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Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity
Author(s) -
Cao Ping,
Marek Peter,
Noor Harris,
Patsalo Vadim,
Tu Ling-Hsien,
Wang Hui,
Abedini Andisheh,
Raleigh Daniel P.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.01.046
Subject(s) - islet , amylin , amyloid (mycology) , cytotoxicity , chemistry , insulin , secretion , amyloid disease , endocrinology , transplantation , medicine , microbiology and biotechnology , biochemistry , biology , amyloid β , in vitro , amyloid fibril , inorganic chemistry , disease
Pancreatic islet amyloid is a characteristic feature of type 2 diabetes. The major protein component of islet amyloid is the polypeptide hormone known as islet amyloid polypeptide (IAPP, or amylin). IAPP is stored with insulin in the β‐cell secretory granules and is released in response to the stimuli that lead to insulin secretion. IAPP is normally soluble and is natively unfolded in its monomeric state, but forms islet amyloid in type 2 diabetes. Islet amyloid is not the cause of type 2 diabetes, but it leads to β‐cell dysfunction and cell death, and contributes to the failure of islet cell transplantation. The mechanism of IAPP amyloid formation is not understood and the mechanisms of cytotoxicity are not fully defined.