Islet amyloid polypeptide, islet amyloid, and diabetes mellitus

P Westermark, A Andersson… - Physiological …, 2011 - journals.physiology.org
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 …

Amylin uncovered: a review on the polypeptide responsible for type II diabetes

K Pillay, P Govender - BioMed research international, 2013 - Wiley Online Library
Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein
misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby …

Screening and classifying small-molecule inhibitors of amyloid formation using ion mobility spectrometry–mass spectrometry

LM Young, JC Saunders, RA Mahood, CH Revill… - Nature …, 2015 - nature.com
The search for therapeutic agents that bind specifically to precursor protein conformations
and inhibit amyloid assembly is an important challenge. Identifying such inhibitors is difficult …

The flavanol (−)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against …

F Meng, A Abedini, A Plesner, CB Verchere… - Biochemistry, 2010 - ACS Publications
Islet amyloid polypeptide (IAPP, amylin) is the major protein component of the islet amyloid
deposits associated with type 2 diabetes. The polypeptide lacks a well-defined structure in …

Ion mobility spectrometry–mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors

LM Young, P Cao, DP Raleigh… - Journal of the …, 2014 - ACS Publications
The molecular mechanisms by which different proteins assemble into highly ordered fibrillar
deposits and cause disease remain topics of debate. Human amylin (also known as islet …

Islet amyloid polypeptide membrane interactions: effects of membrane composition

X Zhang, JR St. Clair, E London, DP Raleigh - Biochemistry, 2017 - ACS Publications
Amyloid formation by islet amyloid polypeptide (IAPP) contributes to β-cell dysfunction in
type 2 diabetes. Perturbation of the β-cell membrane may contribute to IAPP-induced …

The amyloid formation mechanism in human IAPP: dimers have β-strand monomer− monomer interfaces

NF Dupuis, C Wu, JE Shea… - Journal of the American …, 2011 - ACS Publications
Early oligomerization of human IAPP (hIAPP) is responsible for β-cell death in the pancreas
and is increasingly considered a primary pathological process linked to Type II Diabetes …

Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

A Abedini, A Plesner, P Cao, Z Ridgway, J Zhang… - Elife, 2016 - elifesciences.org
Islet amyloidosis by IAPP contributes to pancreatic β-cell death in diabetes, but the nature of
toxic IAPP species remains elusive. Using concurrent time-resolved biophysical and …

Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects

PJ Marek, V Patsalo, DF Green, DP Raleigh - Biochemistry, 2012 - ACS Publications
Amyloid formation plays a role in a wide range of human diseases. The rate and extent of
amyloid formation depend on solution conditions, including pH and ionic strength. Amyloid …

Islet amyloid deposition limits the viability of human islet grafts but not porcine islet grafts

KJ Potter, A Abedini, P Marek… - Proceedings of the …, 2010 - National Acad Sciences
Islet transplantation is a promising treatment for diabetes but long-term success is limited by
progressive graft loss. Aggregates of the beta cell peptide islet amyloid polypeptide (IAPP) …