Literature DB >> 8736810

Islet amyloid polypeptide: actions and role in the pathogenesis of diabetes.

A Clark1, S B Charge, M K Badman, D A MacArthur, E J de Koning.   

Abstract

IAPP has been postulated to have a role as a modulating factor in glucose homoeostasis and to be involved in the pathophysiology of diabetes. However, the normal physiological functions of the peptide remain obscure: exogenous IAPP acts on many experimental systems to modulate nutrient supply and metabolism but there is no evidence to suggest that circulating IAPP has an aetiological role in the onset of Type-2 diabetes. Amyloid deposits formed from polymerized IAPP progressively accumulate in the islets of Type-2 diabetic patients. These insoluble deposits do not precipitate the onset of hyperglycaemia in Type-2 diabetes, but progressive accumulation of amyloid is associated with islet cell destruction and decreased islet function in the later stages of the disease. Although the causative factors of formation of the first IAPP fibril are unknown, continued high levels of insulin and IAPP secretion as a result of nutrient stimulation or insulin resistance will promote binding to preformed fibrils and extension of the deposits. It is important that methods to identify patients susceptible to amyloid deposition are developed and therapeutic agents are produced that can reduce or prevent polymerizatin of IAPP to form amyloid and minimize severe deterioration of islet function in Type-2 diabetes.

Entities:  

Mesh:

Substances:

Year:  1996        PMID: 8736810     DOI: 10.1042/bst0240594

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  8 in total

1.  Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins.

Authors:  Sharmistha Sinha; Dahabada H J Lopes; Zhenming Du; Eric S Pang; Akila Shanmugam; Aleksey Lomakin; Peter Talbiersky; Annette Tennstaedt; Kirsten McDaniel; Reena Bakshi; Pei-Yi Kuo; Michael Ehrmann; George B Benedek; Joseph A Loo; Frank-Gerrit Klärner; Thomas Schrader; Chunyu Wang; Gal Bitan
Journal:  J Am Chem Soc       Date:  2011-09-29       Impact factor: 15.419

2.  BACE2 suppression promotes β-cell survival and function in a model of type 2 diabetes induced by human islet amyloid polypeptide overexpression.

Authors:  Gema Alcarraz-Vizán; Carlos Castaño; Montse Visa; Joel Montane; Joan-Marc Servitja; Anna Novials
Journal:  Cell Mol Life Sci       Date:  2017-03-23       Impact factor: 9.261

3.  Structure and composition of insulin fibril surfaces probed by TERS.

Authors:  Dmitry Kurouski; Tanja Deckert-Gaudig; Volker Deckert; Igor K Lednev
Journal:  J Am Chem Soc       Date:  2012-08-03       Impact factor: 15.419

4.  S20G mutant amylin exhibits increased in vitro amyloidogenicity and increased intracellular cytotoxicity compared to wild-type amylin.

Authors:  S Sakagashira; H J Hiddinga; K Tateishi; T Sanke; T Hanabusa; K Nanjo; N L Eberhardt
Journal:  Am J Pathol       Date:  2000-12       Impact factor: 4.307

Review 5.  Neuroendocrine hormone amylin in diabetes.

Authors:  Xiao-Xi Zhang; Yan-Hong Pan; Yan-Mei Huang; Hai-Lu Zhao
Journal:  World J Diabetes       Date:  2016-05-10

Review 6.  Pituitary adenylate cyclase-activating polypeptide and islet amyloid polypeptide in primary sensory neurons: functional implications from plasticity in expression on nerve injury and inflammation.

Authors:  H Mulder; H Jongsma; Y Zhang; S Gebre-Medhin; F Sundler; N Danielsen
Journal:  Mol Neurobiol       Date:  1999-06       Impact factor: 5.590

7.  Intracellular amyloidogenesis by human islet amyloid polypeptide induces apoptosis in COS-1 cells.

Authors:  H J Hiddinga; N L Eberhardt
Journal:  Am J Pathol       Date:  1999-04       Impact factor: 4.307

Review 8.  Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal models.

Authors:  Aida Attar; Gal Bitan
Journal:  Curr Pharm Des       Date:  2014       Impact factor: 3.116

  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.