Gastric inhibitory polypeptide |
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Authors: | R Ebert W Creutzfeldt |
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Affiliation: | 1. Department of Mechanical Engineering, Raghu Engineering College (Autonomous), Vishakhapatnam, A.P, India;2. Department of Mechanical Engineering, National Institute of Technology, Rourkela, Odisha, India;1. Department of Chemistry, University of Wisconsin, Madison, WI, United States;2. Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences and Department of Pharmacology, Monash University, Parkville, Australia;1. Institute for Diabetes and Obesity, Helmholtz Diabetes Center at Helmholtz Zentrum München, German Research Center for Environmental Health (GmbH), Neuherberg, Germany;2. Division of Metabolic Diseases, Department of Medicine, Technische Universität München, Munich, Germany;3. German Center for Diabetes Research (DZD), Neuherberg, Germany;4. Metabolic Diseases Institute, Division of Endocrinology, Department of Internal Medicine, University of Cincinnati College of Medicine, Cincinnati, OH, USA;5. Department of Chemistry, Indiana University, Bloomington, IN, USA;1. Cell Biology and Experimental Cancer Research, Institute of Pathology, University of Berne, CH-3010 Berne, Switzerland;2. LPCNO, ERL 1226 INSERM, Université De Toulouse, CNRS, INSA, UPS, 135 Avenue De RAngueil, 31077 Toulouse, France;3. Laboratori De Medicina Computacional, Unitat De Bioestadística, Facultat De Medicina, Universitat Autònoma De Barcelona, Barcelona, Spain;4. School of Pharmacy, Medical Biology Centre, Queen’s University Belfast, Belfast BT9 7BL, Northern Ireland, United Kingdom;1. The National Center for Drug Screening and CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (CAS), Shanghai 201203, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Department of Biomedical Sciences, University of Copenhagen, Copenhagen N DK-2200, Denmark;4. School of Pharmacy, Fudan University, Shanghai 201203, China;5. Centre for Sport, Exercise and Life Sciences, Faculty of Health and Life Sciences, Alison Gingell Building, Coventry University, Coventry, CV1 2DS, UK;6. Department of Pharmacology, School of Basic Medical Sciences, Fudan University, Shanghai 200032, China;7. Drug Discovery Biology Theme, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia;8. ARC Centre for Cryo-electron Microscopy of Membrane Proteins, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia;1. Institute for Diabetes and Obesity, Helmholtz Diabetes Center, Helmholtz Zentrum München, Neuherberg, Germany;2. German Center for Diabetes Research (DZD), Neuherberg, Germany;3. Division of Metabolic Diseases, Department of Medicine, Technische Universität München, D-80333 Munich, Germany;4. Institute of Metabolism and Systems Research, University of Birmingham, Birmingham, B15 2TT, UK;5. Center of Membrane Proteins and Receptors (COMPARE), Universities of Nottingham and Birmingham, Birmingham, B15 2TT, UK;6. Novo Nordisk Research Center Indianapolis, Indianapolis, IN 46241, USA;7. Chair for Molecular Nutritional Medicine, School of Life Sciences, Technical University of Munich, 85354 Freising, Germany;8. Institute for Diabetes and Cancer, Helmholtz Center Munich, 85764 Neuherberg, Germany;9. Joint Heidelberg-IDC Translational Diabetes Program, Inner Medicine 1, Heidelberg University Hospital, Heidelberg, Germany;10. Department of Chemistry, Indiana University, Bloomington, IN 47405, USA;11. Helmholtz Zentrum München, Neuherberg, Germany;12. Technische Universität München, München, Germany;13. Department of Pharmacology and Experimental Therapy, Institute of Experimental and Clinical Pharmacology and Toxicology, Eberhard Karls University Hospitals and Clinics, 72076 Tübingen, Germany |
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Abstract: | The available data show that GIP is at present the strongest candidate for the insulin-secreting factor of the gut named incretin. Its release is triggered by the absorption of ingested nutrients. GIP acts on the B-cells of the pancreas by potentiating glucose-induced insulin secretion. The role of GIP as an enterogastrone is less well established. The release of GIP from the gut cells seems to be regulated by the composition and the amount of the ingested food, by the rate of absorption of nutrients by neural factors (vagal), and by feedback control mediated by insulin. In addition, the adaptation of the intestine to individual eating habits influences the response of the GIP cells. It is suggested that an overactive enteroinsular axis, i.e. enhanced GIP secretion, participates in the development of the hyperinsulinaemia of obesity and maturity onset diabetes mellitus. In gastrointestinal diseases accompanied by malabsorption the GIP response is diminished. In gastrointestinal disorders with rapid gastric emptying (duodenal ulcer) or with accelerated passage of the nutrients through the intestine, hypersecretion of GIP and insulin occurs. This may be significant for the reactive hypoglycaemia of these conditions. |
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