also been found to play an important role in the pathogenesis of insulin resistance. Conceivably, a combination of both increased expression of p85α and increased serine phosphorylation of IRS-1 is needed to induce clinically apparent insulin resistance.
IRS-1 protein is a gene product of IRS-1 gene. In humans, rare mutations of the IRS-1 protein are associated with insulin resistance [43] and disruption of the IRS-1 gene in mice results in insulin resistance mainly of muscle and fat [44]. The genetic analysis of the IRS-1 gene has revealed several base-pair changes that result in amino acid substitutions [45-47]. The most common amino acid change is a glycine to arginine substitution at codon 972 (G972R), which has an overall frequency of ≈6% in the general population [48], with a carrier prevalence of 9% among Caucasians [49]. This mutation has been reported to significantly impair IRS-1 function in experimental models [50], and clinical studies have shown that this genetic variant is associated with reduced insulin sensitivity [51]. Expression of this variant in 32-D cells is associated with a significant (20-30%) impairment of insulin-stimulated PI3-kinase activity, as well as reduced binding of IRS-1 to the p85 regulatory subunit of PI3-kinase. Genotype/phenotype studies stratified according to body mass index (BMI) indicate that obese subjects who are heterozygous for the mutant allele have a 50% decrease in insulin sensitivity, compared with wild-type obese subjects. This suggests that there may be an interaction between the mutant allele and obesity, such that, in the presence of obesity, the mutant variant may aggravate the obesity-associated insulin resistance [49]. Moreover, earlier observations have indicated that the presence of a mutated IRS-1 gene is associated with dyslipidemia, further suggesting that this gene variant may have a significant effect on several risk factors for CAD [48, 50-52].
Interestingly, IRS-2 knockout mice not only show insulin resistance of muscle, fat and liver, but also manifest diabetes as a result of cell failure [53]. This phenotype with severe hyperglycemia as a consequence of peripheral insulin resistance and insufficient insulin secretion due to a significantly reduced β-cell mass reveals many similarities to type 2 diabetes in man and outlines the role of IRS proteins for the development of cellular insulin resistance. Homozygous knockout mice lacking a single allele of IRS-1 gene lack any significant phenotype, whereas homozygous disruption of the IRS-1 gene results in a mild form of insulin resistance [54]. IRS-1 homozygous null mice (IRS-1-/-) do not show a clear diabetic phenotypic expression, presumably because of pancreatic β cell compensation. IRS-2−/− mice, on the other hand, developed diabetes as a result of severe insulin resistance paired with β-cell failure [55, 56]. Even though β cell mass was reduced in IRS-2−/− mice, individual β cell showed normal or increased insulin secretion in response to glucose [55].
In regard to insulin signaling, experiments in immortalized neonatal hepatocytes show that the lack of IRS-2 is not compensated for by an elevation of IRS-1 protein content or an increase in tyrosine phosphorylation [57]. Previous experiments performed in peripheral tissues of IRS-1−/− mice by Yamauchi et al. [44] suggested that IRS-2 could be a major player in hepatic insulin action. However, to what extent reduced IRS-2 contributes to insulin resistance in the liver remains uncertain. In humans, a number of polymorphisms have been identified in the IRS-2 gene. Among those, the amino acid substitution Gly1057Asp has been found in various populations with a prevalence sufficiently high to modulate a population’s risk of type 2 diabetes. In Caucasians, Finns, and Chinese, however, this variant has not shown an associated with type 2 diabetes [58, 59]. Although the polymorphism was associated with decreased insulin sensitivity and impaired glucose tolerance in women with polycystic ovary syndrome [60], it showed no association with insulin sensitivity in other studies [59, 61, 62]. In contrast, another study in women with polycystic ovary syndrome found that homozygous carriers of the Gly1057 allele had higher 2-h plasma glucose concentrations during an oral glucose tolerance test (OGTT) [63]. Decreased serum insulin and C-peptide concentrations during an OGTT were reported in middle-aged glucose-tolerant Danish males carrying the Asp1057 allele [62]. However, using formal β-cell function tests, associations with insulin secretion were not reproduced in German, Finnish, and Swedish populations [59, 61, 62].
IRS-1 contains 21 putative tyrosine phosphorylation sites, several of which are located in amino acid sequence motifs that bind to SH-2 domain proteins, including the p85 regulatory subunit of PI 3-kinase, Grb-2, Nck, Crk, Fyn, Csk, phospholipase Cγ, and SHP-2 [64]. IRS-1 contains also > 30 potential serine/threonine phosphorylation sites in motifs recognized by various kinases such as casein kinase II, protein kinase C, protein kinase B/Akt, and mitogen-activated protein (MAP) kinases [12, 64].
Human IRS-2 contains 22 potential tyrosine phosphorylation sites, but only 13 are conserved in IRS-1. The amino acid sequence identity between IRS-1 and IRS-2 is 43%, with some domains such as the PH and PTB domains exhibiting higher degrees of identity (65 and 75%, respectively). The COOH-terminal domains of IRS-1 and IRS-2 are poorly conserved, displaying only 35% identity, which arises largely from similar tyrosine phosphorylation motifs surrounded by variable stretches of amino acid sequence. The middle of IRS-2 possesses a unique region comprising amino acids 591–786 that interacts specifically with the kinase regulatory loop binding (KRLB) domain of the insulin receptor β subunit [65]. Since this region is absent in IRS-1, this domain may contribute to the signaling specificity of IRS-2. In addition, IRS-1 and IRS-2 may regulate unique signaling pathways because of different tissue distribution, subcellular localization, kinetics of activation/deactivation, or specificity of interaction with downstream effectors [66-68]. For example, it has been shown that IRS-1 and IRS-2 differ in their subcellular localization since IRS-1 is twofold more concentrated in the intracellular membrane compartment than in cytosol, whereas IRS-2 is twofold more concentrated in cytosol than in the intracellular membrane compartment [69]. Further studies have shown that IRS-2 is dephosphorylated more rapidly and activates PI 3-kinase more transiently than IRS-1, thus indicating that differences in kinetics of activation may contribute to the diversity of the insulin signaling transduced by IRS-1 and IRS-2 [69,70].
Since, IRS-1 and IRS-2 have the longest tails, which contain ∼20 potential Tyr phosphorylation sites. Many of the Tyr residues gather into common Tyr-phosphorylated consensus motifs (YMXM or YXXM) that bind SH2 domains of their effector proteins. Spatial matching is required for successful protein-protein interaction. Ser/Thr phosphorylation of IRS proteins in close proximity to their PTB (receptor-binding) region impedes the binding of the SH2 domains of these effectors, thus inhibiting insulin signaling [71].
Serine phosphorylation of IRS proteins can occur in response to a number of intracellular serine kinases [72].The causes of IRS-1 serine phosphorylation are-
mTOR- p70S6 kinase, Amino acids, Hyperinsulinemia
JNK- Stress, Hyperlipidemia, Inflammation
IKK- Inflammation
TNFα- Obesity, Inflammation
Mitochondrial dysfunction
PKC θ- Hyperglycemia, Diacylglycerol, Inflammation
Recent studies have demonstrated hyper-serine phosphorylation of IRS-1 on Ser302, Ser307, Ser612, and Ser632 in several insulin-resistant rodent models [73- 76] as well as in lean insulin-resistant offspring of type 2 diabetic parents [77]. Further evidence for this hypothesis stems from recent studies in a muscle-specific triple serine to alanine mutant mouse (IRS-1 Ser → Ala302, Ser → Ala307, and Ser → Ala612), which has been shown to be protected from high-fat diet–induced insulin resistance in vivo [78]. Based on in vitro studies, serine phosphorylation may lead to dissociation between insulin receptor/IRS-1 and/or IRS-1/PI 3-kinase, preventing PI 3-kinase activation [79, 80] or increasing degradation of IRS-1 [81].
Ser318 of IRS-1 is a potential target for PKCζ [82], JNK, and kinases along the PI3K-mTOR pathway [83]. It is located in close proximity to the PTB domain. Therefore, its phosphorylation presumably disrupts the interaction between IR and IRS-1. Phosphorylation of Ser318 is not restricted to insulin stimulation. Elevated plasma levels of leptin, an adipokine produced by adipocytes [84], also stimulates the phosphorylation of Ser318. This down regulates insulin-stimulated Tyr phosphorylation of IRS-1 and glucose uptake.
In a recent study using skeletal muscle biopsies from 11 humans, the mTOR-S6K pathway was shown to negatively modulate glucose metabolism under nutrient abundance [151]. In agreement with previous studies, phosphorylation of Ser312 and Ser636 of IRS-1 was implicated as part of this negative regulation [85, 86]. Increased phosphorylation of Ser636 of IRS-1 was observed in myotubes of patients with type 2 diabetes. Inhibition of ERK1/2 with PD-98059 reduced this phosphorylation, thereby implicating ERK1/2 in the phosphorylation of Ser636 in human muscle [87].
To unveil the importance of phosphorylated Ser/Thr residues of human IRS-1, Yi et al. [88] adopted a mass spectrometry approach. More than 20 Ser residues of IRS-1 were found to undergo insulin-stimulated phosphorylation in human muscle biopsies, three of which were newly identified sites: Thr495, Ser527, and Ser1005. This report validates previous in vitro and in vivo studies in animal models and suggests that the same strategy could be employed to identify phosphorylated Ser/Thr sites under conditions of insulin resistance, obesity, or type 2 diabetes.
Impaired hepatic glycogen storage and glycogen synthase activity is a common finding in insulin resistance [89] and polymorphisms in the glycogen synthase gene have been described in insulin resistant patients. The most frequent mutations are the so-called XbaI mutations and Met416Val within intron 14 and exon 10, respectively. Currently, there are conflicting data on the correlation of these polymorphisms with insulin resistance and Type 2diabetes mellitus [90-92].
Recently, a hypothesis that mitochondrial dysfunction or reduced mitochondrial content accompanied by a decreased mitochondrial fatty acid oxidation and accumulation of fatty acid acyl CoA and diacylglycerol can cause insulin resistance has gained substantial experimental support [93- 95]. The mechanism of insulin resistance in these cases has been suggested to involve activation of a novel PKC that either by itself or via IKKβ or JNK-1 could lead to increased serine phosphorylation of IRS-1. Severe mitochondrial dysfunction can result in diabetes that is typically associated with severe β-cell dysfunction and neurological abnormalities [96]. In a study,using 13C/31P MRS, it was found that in the healthy lean elderly volunteers with severe muscle insulin resistance, there is∼40% reduction in rates of oxidative phosphorylation activity associated with increased intramyocellular and intrahepatic lipid content [94]. This study suggests that an acquired loss of mitochondrial function associated with aging predisposes elderly subjects to intramyocellular lipid accumulation, which results in insulin resistance [78]. Further, it was found that mitochondrial density was reduced by 38% in the insulin-resistant offspring [77].
[This topic has been dealt in details in subsequent chapter by Wang etal.]
The proinflammatory novel PKCθ has been found to cause serine phosphorylation of IRS-1 [97, 98], while PKCθ knockout mice have been shown to be protected from fat-induced insulin resistance [75]. Increased activity of PKCθ, along with increased activity of JNK, has also been found in skeletal muscle of obese and type 2 diabetic subjects [99, 100], supporting a potential role of these serine kinases in the pathogenesis of insulin resistance.
Insulin signaling pathway showing that the binding of insulin with Insulin receptor (IR) leads to phosphorylation of tyrosine residues followed by activation of downstream signalling pathways which result in recruitment in recruitment of GLUT-4 transporter to the plasma membrane and entry of glucose molecules within the cell. Serine phosphorylation of IRS protein has an inhibitory effect on downstream pathways resulting in insulin Resistance.
A molecular mechanism that can potentially lead to insulin resistance is a disruption in the balance between the amounts of the PI 3-kinase subunits [101]. PI 3-kinase belongs to the class 1a 3-kinases [102], which exist as heterodimers, consisting of a regulatory subunit p85, which is tightly associated with a catalytic subunit, p110. Most tissues express two forms of regulatory subunit, p85α and p85β, and two forms of catalytic subunit, p110α and p110β [102]. p85α and p85β share the highest degree of homology in the C-terminal half of the molecules, which contains two SH2 domains that bind to tyrosine-phosphorylated proteins and an inter-SH2 domain that interacts with the catalytic subunit. The N-terminal halves of p85α and p85β contain an SH3 domain, a BCR homology region, and two proline-rich domains, but these domains are less well conserved between the two molecules. Two isoforms of p85α truncated in the N-terminal region, identified as AS53 (or p55α) [103, 104] and p50α [105, 106], as well as p85α itself, are derived from a single gene (Pik3r1). p85β and another short isoform with limited tissue distribution termed p55γ/p55PIK are encoded by separate genes [107]. Normally, the regulatory subunit exists in stoichiometric excess to the catalytic one, resulting in a pool of freep85 monomers not associated with the p110 catalytic subunit. However, there exists a balance between the free p85 monomer and the p85-p110 heterodimer, with the latter being responsible for the PI 3-kinase activity [108-110]. Because the p85 monomer and the p85-p110 heterodimer compete for the same binding sites on the tyrosine-phosphorylated IRS proteins, an imbalance could cause either increased or decreased PI 3-kinase activity [111]. Increase or decrease in expression of p 85 would result in a shift in the balance either in the favour of free p85 or p85-p110 complexes [108-110].
One of the first indications that an imbalance between the abundance of p85 and p110 can alter PI 3-kinase activity came from experiments with l-6 cultured skeletal muscle cells treated with dexamethazone [111]. This treatment significantly reduced PI 3-kinase activity, despite an almost fourfold increase in expression of p85α (no change in p85β) and only a minimal increase in p110. The authors concluded that p85α competes with the p85-p110 heterodimer, thus, reducing PI 3-kinase activity.
Subsequently, animals with a targeted disruption of p85α (p85+/− heterozygous mice) have been found to have a higher ratio of p85-p110 dimer to free p85 and to be more sensitive to insulin [101, 111-114].
The possibility of mismatch between free p85 and p85-p110 complexes has been recently supported by studies in insulin-resistant states induced by human placental growth hormone [115], obesity, and type 2 diabetes [100] and by short-term overfeeding of lean non-diabetic women [116]. Barbour etal [117] have demonstrated that insulin resistance of pregnancy is likely due to increased expression of skeletal muscle p85 in response to increasing concentrations of human placental growth hormone. Furthermore, women remaining insulin resistant postpartum have been found to display higher levels of p85 in the muscle [118].
Another small study of eight healthy lean women without a family history of diabetes, by Cornier et al showed that 3 days of overfeeding (50% above usual caloric intake) led to a significant increase in expression of p85α, ratio of p85α to p110, and a decline in insulin sensitivity. Within this experimental time frame, overfeeding did not cause any change in serine phosphorylation of either IRS-1 or S6K1, suggesting that increased expression of p85α may be an early molecular step in the pathogenesis of the nutritionally induced insulin resistance [116].
Insulin has 3 major target tissues—skeletal muscle, liver and adipose tissue. It has been postulated that the insulin receptor (IR) is overexpressed in the cells of these tissues. Also only these three organs in the body are capable of glucose deposition and storage; no other cells can store glucose. Removal of excess postprandial glucose by insulin occurs due to glucose uptake and storage in insulin sensitive target cells. About 75% of insulin-dependent postprandial glucose disposal occurs into the skeletal muscle [119]; therefore, it is the major target cell. While insulin-stimulated glucose disposal in adipose tissue is of little quantitative importance compared with that in muscle, regulation of lipolysis with subsequent release of glycerol and FFA into the circulation by insulin has major implications for glucose homeostasis.
It is widely accepted that increased availability and utilization of FFA contribute to the development of skeletal muscle insulin resistance [120-122]. Moreover, FFA have been shown to increase endogenous glucose production both by stimulating key enzymes and by providing energy for gluconeogenesis [123]. Finally, the glycerol released during triglyceride hydrolysis serves as a gluconeogenic substrate [124]. Consequently, resistance to the antilipolytic action of insulin in adipose tissue resulting in excessive release of FFA and glycerol would have deleterious effects on glucose homeostasis.
Patients suffering from insulin resistance and type 2 diabetes frequently display signs of abnormal lipid metabolism, increased circulatory concentration and elevated deposition of lipids in the skeletal muscle [125]. Increase in plasma FFA reduces insulin-stimulated glucose uptake, whereas a decrease in lipid content improves insulin activity in the skeletal muscle cells, adipocytes and liver [126]. Lipid-associated insulin resistance has also been shown to be linked to Glut4 translocation defects [27]. Studies have shown that raising plasma fatty acids in both rodents [75] and humans [127] abolishes insulin activation of IRS-1–associated PI 3-kinase activity in skeletal muscle where IRS-1 is most prevalent.
Adipose tissue can modulate whole body glucose metabolism by regulating levels of circulating free fatty acids (FFA) and also by secreting adipokines, thereby acting as an endocrine organ. However, the underlying mechanism of FFA-induced impairment of insulin signals is still unclear. The molecular mechanism underlying defective insulin-stimulated glucose transport activity can be attributed to increases in intramyocellular lipid metabolites such as fatty acyl CoAs and diacylglycerol, which in turn activate a serine/threonine kinase cascade, thus leading to defects in insulin signaling through Ser/Thr phosphorylation of insulin receptor substrate-1 [78].
Some of the PKC isoforms represent such signalling molecules. PKC isoforms are classified as classical (cPKCα, βI, βII, γ), novel (nPKCδ, ε, θ, η) and atypical (aPKCζ, λ). cPKCs are activated by Ca+2 and diacylglycerol (DAG), nPKCs are activated by only DAG and aPKCs respond to neither Ca+2 nor DAG [128]. Among all these PKC isoforms, nPKCs are said to have a modulatory role in insulin signalling. Recent reports also demonstrate a link between nPKCs and FFA induced insulin resistance.
Diacylglycerol is an attractive trigger for fat-induced insulin resistance in skeletal muscle, since it has been shown to increase in muscle during both lipid infusions and fat feeding and it is a known activator of novel protein kinase C (PKC) isoforms [78].
Recent studies have revealed that accumulation of intracellular lipid metabolites activate a serine kinase cascade involving PKC-ε, leading to decreased insulin receptor kinase activity resulting in 1) lower insulin-stimulated IRS-2 tyrosine phosphorylation, 2) lower IRS-2–associated PI 3-kinase activity, and 3) lower AKT2 activity [129]. These fat-induced defects in insulin signalling in turn result in reduced insulin stimulation of glycogen synthase activity, resulting in decreased insulin-stimulated hepatic glucose uptake and reduced insulin stimulation of hepatic glucose production. Furthermore, reduced activity of AKT2 results in decreased phosphorylation of forkhead box protein O (FOXO), allowing it to enter the nucleus and activate the transcription of the rate-controlling enzymes of gluconeogenesis (phosphoenolpyruvate carboxykinase, glucose-6-phosphate phosphatase).
Increased gluconeogenesis further exacerbates hepatic insulin resistance and results in fasting hyperglycemia [129- 131]. Mitochondrial glycerol-3-phosphate acyltransferase (mtGPAT) is a key enzyme in de novo fat synthesis in liver, and recent studies in mtGPAT knockout mice have clearly implicated intracellular accumulation of diacylglycerol in triggering fat-induced insulin resistance in liver through activation of PKC-ε [132]. These data have important implications for the development of novel therapeutic agents to reverse and prevent hepatic insulin resistance associated with non-alcoholic fatty liver and type 2 diabetes [133].
Lipid infusion in rats and humans impaired insulin-stimulated glucose disposal into the muscle and concomitant activation of PKCθ and PKCδ [134, 135]. PKCδ has been shown to be a possible candidate for phosphorylation of the IR on serine residues [136]. These result in defects in the insulin signalling pathway imposing insulin resistance.
Recently, the PPARγ co-activator-1 (PGC-1) has been recognized as playing a major role in glucose homeostasis of the organism. Work mainly by Spiegelman’s group demonstrated a crucial role of PGC-1 in the regulation of GLUT4 in muscle cells [137]. (PGC)-1α and PGC-1 β are transcriptional factor co-activators that regulate mitochondrial biogenesis. In addition AMP kinase, which is activated during exercise and ischemia by a reduction in the ATP/AMP ratio, has been shown to be an important regulator of mitochondrial biogenesis, mediating its effects through MEF2- and CREB-mediated increased PGC-1α expression [138-141]. Extracellular stimuli such as cold, thyroid hormone, and exercise stimulate mitochondrial biogenesis through PGC-1 in brown fat and skeletal muscle. Increased PGC-1 protein expression leads to increases in the target genes, including nuclear respiratory factor (NRF)-1. NRF-1 is a transcription factor stimulating many nuclear-encoded mitochondrial genes such as OXPHOS genes and also mitochondrial transcription factor A (mtTFA), a key transcriptional factor for the mitochondrial genome. mtTFA can bind to the D-loop of the mitochondrial genome and increase transcription of mitochondrial genes and replication of mitochondrial DNA [142].
A recent study by Ling et al. [143] demonstrated an age dependent decrease in muscle gene expression of PGC-1 α and PGC-1 β in young and elderly dizygotic and monozygotic twins without known diabetes
Adipose tissue also acts as an endocrine organ producing adipokines which modulate glucose homeostasis [144]. Currently, those most intensely discussed are tumor necrosis factor-α (TNF α), leptin, adiponectin and resistin. At a molecular level, TNF α increases serine phosphorylation of IRS-1 and down-regulates GLUT4 expression, thereby contributing to insulin resistance [38]. Furthermore, mice lacking TNF α function were protected from obesity-induced insulin resistance [145]. The role of leptin in regulating food intake and energy expenditure is well established. Humans with leptin deficiency or leptin receptor mutations are severely obese [146,147]. The adiponectin has insulin-sensitizing effects as it enhances inhibition of hepatic glucose output as well as glucose uptake and utilization in fat and muscle. The expression of adiponectin is decreased in obese humans and mice [148]. Thus, in humans, adiponectin levels correlate with insulin sensitivity. Because of its insulin-antagonistic effects, the adipocytokine resistin has attracted a lot of research interest. This is mainly based on data obtained in-vitro and from some animal models. Resistin decreases insulin-dependent glucose transport in-vitro and increases fasting blood glucose concentrations and hepatic glucose production in-vivo [149, 150].
The fasting hyperglycaemia in patients with Type 2 diabetes is the clinical correlate of the increased glucose production by the liver because of insulin resistance. This is as a result of the lack of inhibition of the two key gluconeogenic enzymes, phospho-enolpyruvate carboxykinase (PEPCK) and the glucose-6- phosphatase (G6Pase) catalytic subunit. Studies in hepatoma cells [151,152] suggest that Foxo1 and -3 regulate the transcription of reporter genes containing insulin response elements from the PEPCK and G6Pase promoters. Furthermore, Foxo1 is phosphorylated in an insulin-responsive manner by PIP3-dependent kinases, such as Akt. Reduced activity of AKT2 results in decreased phosphorylation of Foxo protein, allowing it to enter the nucleus and activate the transcription of these rate-controlling enzymes of gluconeogenesis [151,153]. There is increasing evidence that Foxo-proteins are critically involved in the insulin dependent regulation of gluconeogenic gene expression and insulin-resistancein-vivo [154, 155]. In addition, the PPARγco-activator-1 (PGC-1), a factor integrating the effects of glucocorticoids and cAMP on gluconeogenic geneexpression in the liver [156, 157] is also regulated by PKB and Foxo1 [158].
Clearly, the IR is one of the major targets in FFA-induced impairment of insulin activity. Recent studies performed in-vivo suggested that glucose uptake rather than intracellular glucose metabolism is the rate-limiting step for fatty acid induced insulin resistance in humans [159]. This indicates a mechanism in which accumulation of intracellular fatty acids or their metabolites results in an impairment of signaling through IRS/PI 3-kinase.
Recent evidence has shown that PDK1 can directly phosphorylate all PKCs including nPKCs [160]. The PKCε isotype has recently been shown to be related to insulin resistance. Insulin stimulation of PDK1 phosphorylation is inhibited by an FFA, i.e. palmitate. PKCε phosphorylation is dependent on PDK1; FFA incubation of skeletal muscle cells and adipocytes inhibited PDK1 phosphorylation but surprisingly increased PKCε phosphorylation. Inhibition of PDK1 by FFA is reflected in Akt phosphorylation as Akt phosphorylation is also dependent on PDK1 [161]. It has been shown that myristic acid incubation of HEPG2 cells causes myristoylation of PKCε which results in constitutive phosphorylation of PKCεat thr566/ser729 in the kinase domain required for PKCε activity. This phosphorylation was totally independent of PDK1, which the workers demonstrated by using PDK1 knockout cells. In the same way, addition of palmitate to skeletal muscle cells or adipocytes may affect palmitoylation of PKCε resulting in constitutive phosphorylation of PKCε [162, 163]. Taken together, it is clear that FFA causes PDK1-independent phosphorylation of PKCε which in turn translocates to the nucleus, and its time of entry into the nucleus coincides with inhibition of IR gene transcription.
In this review, current developments contributing to understanding of insulin resistance and to the pathogenesis of metabolic syndrome has been discussed. Among the many molecules involved in the intracellular processing of the signal provided by insulin, IRS-2, PKB, Foxo protein and p85 regulatory subunit of PI-3 kinase have attracted particular interest, because their dysfunction results in insulin resistance in-vivo. It has been well established that FFA are responsible for insulin resistance. This review focuses on the current trends in research in this important domain and throws light on certain possibilities regarding the manner in which FFA inhibits insulin activity.
Crude oil has remained the major source of world energy supply despite considerable efforts on other sources of energy [1]. Due to rapid industrialization, there is an increase in world energy demand leading the need to produce increasing volume of crude oil to support this demand. Meanwhile, the oil and gas industry is concerned with the shortage of new conventional oil reserves and low production from existing conventional reservoirs. On average, one-third of conventional reservoirs can be recovered through primary and secondary (i.e. waterflooding) oil recovery processes. The remaining oil-in-place is the target for enhanced oil recovery (EOR). Several EOR methods have been developed to recover bypassed and residual oil in the reservoir. These are majorly categorized into thermal and non-thermal EOR methods. Thermal EOR are unsuitable for reservoirs with great depth or thin pay zones. Hence, non-thermal EOR methods such as gas flooding, chemical flooding and microbial methods have received important attention over the last decades for oil recovery processes [2, 3, 4].
Of the numerous EOR methods, chemical EOR has been considered as the most promising because of its high efficiency, technical and economic feasibilities. Chemical EOR methods increase the efficiency of oil production by increasing the volumetric sweep efficiency of the injected waterflood. By tuning the efficiency of the injected chemical floods, the microscopic (pore scale) displacement efficiency and/or macroscopic (sweep) efficiency of the reservoir is increased leading to an increase in oil production. Chemicals for injection include alkali, surfactants, and polymers. Alkali and surfactants increase oil recovery by improving microscopic displacement at the pore scale; while polymers enhance the volumetric sweep efficiency of the reservoir [5].
Despite its highly reported efficiency and widely acclaimed potentials, chemical EOR has several limitations. The chemicals injected degrade and/or precipitate in the presence of resident reservoir brines and elevated temperature conditions. Besides, retention of the chemicals occurs during their flow in porous media which decreases it process efficiency and may lead to formation damage. To overcome this shortcoming, new salt and temperature-tolerant chemicals of various kinds have been developed and tested for their EOR potentials. Nonetheless, most of the newly developed chemicals have been jettisoned as they were found to increase the cost of the overall EOR process.
Nanotechnology is the application of nanoparticles characterized by a size ranging from 1 to 100 nm (see Figure 1) [6, 7]. In the oil and gas industry, applications of nanotechnology ranges from drilling processes, flow assurance, hydraulic fracturing, cementing, to EOR [8]. For EOR process, the engineered nanomaterials are mixed with fluids that are injected into the reservoir to boost oil production [9].
Schematic of increasing surface area of nanoparticle with decreasing particle size [6].
Nanoparticles and conventional EOR chemicals blends have been reported to possess important properties that are not observed in the individual chemical or nanoparticle [10]. For example, surfactant nanofluids (or nanosurfactant), a blend of nanoparticle and surfactant were reported to improve the efficiency of the surfactant at lowering the interfacial tension (IFT) of oil/water (o/w) interface and lower their adsorption during their transport in porous media [11]. Besides, emulsions and foams stabilized by nanoparticles are found to be thermodynamically stable and easily transported in reservoirs [12]. Meanwhile, polymeric nanofluids demonstrated to have improved rheological behavior and stability at characteristic reservoir temperature and salinity conditions [4]. This chapter presents an overview of nanotechnology applications in chemical EOR. First, the challenges of chemical EOR are briefly discussed. Subsequently, the mechanism and efficiency of nanotechnology application in chemical EOR is discussed. Finally, the experimental and laboratory studies of the newly devised EOR technique are outlined.
An oil reservoir exists at a specific temperature, salinity, and pH. The prevailing conditions of the reservoir influence the efficiency of the injected chemicals and consequently of the EOR process [13]. Most injected chemicals degrade and become unstable at high salinity, elevated temperature, and low pH conditions [14]. For polymers, under saline conditions, screening of the charged polymer molecules by cations contained in the reservoir brine occurs. This reduces the hydrodynamic radius and polymer chain entanglement causing the contraction of the macromolecules that ultimately results in the loss of polymer solution viscosity [15, 16]. Meanwhile, high temperature causes hydrolysis of the polymer and its precipitation in the presence of divalent ions [17]. In the case of surfactant and alkali solutions, depending on the rock type, precipitation of the chemicals occurs in the presence of divalent cations [18]. Low pH reservoir conditions might interact and acidify injected chemical solutions [15].
Depending on the type of chemical injected into the reservoir, adsorption and retention of chemical occur during flow through porous media, which negatively affects the efficiency of the EOR process [19]. Chemicals react with the rock surface through electrostatic attraction, steric interaction, and van der Waal forces that reduces the concentration of the injected chemical solutions. Adsorption is prevalent for surfactant and alkali chemicals, while polymer is mainly retained due to mechanical entrapment because of the size of the polymer macromolecules [3, 18, 20]. The adsorption process occurs when the interface is energetically favored by the surfactant and/or alkali in comparison to the bulk phase. Thus, the adsorption at the solid–liquid interface takes place by the transfer of the molecule of the chemical to the solid–liquid interface from the bulk solution phase [21]. Meanwhile, polymer retention and inaccessible pore volume dictates the propagation of polymer flow in the reservoir [22]. Retention of polymer is alluded to any mechanism that leads to reduction or removal of polymer molecules from transported aqueous phase. The nature of polymer retention in reservoir rock is depicted in Figure 2. Overall, adsorption and/or retention of chemicals in porous media governs the efficiency and economic viability of the EOR process. Several factors affecting adsorption or retention of chemical EOR includes; electrolyte concentration (salinity), temperature, pH, composition of reservoir fluids, and the presence of clay mineral content [21, 23].
Retention of polymers in porous media. Sourced from [19].
Nanotechnology application in chemical EOR is used to overcome the shortcomings and improve the process efficiency of chemical EOR methods. Though most works are still at the laboratory scale, the synergic application of nanoparticles and chemicals have led to the formation of novel nanomaterials with exceptional qualities [6]. Recently, field trials have been reported in Columbia oilfield [24]. Depending on the nanoparticle type and chemical used, the formulated nanomaterials have demonstrated better stability and superior quality which enhances their performance during simulated reservoir conditions. So far, the most common nano-chemical studies are polymeric nanofluids and surfactant nanofluids.
Surfactant nanofluid, a combination of nanoparticle and surfactant, increases the microscopic displacement efficiency through the mechanisms of IFT reduction and wettability alteration [11, 25, 26]. This nanofluid could be used for the generation or formation of stable foams and emulsions in the reservoir. Stable foams ensure fluid diversion from thief zones to lower permeability regions in the reservoir, while emulsions ensure conformance efficiency of the injectant [27, 28]. Furthermore, surfactant nanofluids have been reported to have lower adsorption onto rock surface compared to ordinary surfactant solutions [29, 30].
IFT and wettability are major parameters for quantifying fluids distribution and movement in the reservoir [31]. After secondary oil recovery, a portion of the oil is trapped in the reservoir due to capillary forces. This capillary force is measured by a dimensionless capillary number defined as [32]:
Where μ is the displacing fluid viscosity, v is the displacing Darcy velocity, θ is the contact angle, and σ is the IFT between the displacing fluid (water) and the displaced fluid (oil).
Driven primarily by electrostatic interaction, the surfactant adsorbs on the nanoparticles surface forming surfactant-coated nanoparticles [11]. Nonetheless, the relative concentration of nanoparticles and surfactant in the solution determines the properties of the mixture. A lower concentration ratio of surfactant to nanoparticle in the mixture means that only a small fraction of the nanoparticle surface will be coated by surfactant. Conversely, a higher concentration ratio of surfactant to nanoparticles implies the surfactant molecules will form a bilayer on the particle surface [11, 34]. A single-chain surfactant on nanoparticle is required to form maximum nanoparticle flocculation and hydrophobic nature required for an optimal performance.
To quantify the performance of surfactant nanofluid on IFT of o/w interface, Le et al. evaluated the impact of silica (SiO2) nanoparticles and anionic surfactant for IFT reduction using a spinning drop tensiometer. Their results indicated that at a total concentration of 1000 ppm and at a surfactant to SiO2 ratio of 8:2, a four-fold IFT reduction was achieved by the nanosurfactant. Hence, they proposed the application of surfactant nanofluids for EOR in high temperature and high salinity (HTHS) conditions [35]. Mohajeri et al. evaluated the effect of zirconium oxide (ZrO2) nanoparticles on anionic sodium dodecyl sulfate (SDS) surfactant and cationic cetyltrimethylammonium bromide (CTAB) surfactant [25]. They reported that the contribution of ZrO2/SDS yielded an IFT reduction of 81% while ZrO2/CTAB decreased the IFT of o/w interface by 70%. Zargartalebi et al. probed the effect of SiO2 nanoparticles and anionic SDS to quantify the effect of the nanoparticle on IFT, adsorption and oil recovery potential of the surfactant molecules. They observed that nanoparticles effectively improve surfactant performance by enhancing the governing mechanism. Furthermore, flooding results shows that oil recovery increased significantly due to the inclusion of nanoparticles in the surfactant solution [26].
The mechanisms of nanosurfactant for reducing IFT at o/w interface has been explored. Researchers noted that the adsorption of the surfactant on the nanoparticle surface occurs as a result of the mix, leading to a hydrophobic character of the nanoparticle surface. Due to their Brownian motion, the nanoparticle acts as carriers for the surfactant molecules from the bulk of the fluid to the interface. At the interface, the minimization of the interfacial energy by the nanosurfactant leads to IFT reduction. As compared to ordinary surfactant whose molecule desorbs from the interface after some time, the nanoparticle prevents desorption of surfactant molecules from the interface, hence, better IFT reduction [11].
The reduction of interfacial energy at the rock/oil/brine interface by nanosurfactant also results in higher wettability alteration. Besides, the relative permeability curves of oil and water also changes after contact with the surfactant nanofluid; the relative permeability to water and oil decreases and increases respectively [34]. Mohajeri et al. studied the effect of ZrO2/surfactants on wettability alteration in a fractured micromodel. The sessile drop experiments and wettability alteration measurements showed that coating the micromodel with heavy oil makes an oil-wet surface. Moreover, coating of the oil-wet micromodel with surfactant or nanoparticle altered the wettability of the surface to water-wet condition, while coating the surface with the blend ZrO2/surfactant altered the wettability to strongly water-wet condition [25].
Additionally, the use of nanosurfactants as wettability alteration agents have proved useful for improving oil recovery from carbonates reservoir, which are characterized by poor oil recovery owing to its inherent natural fractures and hydrophobic nature that makes water imbibition into its rock matrix difficult, because of capillary pressure effects. Nwidee et al. assessed the effect of nanosurfactant formulation for wettability alteration of oil-wet limestone over a wide range of temperatures (0–70
Surfactant nanofluids have also been used to improve wettability alteration of sandstone cores to boost oil recovery. Giraldo et al. tested alumina-surfactant nanofluid to improve oil recovery in sandstone cores via wettability alteration using contact angle and imbibition tests. Their results show that the effectiveness of surfactant as wettability modifier was improved with the addition of 100 ppm of alumina nanoparticles. Additionally, the effective oil permeability increased by 33%, and consequently, a higher oil recovery was recorded [37]. Huibers et al. measured changes in wettability of sandstone cores of saturated with light and heavy crude oil using surfactant nanofluid composed of SiO2 nanoparticle and Tween 20 nonionic surfactant in Berea and Boise sandstone cores. Using direct imaging and contact angle measurements, 0.001 wt.% SiO2 nanoparticles yielded an increase in contact angle of 101.6% for light oil saturated cores, while the optimum concentration for heavy oil was not ascertained at the nanoparticle concentration range investigated [38].
One of the major challenges of surfactant EOR is the loss of surfactant molecules to adsorption onto the formation rock during the flooding process. Surfactant adsorption can make the chemical EOR process economically unfeasible. Therefore, reducing the surfactant adsorption improves the oil recovery process. Previous studies have investigated the use of polymers such as sodium polyacrylate as sacrificial agent to reduce surfactant adsorption during flow in porous media [39]. Recently, the adsorption reduction effect of nanoparticles has been investigated during the co-injection of nanoparticles with surfactant for oil recovery. Nanoparticles showed good potential for inhibiting surfactant adsorption via competitive adsorption mechanism by blocking the active site of the porous media while the surfactant flows through the porous media contacting the resident fluids in the reservoir. Yekeen et al. observed that the presence of SiO2 and Al2O3 nanoparticles decreased surfactant adsorption on kaolinite in the presence of reservoir brines. The addition of Al2O3 nanoparticles reduced the SDS adsorption on kaolinite by 38%, while the addition of SiO2 nanoparticles reduced the SDS adsorption by 75% [40].
Wu et al. conducted static and dynamic adsorption experiments to investigate the inhibition mechanism of SiO2 nanoparticle during co-injection with surfactant. An optimum aging time, solid–liquid ratio, nanoparticle concentration, and surfactant concentration were determined for the adsorption process. Static adsorption experiments showed that 0.5 wt.% of SiO2 nanoparticle concentration reduced the adsorption of SDS from 2.84 to 1.61 mg/g. Dynamic adsorption experiments conducted at 20
Foams used for oil recovery are generated by co-injecting a gas (e.g., carbon dioxide, nitrogen or air) and a foaming agent containing liquid into the reservoir [41]. In the porous media, foams act as a dispersion of gas in liquid separated by a lamella, with the gas phase residing in the upper side while the bulk liquid is located at the bottom of the foam structure [42]. They perform two diverse roles in the reservoir namely; (1) mobility control, (2) fluid diversion. These mechanisms aid foam to overcome the challenges of gas EOR such as gravity override and viscous fingering phenomena. The liquids used as conventional foaming agents includes surfactants, polymers, and proteins. When used with polymers, foams are used to plug high permeability areas, while the polymer is diverted to lower permeability regions, thus, improving the volumetric sweep efficiency of the reservoir. In the case of surfactant-stabilized foams, a stable foam is formed due to a decrease in the required energy to form the gas–liquid interface [43]. Moreover, the synergic combination with surfactant lowers the interfacial tension of the capillary trapped oil, hence, facilitates oil displacement [44, 45]. Conventional foams have been shown to be thermodynamically unstable in the presence of oil and resident reservoir brines. This implies that the foam coalesces leading to of the reduced efficacy of the process. The addition of nanoparticles to the surfactant solution seems to generate more stable foams with longer half-life and ability to withstand harsh reservoir conditions [43]. Due to the solid nature of nanoparticles, the foams they stabilize are highly resistant to unfavorable reservoir conditions. Nanoparticles adsorb at the lamellae interface of the foam with a strong adhesion energy that makes their attachment irreversible (see Figure 3) [41, 46].
Foams stabilized (a) without nanoparticles showing signs of foam drainage, (b) with nanoparticles stabilizing the lamellae [46].
Sun et al. studied the influence of nanoparticles on the generation, propagation, and stability of SiO2/SDS-stabilized foam in micromodels and sandpack porous media [47]. In the case of the SDS-stabilized foam, the shape of the oil droplet could not be changed by the foam because the microforce acting on the oil droplet was small. This subsequently leads to bubbles rupture and coalescence leaving a substantial amount of oil trapped in the porous media. In the case of SiO2/SDS foam, a large amount of oil was displaced by the foam due to the higher microforce acting on the oil droplet. The higher microforce was attributed to the enhanced viscoelasticity of the bubble surface by the attached nanoparticles. Yekeen et al. studied the influence of SiO2 and Al2O3 nanoparticles on surfactant-foam stability and propagation in the presence of oil. They noted that the presence of nanoparticle increases foam half-life. Additionally, the SiO2-SDS and Al2O3-SDS foam achieved nearly 100% microscopic efficiency even in the presence of oil. Finally, they identified mechanisms of foam flow as lamellae division and bubble-to-multiple bubble lamellae division, while the dominant mechanism of oil displacement and residual oil saturation are direct displacement and emulsification of oil [40]. Tables 1 and 2 summarizes laboratory and experimental results of nanoparticles-stabilized and nanoparticle-surfactant stabilized foams.
Nanoparticle | Surfactant | NP conc. (wt.%) | Surfactant conc. | Base fluid | Oil type | Porous media type | Mechanism of recovery | RF | Ref. |
---|---|---|---|---|---|---|---|---|---|
SiO2 | SDS | 0.1–0.5 | 0.2 wt.% | Deionized water | Crude oil | Quartz sand | IFT, competitive adsorption | 4.68% IO | [29] |
SiO2 | Alfoterra, Soloterra | 0.1–0.8 | 0.005–0.2 wt.% | Brine | Crude oil | Dolomite, Limestone | IFT, WA | 37–45% OOIP | [48] |
SiO2 | TX-100 | 0.1 | 0.1 wt.% | Brine | Crude oil + kerosene | Sandstone | IFT, WA | 8% IO | [49] |
SiO2 | CTAB | 0.05–0.5 | 0.1 wt.% | Brine | Heavy oil | Micromodel | ES | 17.4–38% OOIP | [50] |
SiO2 | SDS | 0.25 | 1 wt.% | Brine | Heavy oil | Mircomodel | IFT, ES | 5% IO | [51] |
SiO2 | Non-ionic Tween 20 | 2–4 | 0.74 wt.% | Deionized water | Heavy oil | Micromodel | IFT, ES | 18–39% | [52] |
SiO2 | CTAB | 0–5 | 0.09 mM | Distilled water | Heptane | — | IFT | — | [53] |
Hydrophilic and hydrophobic SiO2 | SDS | 0.1 | 0.01–0.6 wt.% | Deionized water | — | Sandstone | IFT, Adsorption reduction | — | [54] |
Non-ferrous metal | Sulphanole | 0.001 | 0.0078–0.05 wt.% | — | Heavy oil | — | IFT, WA | 12–22% IO | [55] |
Al2O3 | PRNS | 0.001–1 | Distilled water | Heavy oil | Sandstone | WA | 33% IO | [37] | |
Fumed SiO2 Hydrophobic SiO2 | Zyziphus Spina Christi | 0.05–0.2 | 0.1–8 wt.% | Deionized water | — | Shale sandstone | Adsorption reduction | — | [56] |
ZrO2 | SDS, CTAB | 0.01 | 0.1–0.4 wt.% | Distilled water | Heavy oil | Micromodel | IFT, WA | — | [25] |
ZrO2, NiO | TX-100, CTAB | 0.004–0.05 | 0.1–3.2 wt.% | Deionized water | — | Limestone | WA | — | [36] |
SiO2 | SDS, PAM | 0.5–2.0 | 0.14 wt.% | Deionized water | Medium oil | Sandstone | IFT, WA | 60% OOIP | [57] |
Laboratory results of oil recovery applications by nanosurfactant.
Ref. | NP type | NP size (nm) | NP Conc. | Surfactant | Temperature | Pressure | Salinity | Foam generator | Oil recovery |
---|---|---|---|---|---|---|---|---|---|
[58] | SiO2, Al2O3, CuO, TiO2 | 10–40 | 0.002–0.1 wt.% | — | 27 | — | NaCl (0.3 wt%) | Sandpack | 5.1–17.4% OOIPa |
[59] | PEG coated-SiO2 | 5 | 0.01–0.1 wt.% | — | 21.1–90 | 1350–1400 psia | NaCl (2–4 wt.%) | Glass beads pack, Capillary tube | — |
[60] | SiO2 | 100–150 | 0 – 5 wt.% | — | 25 | 1200 – 2000psia | NaCl (0.5, 2.0, 5.0%) | Sapphire observation tube | — |
[61] | AlOOH | 10–100 | 1 wt.% | SC (0–100 mM) | 60 | 6 mPa | NaCl (10–600 mM), CaCl2 (10–200 mM) | Sanpack | |
[62] | SiO2 | 17 | 0.01–0.5 wt.% | — | 25 | 1200 psig, 1500 psig | NaCl (2.0%) | Berea sandstone core | — |
[63] | SiO2 | 100–200 | 0.05–3.0% w/v | PEG, Tergitol 15-S-20, DCDMS | 35 | 1200–3000 psia | — | Glassbead pack | — |
[64] | APTES – SiO2 | 20–30 | 0.01 wt.% | SDS (0.4 wt.%) | 25 | 14.7 psi | — | Glassbead pack | 18% OOIPa |
[65] | PECNP | — | 1.0 wt.% | Surfonic N120 | 40 | 1300 psi, 1800 psi | KCl (2.0 wt.%) | Indiana limestone | 10.71% OOIPb |
[66] | TTFA | 80 | 0.5 wt.% | Cationic, anionic and non-ionic surfactant (0.2 wt.%) | 25 | 1300 psi (backpressure) | NaCl (1.0 wt.%) | Berea sandstone | — |
[67] | PEG coatedSiO2 | 10 (20) | 0.5 wt.% | AOS (0–0.5 wt.%) | 25 | 100 psi (backpressure) | NaCl (1–10 wt.%), API Brine | Berea sandstone | 10% OOIPa |
[68] | SiO2, Al2O3, CuO, TiO2 | 10–40 | 0.1–1.0 wt.% | AOS (O.5 wt.%) | Room temperature | — | NaCl (2 wt.%) | Sandpack models | 5–14% OOIPa |
[69] | FA | 100–200 | < 0.05 wt.% | AOS (0.0315 wt.%) | — | — | NaCl (1.0–5.0 wt.%), CaCl2 (0–9.5 wt.%) | Bentheimer sandstone | — |
[70] | SiO2 | 5, 12, 25, 80 | 0.5–10 wt.% | — | 70 | 2200 psi | NaCl (8.0 wt.%), CaCl2 (2.0 wt.%) | Biose sandstone, Sandpack | — |
[71] | Al2O3 – coated SiO2 | 20 | 1–5 wt.% | Triton CG-110 AOS, PG (0.1–0.5 wt.% | Room temperature | 100 psi (backpressure) | — | Berea sandstone | 14.8–20.6% OOIPa |
[72] | MWCNT | 10 | 0.01 wt.% | Tergitol 15-s-40, AOS | 25 | — | NaCl (2.4 wt.%), CaCl2 (0.6 wt.%) | Ottawa sandpack | — |
[73] | PEG coated SiO2 | 5 (10) | 0.3 wt.% | AOS (0.5 wt.% | 55, 75 | 110 psi (backpressure) | NaCl (1–8 wt.%) | Heterogeneous sandpack | 34.4% OOIPa 9% OOIPb |
[46] | SiO2 Al2O3 | 12–20 | 0.05–5.0 wt% | SDS (0.03 wt.%) | 25 | — | NaCl (0.5 wt.%) | Hele-shaw cell | — |
[74] | PEG-SiO2, GLYMO-SiO2 | 12, 20 | 0.5 wt.% | AOS | 25, 60, 80 | 110 psi (backpressure) | NaCl (8 wt.%), CaCl2 (2 wt.%) | Sandpack | 29.0–43.3% OOIPa |
Laboratory and experimental investigation of nanoparticle/nanoparticle-surfactant stabilized foams.
aIncremental oil recovery over waterflood.
bIncremental oil recovery over surfactant-stabilized foam.
On the other hand, the interactions of surfactants with oil during flow through porous media may generate emulsions. Emulsions generated in situ have potential for mobility and conformance control in the reservoir, which are desirable properties for improving the oil recovery process. Further, the feasibility of injecting emulsions has also been explored, exhibiting appropriate potential for oil recovery. Nonetheless, conventional emulsions show poor stability at high pressure and high temperature conditions. As temperature increases, the average droplet size of the dispersed phase increases which eventually plug pore throats in the reservoir [75]. Recently, the binary mix of nanosurfactant with oil have been evaluated for emulsion generation showing better stability performance in the reservoir for oil recovery applications. Besides, the presence of nanoparticle significantly improved the stability and mobility of the emulsions.
Pei et al. investigated the synergetic effect of SiO2 nanoparticle and CTAB for o/w emulsions applications. Phase behavior testing, rheology evaluation, and micro-visualization studies showed that nano-surfactant-stabilized emulsion demonstrated a high bulk viscosity and desirable mobility for recovering heavy oil [50]. Kumar et al. synthesized a Pickering emulsion stabilized by SiO2 nanoparticle and sodium dodecylbenzene sulfonate (SDBS) surfactant. The synthesized Pickering emulsion displayed better thermal stability at the high pressure (0–5 MPa) and high temperature (30–100
Depending on the method of preparation, polymeric nanofluids are categorized into two types; polymer-coated nanoparticles and polymer nanoparticles. Polymer-coated nanoparticles were developed due to overcome the aggregation and agglomeration problems of nanoparticles at reservoir conditions. It involves grafting polymers onto the surface of nanoparticles to improve dispersibility. In addition, their properties can be customized for particular applications [34]. Meanwhile, polymer nanoparticles are prepared by the hybrid dispersion of nanoparticles in polymer solutions. These polymer nanoparticles emerged as a means of inhibiting polymer degradation in typical reservoir conditions [4]. The mechanisms of polymeric nanofluids performance during EOR applications include improved rheology and stability, wettability alteration, and lower polymer adsorption [6].
Rheology is defined as the study of flow and deformation behaviors of fluids under stress [76]. For EOR applications, an improved rheological behavior of injectant is required to inhibit viscous fingering phenomena and maintain a suitable mobility ratio in the reservoir; which requires that the displacing fluid maintain its viscosity and chemical integrity in the presence of resident reservoir brines [77]. Polymer and nanoparticles undergo degradation in the presence of reservoir brines. The cations present in the brine interact with the carboxylate and amide groups in the polymer molecule resulting in viscosity loss [78]. In the case of nanoparticles, the electrostatic attraction among nanoparticles are increased in the presence of brine fostering their aggregation and agglomeration; which implies the loss of surface functionality that is required for EOR [79]. However, the combination of polymer and nanoparticles results in a synergistic effect that improves the rheology of the polymer and the stability of the nanoparticle [4].
The preparation of polymer-nanoparticles blends involves the mixing of the nanoparticle and the polymer solution or grafting of the polymer on the nanoparticle [80, 81]. Subsequently, interactions occur between the nanoparticle and the carboxylate and amide group in the polymer molecules. Therefore, nanoparticles act as physical crosslinkers among the polymer chains forming three-dimensional network of stable flocs that increases the viscosity of the suspension [82]. At high temperature, polymer-nanoparticles blends exhibit better rheological performance due to the enhanced bridging induced flocculation [82, 83]. Furthermore, in the presence of reservoir brines, nanoparticles shield the polymer backbone from the cations of the brine by inducing ion-dipole interactions that inhibit the degradation of the polymer molecules [81].
Lai et al. noted that the shear and mechanical resistance of acrylamide polymer solution can be increased by adding modified nano-SiO2, because the presence of SiO2-NP caused a reduction of the hydrodynamic radius of the polymer molecules [84]. Hu et al. studied the rheological properties on an oilfield polyacrylamide (HPAM) -SiO2 NP under different aging times, salinity, and temperature conditions. The results demonstrated that the presence of the SiO2-NP significantly improved the viscosity and viscoelastic properties of the HPAM under high temperature and high salinity (HTHS) conditions [80]. Haruna et al. grafted HPAM molecules with graphene oxide (GO) nanosheets and evaluated the rheological and stability properties of the formulated polymeric nanofluid. They reported enhancement of the suspension viscosity behavior, as well as high-temperature stability and improved elastic properties of the dispersion [85].
As for polymer-coated nanoparticles, depending on the grafting method, the polymeric chains protrude from the nanoparticle surface. Hence, hydrodynamic interactions occur between the grafted nanoparticle when subjected to shear. Besides, polymeric chains grafted on the surface of the nanoparticle overlap with another polymer chain adsorbed on another nanoparticle. The overlapping of several grafted nanoparticles results in the strengthening of the network structure of the polymer -nanoparticle system. Consequently, hydro clusters are formed, which results in an increase of stability and viscosity [86]. Liu et al. grafted a layer of amphiphilic-polymeric chains on nano-SiO2 core shell via a facile water-free radical polymerization and evaluated its rheological properties and oil recovery performance. The synthesized polymer-coated nanoparticle formed a three-dimensional microstructure and intermolecular associations characterized by long-term stability and better rheological properties than the individual polymer or nanoparticles. Furthermore, a 20% incremental oil recovery was recorded after flooding the polymer-coated nanoparticle solution at a concentration of 1500 mg/L in sandstone cores [87]. Table 3 summarizes some laboratory and experimental studies of improved rheological properties and oil displacement properties of polymeric nanofluids.
References | NP type | Polymer/copolymer type | PNF conc. (ppm) | Brine/conc. | Temp. (°C) | Porous media type | Incremental oil recovery (%) |
---|---|---|---|---|---|---|---|
[88] | SiO2 | PEOMA | 10,000 | 1.0 wt.% NaCl | 30 | Berea sandstone | 19.5 |
[89] | SiO2 | AMPS | 50,000 | — | 80 | Quartz sand | 23.22 |
[90] | SiO2 | PEG | 10,000 | — | 80 | Glass micromodel | 20.0 |
[87] | SiO2 | MeDiC8AM | 1500 | 12 wt.% (NaCl & CaCl2) | 82.3 | Sandstone | 20.0 |
[91] | SiO2 | AMC12S | 1100 | 18 wt.% | 110 | Sandstone | 24.0 |
[92] | SiO2 | AA/AM | 2000 | 2 wt.% NaCl, 0.18 wt.% CaCl2 | 65 | Sandstone | 20.1 |
[93] | SiO2 | AM/AA | 1500 | — | — | — | 18.84 |
[94] | SiO2 | HPAM | 1000 | 2.4 wt.% (NaCl, CaCl2, MgCl2) | 25 | Glass micromodel | 10.0 |
[95] | SiO2 | HPAM | 800 | 3 wt.% NaCl | — | Glass micromodel | 10.0 |
[76] | MMT clay | HPAM | 1000 | 10 wt.% (NaCl, CaCl2, MgCl2) | 90 | Quartz sand | 33.0 |
Laboratory results of oil recovery applications by polymeric nanofluid [6].
Polymeric nanofluids also show reduced adsorption onto porous media due to the synergic interaction between the polymer and nanoparticles. Foster et al. used the grafting through approach to tether tuneable quantities of poly(2-acrylamido-2-methylpropanesulfonic acid) (PAMPS) and poly([3-(methacryloxylamino)propyl]dimethyl(3-sulfopropyl)ammoniumhydroxide)(PMPDSA) homopolymer (PMPDSA) onto iron oxide nanoparticle surfaces. Steric stabilization of the synthesized polymer-coated nanoparticle was observed which remained stable at HTHS conditions. Moreover, adsorption experiments on crushed Berea sandstone cores showed that the adsorption of polymer-coated iron oxide nanoparticles was infinitesimal and almost negligible [96]. Cheraghian et al. performed static adsorption experiments to investigate the impact of nano-SiO2 and nanoclay on the adsorption inhibition of polyacrylamide onto sandstone rocks. Polymer nanoparticles containing SiO2 nanoparticle showed lower adsorption onto sandstone rock surface compared to the polymer containing nanoclay [97].
Wettability alteration plays a vital role in enhancing the microscopic displacement efficiency. In the case of polymeric nanofluids, an interplay of electrostatic repulsive forces occur at the interface of the nanoparticles., Two-dimension layered structure of nanoparticles occur due to Brownian motion when brought into contact with an oil-wet solid surface, creating a wedge film because of the ordering of nanoparticles at the three-phase (solid-oil–water) contact region. This results in an increase of the disjoining pressure,which causes the spreading of the nanofluid phase at the wedge of the vertex, altering the wettability of the surface [6]. Maurya et al. grafted polyacrylamide on the surface of SiO2 using the free radical polymerization approach and investigated its wettability potential on an oil-wet sandstone rock surface. They indicated that the polymer grafted nanoparticle altered the wettability of the sandstone surface to a more water-wet condition [86]. Maghzi et al. performed wettability alteration studies employing polymer nanoparticles consisting of SiO2 nanoparticle and polyacrylamide polymer solution in a five-spot glass micromodel. The polymer nanoparticle altered the surface of the micromodel from an average contact angle of 112
This chapter summarizes some of the recent advances in the application of nanotechnology in chemical EOR processes to boost oil production. The mechanisms of oil recovery through nanotechnology were reviewed. Several experimental studies were summarized and discussed. Results of various experiments shows that the incorporation of nanotechnology with chemical EOR shows good potential to improve pore scale mechanisms in the case of surfactant. Adsorption of surfactant on rock pores is inhibited while greater IFT reduction and better wettability alteration were achieved. Furthermore, nanotechnology improved the rheological properties of polymer and stability of emulsions and foams indicating the good potentials of improving sweep efficiency of injected chemicals especially in the presence of harsh reservoir conditions. Finally, future research should focus on modeling the flow behavior of nanomaterials through porous media, which is required for the designing and field implementation of nano-chemicals EOR.
AA | acrylic acid |
AlOOH | aluminum hydroxide |
AM | acrylamide |
AMPS | 2-acrylamido-2-methyl-1-propanesulfonic acid |
AMC12S | 2-acrylamido-dodecylsulfonate |
APTES | (3-aminopropyl)triethoxysilane |
AOS | alpha olefin sulfonate |
CaCl2 | calcium chloride |
CuO | copper oxide |
DCDMS | dichlorodimethylsilane |
ES | emulsion stability |
FA | fly ash |
GLYMO | (3-glycidyloxypropyl)trimethoxysilane |
HPAM | hydrolysed polyacrylamide |
IO | incremental oil |
KCl | potassium chloride |
PAM | polyacrylamide |
PECNP | polyelectrolyte composite nanoparticle |
PEG | polyethylene glycol |
PEOMA | poly(oligo(ethylene oxide) mono methyl ether methacrylate) |
MeDiC8AM | 2-methyl-N,N-dioctyl-acrylamide |
MWCNT | multiwall carbon nanotube |
MgCl2 | magnesium chloride |
MMT | montmorillonite |
NaCl | sodium chloride |
NiO | nickel oxide |
NP | nanoparticle |
OOIP | original-oil-in-place |
RF | recovery factor |
SC | sodium cumenesulfonate |
TTFA | thermally treated fly ash |
WA | wettability alteration |
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\n'}]},successStories:{items:[]},authorsAndEditors:{filterParams:{sort:"featured,name"},profiles:[{id:"105746",title:"Dr.",name:"A.W.M.M.",middleName:null,surname:"Koopman-van Gemert",slug:"a.w.m.m.-koopman-van-gemert",fullName:"A.W.M.M. Koopman-van Gemert",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/105746/images/5803_n.jpg",biography:"Dr. Anna Wilhelmina Margaretha Maria Koopman-van Gemert MD, PhD, became anaesthesiologist-intensivist from the Radboud University Nijmegen (the Netherlands) in 1987. She worked for a couple of years also as a blood bank director in Nijmegen and introduced in the Netherlands the Cell Saver and blood transfusion alternatives. She performed research in perioperative autotransfusion and obtained the degree of PhD in 1993 publishing Peri-operative autotransfusion by means of a blood cell separator.\nBlood transfusion had her special interest being the president of the Haemovigilance Chamber TRIP and performing several tasks in local and national blood bank and anticoagulant-blood transfusion guidelines committees. Currently, she is working as an associate professor and up till recently was the dean at the Albert Schweitzer Hospital Dordrecht. She performed (inter)national tasks as vice-president of the Concilium Anaesthesia and related committees. \nShe performed research in several fields, with over 100 publications in (inter)national journals and numerous papers on scientific conferences. \nShe received several awards and is a member of Honour of the Dutch Society of Anaesthesia.",institutionString:null,institution:{name:"Albert Schweitzer Hospital",country:{name:"Gabon"}}},{id:"83089",title:"Prof.",name:"Aaron",middleName:null,surname:"Ojule",slug:"aaron-ojule",fullName:"Aaron Ojule",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Port Harcourt",country:{name:"Nigeria"}}},{id:"295748",title:"Mr.",name:"Abayomi",middleName:null,surname:"Modupe",slug:"abayomi-modupe",fullName:"Abayomi Modupe",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/no_image.jpg",biography:null,institutionString:null,institution:{name:"Landmark University",country:{name:"Nigeria"}}},{id:"94191",title:"Prof.",name:"Abbas",middleName:null,surname:"Moustafa",slug:"abbas-moustafa",fullName:"Abbas Moustafa",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/94191/images/96_n.jpg",biography:"Prof. Moustafa got his doctoral degree in earthquake engineering and structural safety from Indian Institute of Science in 2002. He is currently an associate professor at Department of Civil Engineering, Minia University, Egypt and the chairman of Department of Civil Engineering, High Institute of Engineering and Technology, Giza, Egypt. He is also a consultant engineer and head of structural group at Hamza Associates, Giza, Egypt. Dr. Moustafa was a senior research associate at Vanderbilt University and a JSPS fellow at Kyoto and Nagasaki Universities. He has more than 40 research papers published in international journals and conferences. He acts as an editorial board member and a reviewer for several regional and international journals. His research interest includes earthquake engineering, seismic design, nonlinear dynamics, random vibration, structural reliability, structural health monitoring and uncertainty modeling.",institutionString:null,institution:{name:"Minia University",country:{name:"Egypt"}}},{id:"84562",title:"Dr.",name:"Abbyssinia",middleName:null,surname:"Mushunje",slug:"abbyssinia-mushunje",fullName:"Abbyssinia Mushunje",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"University of Fort Hare",country:{name:"South Africa"}}},{id:"202206",title:"Associate Prof.",name:"Abd Elmoniem",middleName:"Ahmed",surname:"Elzain",slug:"abd-elmoniem-elzain",fullName:"Abd Elmoniem Elzain",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Kassala University",country:{name:"Sudan"}}},{id:"98127",title:"Dr.",name:"Abdallah",middleName:null,surname:"Handoura",slug:"abdallah-handoura",fullName:"Abdallah Handoura",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"École Supérieure des Télécommunications",country:{name:"Morocco"}}},{id:"91404",title:"Prof.",name:"Abdecharif",middleName:null,surname:"Boumaza",slug:"abdecharif-boumaza",fullName:"Abdecharif Boumaza",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"Abbès Laghrour University of Khenchela",country:{name:"Algeria"}}},{id:"105795",title:"Prof.",name:"Abdel Ghani",middleName:null,surname:"Aissaoui",slug:"abdel-ghani-aissaoui",fullName:"Abdel Ghani Aissaoui",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/105795/images/system/105795.jpeg",biography:"Abdel Ghani AISSAOUI is a Full Professor of electrical engineering at University of Bechar (ALGERIA). He was born in 1969 in Naama, Algeria. He received his BS degree in 1993, the MS degree in 1997, the PhD degree in 2007 from the Electrical Engineering Institute of Djilali Liabes University of Sidi Bel Abbes (ALGERIA). He is an active member of IRECOM (Interaction Réseaux Electriques - COnvertisseurs Machines) Laboratory and IEEE senior member. He is an editor member for many international journals (IJET, RSE, MER, IJECE, etc.), he serves as a reviewer in international journals (IJAC, ECPS, COMPEL, etc.). He serves as member in technical committee (TPC) and reviewer in international conferences (CHUSER 2011, SHUSER 2012, PECON 2012, SAI 2013, SCSE2013, SDM2014, SEB2014, PEMC2014, PEAM2014, SEB (2014, 2015), ICRERA (2015, 2016, 2017, 2018,-2019), etc.). His current research interest includes power electronics, control of electrical machines, artificial intelligence and Renewable energies.",institutionString:"University of Béchar",institution:{name:"University of Béchar",country:{name:"Algeria"}}},{id:"99749",title:"Dr.",name:"Abdel Hafid",middleName:null,surname:"Essadki",slug:"abdel-hafid-essadki",fullName:"Abdel Hafid Essadki",position:null,profilePictureURL:"//cdnintech.com/web/frontend/www/assets/author.svg",biography:null,institutionString:null,institution:{name:"École Nationale Supérieure de Technologie",country:{name:"Algeria"}}},{id:"101208",title:"Prof.",name:"Abdel Karim",middleName:"Mohamad",surname:"El Hemaly",slug:"abdel-karim-el-hemaly",fullName:"Abdel Karim El Hemaly",position:null,profilePictureURL:"https://mts.intechopen.com/storage/users/101208/images/733_n.jpg",biography:"OBGYN.net Editorial Advisor Urogynecology.\nAbdel Karim M. A. El-Hemaly, MRCOG, FRCS � Egypt.\n \nAbdel Karim M. A. El-Hemaly\nProfessor OB/GYN & Urogynecology\nFaculty of medicine, Al-Azhar University \nPersonal Information: \nMarried with two children\nWife: Professor Laila A. Moussa MD.\nSons: Mohamad A. M. El-Hemaly Jr. MD. Died March 25-2007\nMostafa A. M. El-Hemaly, Computer Scientist working at Microsoft Seatle, USA. \nQualifications: \n1.\tM.B.-Bch Cairo Univ. June 1963. \n2.\tDiploma Ob./Gyn. Cairo Univ. April 1966. \n3.\tDiploma Surgery Cairo Univ. Oct. 1966. \n4.\tMRCOG London Feb. 1975. \n5.\tF.R.C.S. Glasgow June 1976. \n6.\tPopulation Study Johns Hopkins 1981. \n7.\tGyn. Oncology Johns Hopkins 1983. \n8.\tAdvanced Laparoscopic Surgery, with Prof. Paulson, Alexandria, Virginia USA 1993. \nSocieties & Associations: \n1.\t Member of the Royal College of Ob./Gyn. London. \n2.\tFellow of the Royal College of Surgeons Glasgow UK. \n3.\tMember of the advisory board on urogyn. FIGO. \n4.\tMember of the New York Academy of Sciences. \n5.\tMember of the American Association for the Advancement of Science. \n6.\tFeatured in �Who is Who in the World� from the 16th edition to the 20th edition. \n7.\tFeatured in �Who is Who in Science and Engineering� in the 7th edition. \n8.\tMember of the Egyptian Fertility & Sterility Society. \n9.\tMember of the Egyptian Society of Ob./Gyn. \n10.\tMember of the Egyptian Society of Urogyn. \n\nScientific Publications & Communications:\n1- Abdel Karim M. El Hemaly*, Ibrahim M. Kandil, Asim Kurjak, Ahmad G. Serour, Laila A. S. Mousa, Amr M. Zaied, Khalid Z. El Sheikha. \nImaging the Internal Urethral Sphincter and the Vagina in Normal Women and Women Suffering from Stress Urinary Incontinence and Vaginal Prolapse. Gynaecologia Et Perinatologia, Vol18, No 4; 169-286 October-December 2009.\n2- Abdel Karim M. El Hemaly*, Laila A. S. Mousa Ibrahim M. Kandil, Fatma S. El Sokkary, Ahmad G. Serour, Hossam Hussein.\nFecal Incontinence, A Novel Concept: The Role of the internal Anal sphincter (IAS) in defecation and fecal incontinence. Gynaecologia Et Perinatologia, Vol19, No 2; 79-85 April -June 2010.\n3- Abdel Karim M. El Hemaly*, Laila A. S. Mousa Ibrahim M. Kandil, Fatma S. El Sokkary, Ahmad G. Serour, Hossam Hussein.\nSurgical Treatment of Stress Urinary Incontinence, Fecal Incontinence and Vaginal Prolapse By A Novel Operation \n"Urethro-Ano-Vaginoplasty"\n Gynaecologia Et Perinatologia, Vol19, No 3; 129-188 July-September 2010.\n4- Abdel Karim M. El Hemaly*, Ibrahim M. Kandil, Laila A. S. Mousa and Mohamad A.K.M.El Hemaly.\nUrethro-vaginoplasty, an innovated operation for the treatment of: Stress Urinary Incontinence (SUI), Detursor Overactivity (DO), Mixed Urinary Incontinence and Anterior Vaginal Wall Descent. \nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/ urethro-vaginoplasty_01\n\n5- Abdel Karim M. El Hemaly, Ibrahim M Kandil, Mohamed M. Radwan.\n Urethro-raphy a new technique for surgical management of Stress Urinary Incontinence.\nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/\nnew-tech-urethro\n\n6- Abdel Karim M. El Hemaly, Ibrahim M Kandil, Mohamad A. Rizk, Nabil Abdel Maksoud H., Mohamad M. Radwan, Khalid Z. El Shieka, Mohamad A. K. M. El Hemaly, and Ahmad T. El Saban.\nUrethro-raphy The New Operation for the treatment of stress urinary incontinence, SUI, detrusor instability, DI, and mixed-type of urinary incontinence; short and long term results. \nhttp://www.obgyn.net/urogyn/urogyn.asp?page=urogyn/articles/\nurethroraphy-09280\n\n7-Abdel Karim M. El Hemaly, Ibrahim M Kandil, and Bahaa E. El Mohamady. Menopause, and Voiding troubles. \nhttp://www.obgyn.net/displayppt.asp?page=/English/pubs/features/presentations/El-Hemaly03/el-hemaly03-ss\n\n8-El Hemaly AKMA, Mousa L.A. Micturition and Urinary\tContinence. Int J Gynecol Obstet 1996; 42: 291-2. \n\n9-Abdel Karim M. El Hemaly.\n Urinary incontinence in gynecology, a review article.\nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/abs-urinary_incotinence_gyn_ehemaly \n\n10-El Hemaly AKMA. Nocturnal Enuresis: Pathogenesis and Treatment. \nInt Urogynecol J Pelvic Floor Dysfunct 1998;9: 129-31.\n \n11-El Hemaly AKMA, Mousa L.A.E. Stress Urinary Incontinence, a New Concept. Eur J Obstet Gynecol Reprod Biol 1996; 68: 129-35. \n\n12- El Hemaly AKMA, Kandil I. M. Stress Urinary Incontinence SUI facts and fiction. Is SUI a puzzle?! http://www.obgyn.net/displayppt.asp?page=/English/pubs/features/presentations/El-Hemaly/el-hemaly-ss\n\n13-Abdel Karim El Hemaly, Nabil Abdel Maksoud, Laila A. Mousa, Ibrahim M. Kandil, Asem Anwar, M.A.K El Hemaly and Bahaa E. El Mohamady. \nEvidence based Facts on the Pathogenesis and Management of SUI. http://www.obgyn.net/displayppt.asp?page=/English/pubs/features/presentations/El-Hemaly02/el-hemaly02-ss\n\n14- Abdel Karim M. El Hemaly*, Ibrahim M. Kandil, Mohamad A. Rizk and Mohamad A.K.M.El Hemaly.\n Urethro-plasty, a Novel Operation based on a New Concept, for the Treatment of Stress Urinary Incontinence, S.U.I., Detrusor Instability, D.I., and Mixed-type of Urinary Incontinence.\nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/urethro-plasty_01\n\n15-Ibrahim M. Kandil, Abdel Karim M. El Hemaly, Mohamad M. Radwan: Ultrasonic Assessment of the Internal Urethral Sphincter in Stress Urinary Incontinence. The Internet Journal of Gynecology and Obstetrics. 2003. Volume 2 Number 1. \n\n\n16-Abdel Karim M. El Hemaly. Nocturnal Enureses: A Novel Concept on its pathogenesis and Treatment.\nhttp://www.obgyn.net/urogynecolgy/?page=articles/nocturnal_enuresis\n\n17- Abdel Karim M. El Hemaly. Nocturnal Enureses: An Update on the pathogenesis and Treatment.\nhttp://www.obgyn.net/urogynecology/?page=/ENHLIDH/PUBD/FEATURES/\nPresentations/ Nocturnal_Enuresis/nocturnal_enuresis\n\n18-Maternal Mortality in Egypt, a cry for help and attention. The Second International Conference of the African Society of Organization & Gestosis, 1998, 3rd Annual International Conference of Ob/Gyn Department � Sohag Faculty of Medicine University. Feb. 11-13. Luxor, Egypt. \n19-Postmenopausal Osteprosis. The 2nd annual conference of Health Insurance Organization on Family Planning and its role in primary health care. Zagaziz, Egypt, February 26-27, 1997, Center of Complementary Services for Maternity and childhood care. \n20-Laparoscopic Assisted vaginal hysterectomy. 10th International Annual Congress Modern Trends in Reproductive Techniques 23-24 March 1995. Alexandria, Egypt. \n21-Immunological Studies in Pre-eclamptic Toxaemia. Proceedings of 10th Annual Ain Shams Medical Congress. Cairo, Egypt, March 6-10, 1987. \n22-Socio-demographic factorse affecting acceptability of the long-acting contraceptive injections in a rural Egyptian community. Journal of Biosocial Science 29:305, 1987. \n23-Plasma fibronectin levels hypertension during pregnancy. The Journal of the Egypt. Soc. of Ob./Gyn. 13:1, 17-21, Jan. 1987. \n24-Effect of smoking on pregnancy. Journal of Egypt. Soc. of Ob./Gyn. 12:3, 111-121, Sept 1986. \n25-Socio-demographic aspects of nausea and vomiting in early pregnancy. Journal of the Egypt. Soc. of Ob./Gyn. 12:3, 35-42, Sept. 1986. \n26-Effect of intrapartum oxygen inhalation on maternofetal blood gases and pH. Journal of the Egypt. Soc. of Ob./Gyn. 12:3, 57-64, Sept. 1986. \n27-The effect of severe pre-eclampsia on serum transaminases. The Egypt. J. Med. Sci. 7(2): 479-485, 1986. \n28-A study of placental immunoreceptors in pre-eclampsia. The Egypt. J. Med. Sci. 7(2): 211-216, 1986. \n29-Serum human placental lactogen (hpl) in normal, toxaemic and diabetic pregnant women, during pregnancy and its relation to the outcome of pregnancy. Journal of the Egypt. Soc. of Ob./Gyn. 12:2, 11-23, May 1986. \n30-Pregnancy specific B1 Glycoprotein and free estriol in the serum of normal, toxaemic and diabetic pregnant women during pregnancy and after delivery. Journal of the Egypt. Soc. of Ob./Gyn. 12:1, 63-70, Jan. 1986. Also was accepted and presented at Xith World Congress of Gynecology and Obstetrics, Berlin (West), September 15-20, 1985. \n31-Pregnancy and labor in women over the age of forty years. Accepted and presented at Al-Azhar International Medical Conference, Cairo 28-31 Dec. 1985. \n32-Effect of Copper T intra-uterine device on cervico-vaginal flora. Int. J. Gynaecol. Obstet. 23:2, 153-156, April 1985. \n33-Factors affecting the occurrence of post-Caesarean section febrile morbidity. Population Sciences, 6, 139-149, 1985. \n34-Pre-eclamptic toxaemia and its relation to H.L.A. system. Population Sciences, 6, 131-139, 1985. \n35-The menstrual pattern and occurrence of pregnancy one year after discontinuation of Depo-medroxy progesterone acetate as a postpartum contraceptive. Population Sciences, 6, 105-111, 1985. \n36-The menstrual pattern and side effects of Depo-medroxy progesterone acetate as postpartum contraceptive. Population Sciences, 6, 97-105, 1985. \n37-Actinomyces in the vaginas of women with and without intrauterine contraceptive devices. Population Sciences, 6, 77-85, 1985. \n38-Comparative efficacy of ibuprofen and etamsylate in the treatment of I.U.D. menorrhagia. Population Sciences, 6, 63-77, 1985. \n39-Changes in cervical mucus copper and zinc in women using I.U.D.�s. Population Sciences, 6, 35-41, 1985. \n40-Histochemical study of the endometrium of infertile women. Egypt. J. Histol. 8(1) 63-66, 1985. \n41-Genital flora in pre- and post-menopausal women. Egypt. J. Med. Sci. 4(2), 165-172, 1983. \n42-Evaluation of the vaginal rugae and thickness in 8 different groups. Journal of the Egypt. Soc. of Ob./Gyn. 9:2, 101-114, May 1983. \n43-The effect of menopausal status and conjugated oestrogen therapy on serum cholesterol, triglycerides and electrophoretic lipoprotein patterns. Al-Azhar Medical Journal, 12:2, 113-119, April 1983. \n44-Laparoscopic ventrosuspension: A New Technique. Int. J. Gynaecol. Obstet., 20, 129-31, 1982. \n45-The laparoscope: A useful diagnostic tool in general surgery. Al-Azhar Medical Journal, 11:4, 397-401, Oct. 1982. \n46-The value of the laparoscope in the diagnosis of polycystic ovary. Al-Azhar Medical Journal, 11:2, 153-159, April 1982. \n47-An anaesthetic approach to the management of eclampsia. Ain Shams Medical Journal, accepted for publication 1981. \n48-Laparoscopy on patients with previous lower abdominal surgery. Fertility management edited by E. Osman and M. Wahba 1981. \n49-Heart diseases with pregnancy. Population Sciences, 11, 121-130, 1981. \n50-A study of the biosocial factors affecting perinatal mortality in an Egyptian maternity hospital. Population Sciences, 6, 71-90, 1981. \n51-Pregnancy Wastage. Journal of the Egypt. Soc. of Ob./Gyn. 11:3, 57-67, Sept. 1980. \n52-Analysis of maternal deaths in Egyptian maternity hospitals. Population Sciences, 1, 59-65, 1979. \nArticles published on OBGYN.net: \n1- Abdel Karim M. El Hemaly*, Ibrahim M. Kandil, Laila A. S. Mousa and Mohamad A.K.M.El Hemaly.\nUrethro-vaginoplasty, an innovated operation for the treatment of: Stress Urinary Incontinence (SUI), Detursor Overactivity (DO), Mixed Urinary Incontinence and Anterior Vaginal Wall Descent. \nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/ urethro-vaginoplasty_01\n\n2- Abdel Karim M. El Hemaly, Ibrahim M Kandil, Mohamed M. Radwan.\n Urethro-raphy a new technique for surgical management of Stress Urinary Incontinence.\nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/\nnew-tech-urethro\n\n3- Abdel Karim M. El Hemaly, Ibrahim M Kandil, Mohamad A. Rizk, Nabil Abdel Maksoud H., Mohamad M. Radwan, Khalid Z. El Shieka, Mohamad A. K. M. El Hemaly, and Ahmad T. El Saban.\nUrethro-raphy The New Operation for the treatment of stress urinary incontinence, SUI, detrusor instability, DI, and mixed-type of urinary incontinence; short and long term results. \nhttp://www.obgyn.net/urogyn/urogyn.asp?page=urogyn/articles/\nurethroraphy-09280\n\n4-Abdel Karim M. El Hemaly, Ibrahim M Kandil, and Bahaa E. El Mohamady. Menopause, and Voiding troubles. \nhttp://www.obgyn.net/displayppt.asp?page=/English/pubs/features/presentations/El-Hemaly03/el-hemaly03-ss\n\n5-El Hemaly AKMA, Mousa L.A. Micturition and Urinary\tContinence. Int J Gynecol Obstet 1996; 42: 291-2. \n\n6-Abdel Karim M. El Hemaly.\n Urinary incontinence in gynecology, a review article.\nhttp://www.obgyn.net/urogyn/urogyn.asp?page=/urogyn/articles/abs-urinary_incotinence_gyn_ehemaly \n\n7-El Hemaly AKMA. Nocturnal Enuresis: Pathogenesis and Treatment. \nInt Urogynecol J Pelvic Floor Dysfunct 1998;9: 129-31.\n \n8-El Hemaly AKMA, Mousa L.A.E. Stress Urinary Incontinence, a New Concept. Eur J Obstet Gynecol Reprod Biol 1996; 68: 129-35. \n\n9- El Hemaly AKMA, Kandil I. M. Stress Urinary Incontinence SUI facts and fiction. Is SUI a puzzle?! http://www.obgyn.net/displayppt.asp?page=/English/pubs/features/presentations/El-Hemaly/el-hemaly-ss\n\n10-Abdel Karim El Hemaly, Nabil Abdel Maksoud, Laila A. Mousa, Ibrahim M. Kandil, Asem Anwar, M.A.K El Hemaly and Bahaa E. El Mohamady. \nEvidence based Facts on the Pathogenesis and Management of SUI. http://www.obgyn.net/displayppt.asp?page=/English/pubs/features/presentations/El-Hemaly02/el-hemaly02-ss\n\n11- Abdel Karim M. El Hemaly*, Ibrahim M. 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