Impaired Processing of Human Pro-Islet Amyloid Polypeptide Is Not a Causative Factor for Fibril Formation or Membrane Damage in Vitro-Reference-Cited by-同舟云学术

Impaired Processing of Human Pro-Islet Amyloid Polypeptide Is Not a Causative Factor for Fibril Formation or Membrane Damage in Vitro

Published:2009-10-30 Issue:46 Volume:48 Page:10918-10925
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Khemtémourian Lucie¹,Lahoz Casarramona Gemma²,Suylen Dennis P. L.³,Hackeng Tilman M.³,Meeldijk Johannes D.⁴,de Kruijff Ben¹,Höppener Jo W. M.²,Killian J. Antoinette¹

Affiliation:

1. Department of Chemical Biology and Organic Chemistry, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

2. Department of Metabolic and Endocrine Diseases, Division of Biomedical Genetics, University Medical Center Utrecht, P.O. Box 85090, 3508 AB Utrecht, The Netherlands

3. Department of Biochemistry, Cardiovascular Research Institute Maastricht, Maastricht University, Universiteitssingel 50, 6200 MD Maastricht, The Netherlands

4. Department of Molecular Cell Biology, Electron Microscopy Utrecht, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi901076d

Reference36 articles.

1. Islet Amyloid and Type 2 Diabetes Mellitus

2. Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets

3. Amylin, Food Intake, and Obesity

4. Inhibition of Central Amylin Signaling Increases Food Intake and Body Adiposity in Rats

5. Impaired NH2-Terminal Processing of Human Proislet Amyloid Polypeptide by the Prohormone Convertase PC2 Leads to Amyloid Formation and Cell Death

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