scholarly journals β-Cell Dysfunctional ERAD/Ubiquitin/Proteasome System in Type 2 Diabetes Mediated by Islet Amyloid Polypeptide–Induced UCH-L1 Deficiency

Diabetes ◽  
2010 ◽  
Vol 60 (1) ◽  
pp. 227-238 ◽  
Author(s):  
Safia Costes ◽  
Chang-jiang Huang ◽  
Tatyana Gurlo ◽  
Marie Daval ◽  
Aleksey V. Matveyenko ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Islet Amyloid Polypeptide ◽  
Ubiquitin Proteasome System ◽  
Β Cell ◽  
Islet Amyloid ◽  
Ubiquitin Proteasome

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

2017 ◽  
Vol 74 (15) ◽  
pp. 2827-2838 ◽  
Author(s):  
Gema Alcarraz-Vizán ◽  
Carlos Castaño ◽  
Montse Visa ◽  
Joel Montane ◽  
Joan-Marc Servitja ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Cell Survival ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Β Cell ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
And Function

scholarly journals Pancreatic beta-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation

2004 ◽  
Vol 377 (3) ◽  
pp. 709-716 ◽  
Author(s):  
Emma T. A. S. JAIKARAN ◽  
Melanie R. NILSSON ◽  
Anne CLARK
Keyword(s):  
Type 2 Diabetes ◽  
Amyloid Fibrils ◽  
Secretory Granules ◽  
Pancreatic Beta Cell ◽  
Islet Amyloid Polypeptide ◽  
Fibril Formation ◽  
Islet Amyloid ◽  
Β Sheet

Islet amyloid polypeptide (IAPP), or ‘amylin’, is co-stored with insulin in secretory granules of pancreatic islet β-cells. In Type 2 diabetes, IAPP converts into a β-sheet conformation and oligomerizes to form amyloid fibrils and islet deposits. Granule components, including insulin, inhibit spontaneous IAPP fibril formation in vitro. To determine the mechanism of this inhibition, molecular interactions of insulin with human IAPP (hIAPP), rat IAPP (rIAPP) and other peptides were examined using surface plasmon resonance (BIAcore), CD and transmission electron microscopy (EM). hIAPP and rIAPP complexed with insulin, and this reaction was concentration-dependent. rIAPP and insulin, but not pro-insulin, bound to hIAPP. Insulin with a truncated B-chain, to prevent dimerization, also bound hIAPP. In the presence of insulin, hIAPP did not spontaneously develop β-sheet secondary structure or form fibrils. Insulin interacted with pre-formed IAPP fibrils in a regular repeating pattern, as demonstrated by immunoEM, suggesting that the binding sites for insulin remain exposed in hIAPP fibrils. Since rIAPP and hIAPP form complexes with insulin (and each other), this could explain the lack of amyloid fibrils in transgenic mice expressing hIAPP. It is likely that IAPP fibrillogenesis is inhibited in secretory granules (where the hIAPP concentration is in the millimolar range) by heteromolecular complex formation with insulin. Alterations in the proportions of insulin and IAPP in granules could disrupt the stability of the peptide. The increase in the proportion of unprocessed pro-insulin produced in Type 2 diabetes could be a major factor in destabilization of hIAPP and induction of fibril formation.

scholarly journals Molecular Docking Studies of Possible Treatment of Diabetes using Vasicine against Islet Amyloid Polypeptide

2021 ◽  
Vol 9 (VI) ◽  
pp. 4202-4209
Author(s):  
Tushar Kumar
Keyword(s):  
Type 2 Diabetes ◽  
Insulin Secretion ◽  
Molecular Docking ◽  
Islet Amyloid Polypeptide ◽  
Docking Studies ◽  
Islet Amyloid ◽  
Molecular Docking Studies ◽  
The World ◽  
Treatment Of Diabetes

Diabetes is the becoming one of the most common problem all over the world. About 1 in 10 persons are suffering from diabetes and most from type 2 diabetes. It occurs due to problem in pancreas which further results defect in the insulin secretion, as insulin maintains blood glucose level. The effect of Alpha-Amyrin Acetate, Myrcene and Vasicine compounds against Islet Amyloid polypeptide (IAPP) protein was seen through molecular docking studies. IAPP acts as complementary to insulin in regulating the sugar level for the treatment of diabetes disease by virtual screening. Different tools and software used in this research were Uniprot, Pubchem, Swiss ADMS, PyRx, Auto dock Vina/MGL tool and PyMOL.

scholarly journals Dietary Supplementation with Curcumin Reduce Circulating Levels of Glycogen Synthase Kinase-3β and Islet Amyloid Polypeptide in Adults with High Risk of Type 2 Diabetes and Alzheimer’s Disease

Nutrients ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 1032 ◽  
Author(s):  
Rohith N Thota ◽  
Jessica I Rosato ◽  
Cintia B Dias ◽  
Tracy L Burrows ◽  
Ralph N Martins ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Type 2 Diabetes ◽  
Placebo Group ◽  
Glycogen Synthase ◽  
Islet Amyloid Polypeptide ◽  
Dietary Supplementation ◽  
Islet Amyloid ◽  
Gsk 3Β ◽  
Circulating Levels

Dietary supplementation with curcumin has been previously reported to have beneficial effects in people with insulin resistance, type 2 diabetes (T2D) and Alzheimer’s disease (AD). This study investigated the effects of dietary supplementation with curcumin on key peptides implicated in insulin resistance in individuals with high risk of developing T2D. Plasma samples from participants recruited for a randomised controlled trial with curcumin (180 mg/day) for 12 weeks were analysed for circulating glycogen synthase kinase-3 β (GSK-3β) and islet amyloid polypeptide (IAPP). Outcome measures were determined using ELISA kits. The homeostasis model for assessment of insulin resistance (HOMA-IR) was measured as parameters of glycaemic control. Curcumin supplementation significantly reduced circulating GSK-3β (−2.4 ± 0.4 ng/mL vs. −0.3 ± 0.6, p = 0.0068) and IAPP (−2.0 ± 0.7 ng/mL vs. 0.4 ± 0.6, p = 0.0163) levels compared with the placebo group. Curcumin supplementation significantly reduced insulin resistance (−0.3 ± 0.1 vs. 0.01 ± 0.05, p = 0.0142) compared with placebo group. Dietary supplementation with curcumin reduced circulating levels of IAPP and GSK-3β, thus suggesting a novel mechanism through which curcumin could potentially be used for alleviating insulin resistance related markers for reducing the risk of T2D and AD.

scholarly journals Islet amyloid polypeptide gene promoter polymorphisms are not associated with Type 2 diabetes or with the severity of islet amyloidosis

2005 ◽  
Vol 1740 (1) ◽  
pp. 74-78 ◽  
Author(s):  
Christopher Esapa ◽  
Jennifer H. Moffitt ◽  
Anna Novials ◽  
Catherine M. McNamara ◽  
Jonathan C. Levy ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Islet Amyloid Polypeptide ◽  
Gene Promoter ◽  
Promoter Polymorphisms ◽  
Islet Amyloid

scholarly journals Hsp72 (HSPA1A) Prevents Human Islet Amyloid Polypeptide Aggregation and Toxicity: A New Approach for Type 2 Diabetes Treatment

PLoS ONE ◽  
2016 ◽  
Vol 11 (3) ◽  
pp. e0149409 ◽  
Author(s):  
Paola C. Rosas ◽  
Ganachari M. Nagaraja ◽  
Punit Kaur ◽  
Alexander Panossian ◽  
Georg Wickman ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Diabetes Treatment ◽  
Islet Amyloid ◽  
New Approach ◽  
Human Islet Amyloid Polypeptide ◽  
Type 2 Diabetes Treatment
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