Ontology highlight
ABSTRACT:
SUBMITTER: Palato LM
PROVIDER: S-EPMC6639132 | biostudies-literature | 2019 Aug
REPOSITORIES: biostudies-literature
Journal of peptide science : an official publication of the European Peptide Society 20190623 8
The aggregation of the 37-amino acid polypeptide human islet amyloid polypeptide (hIAPP), as either insoluble amyloid or as small oligomers, appears to play a direct role in the death of human pancreatic β-islet cells in type 2 diabetes. hIAPP is considered to be one of the most amyloidogenic proteins known. The quick aggregation of hIAPP leads to the formation of toxic species, such as oligomers and fibers, that damage mammalian cells (both human and rat pancreatic cells). Whether this toxicity ...[more]