Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity

Ping Cao, Peter Marek, Harris Noor, Vadim Patsalo, Ling Hsien Tu, Hui Wang, Andisheh Abedini, Daniel P. Raleigh

Research output: Contribution to journalReview article

115 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1106-1118
Number of pages13
JournalFEBS Letters
Volume587
Issue number8
DOIs
Publication statusPublished - 2013 Apr 17

Keywords

  • Amylin
  • Amyloid
  • IAPP
  • Islet amyloid polypeptide
  • Type 2 diabetes

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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  • Cite this

    Cao, P., Marek, P., Noor, H., Patsalo, V., Tu, L. H., Wang, H., Abedini, A., & Raleigh, D. P. (2013). Islet amyloid: From fundamental biophysics to mechanisms of cytotoxicity. FEBS Letters, 587(8), 1106-1118. https://doi.org/10.1016/j.febslet.2013.01.046