Processing of pro-islet amyloid polypeptide (proIAPP) by the prohormone convertase PC2

Michael K. Badman, Kathleen I.J. Shennan, Joanne L. Jermany, Kevin Docherty*, Anne Clark

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

61 Citations (Scopus)

Abstract

Islet amyloid polypeptide (IAPP), 'amylin', is the component peptide of islet amyloid formed in Type 2 diabetes. IAPP is expressed in islet β-cells and is derived from a larger precursor, proIAPP, by proteolysis. An in vitro translation/ translocation system was used to separately examine processing of human proIAPP by the β-cell endopeptidases PC2, PC3 or furin. ProIAPP was converted to mature IAPP by PC2 but there was little conversion by furin or PC3. These data are consistent with processing of proIAPP in β-cell secretory granules. Abnormal cellular proteolysis associated with type 2 diabetes could contribute to IAPP amyloidosis.

Original languageEnglish
Pages (from-to)227-231
Number of pages5
JournalFEBS LETTERS
Volume378
Issue number3
DOIs
Publication statusPublished - 15 Jan 1996

Keywords

  • Furin
  • Islet amyloid polypeptide
  • PC2
  • PC3
  • Propeptide processing
  • β-Cell

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