نتایج جستجو برای: Islet Amyloid Polypeptide

تعداد نتایج: 80109  

2015
Hanjun Guan K. Martin Chow Eunsuk Song Nirmal Verma Florin Despa Louis B. Hersh Jie Zheng

Amyloid formation and mitochondrial dysfunction are characteristics of type 2 diabetes. The major peptide constituent of the amyloid deposits in type 2 diabetes is islet amyloid polypeptide (IAPP). In this study, we found that pitrilysin, a zinc metallopeptidase of the inverzincin family, degrades monomeric, but not oligomeric, islet amyloid polypeptide in vitro. In insulinoma cells when pitril...

Journal: :iranian journal of immunology 0
fathollah kalantar department of immunology mohammad hossein dabbaghmanesh endocrine and metabolism research center, shiraz university of medical sciences, shiraz, iran emanuela martinuzzi cochin institute, paris, france mohsen moghadami hiv/aids research center zahra amirghofran department of immunology

background: type 2 diabetes (t2d) is a chronic metabolic disorder in which beta-cells are destroyed. the islet amyloid polypeptide (iapp) produced by beta-cells has been reported to influence beta-cell destruction. objective: to evaluate if iapp can act as an autoantigen and therefore, to see if cd8 + t-cells specific for this protein might be present in t2d patients. methods: peripheral blood ...

2011
Per Westermark

Deposition of amyloid, derived from the polypeptide hormone islet amyloid polypeptide (IAPP; 'amylin') is the single most typical islet alteration in type 2 diabetes. Islet amyloid was described as hyalinization already in 1901, but not until 1986 was it understood that it is a polymerization product of a novel β-cell regulatory product. The subject of this focused review deals with the pathoge...

2013
Martina Pannuzzo Antonio Raudino Danilo Milardi Carmelo La Rosa Mikko Karttunen

The human islet amyloid polypeptide (hIAPP) is the primary component in the toxic islet amyloid deposits in type-2 diabetes. hIAPP self-assembles to aggregates that permeabilize membranes and constitutes amyloid plaques. Uncovering the mechanisms of amyloid self-assembly is the key to understanding amyloid toxicity and treatment. Although structurally similar, hIAPP's rat counterpart, the rat i...

Journal: :Experimental Diabetes Research 2008
J. W. M. Höppener H. M. Jacobs N. Wierup G. Sotthewes M. Sprong P. de Vos R. Berger F. Sundler B. Ahrén

Human islet amyloid polypeptide (hIAPP), a pancreatic islet protein of 37 amino acids, is the main component of islet amyloid, seen at autopsy in patients with type 2 diabetes mellitus (DM2). To investigate the roles of hIAPP and islet amyloid in DM2, we generated transgenic mice expressing hIAPP in their islet beta cells. In this study, we found that after a long-term, high-fat diet challenge ...

2017
Sara Ullsten Sara Bohman Marie E Oskarsson K Peter R Nilsson Gunilla T Westermark Per-Ola Carlsson

Islet amyloid and beta cell death in type 2 diabetes are heterogeneous events, where some islets are affected early in the disease process, whereas others remain visibly unaffected. This study investigated the possibility that inter-islet functional and vascular differences may explain the propensity for amyloid accumulation in certain islets. Highly blood-perfused islets were identified by mic...

Journal: :Diabetes 1991
K H Johnson T D O'Brien P Westermark

Islet amyloid polypeptide (IAPP) or amylin is a newly identified 37-amino acid COOH-terminal-amidated polypeptide that is the major protein constituent of amyloid deposits in insulinomas and amyloid deposits in pancreatic islets of non-insulin-dependent (type II) diabetic humans and adult diabetic cats. IAPP is stored with insulin in beta-cell secretory vesicles and is cosecreted with insulin i...

Journal: :Biochimica et Biophysica Acta (BBA) - Biomembranes 2007

Journal: :Physiological reviews 2011
Per Westermark Arne Andersson Gunilla T Westermark

Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon secretion, and at distant targets. It has binding sites in the brain, possibly contributing also to satiety regulation and inhibits gastric emptyi...

Journal: :Chemistry and Physics of Lipids 2009

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