Structure of cat islet amyloid polypeptide and identification of amino acid residues of potential significance for islet amyloid formation

Christer Betsholtz, Lars Christmanson, Ulla Engström, Fredrik Rorsman, Kathy Jordan, Timothy D. O'Brien, Michael Murtaugh, Kenneth H. Johnson, Per Westermark

Research output: Contribution to journalArticlepeer-review

80 Scopus citations

Abstract

Cats and humans, unlike most rodent species, develop amyloid in the islets of Langerhans in conjunction with non-insulin-dependent diabetes mellitus. The amyloid consists of a 37-amino acid polypeptide referred to as islet amyloid polypeptide (IAPP). The primary structures of IAPP from human and three rodent species have previously been determined. Sequence divergence was seen in the region corresponding to amino acid residues 20-29, which in human IAPP has been suggested to confer the amyloidogenic properties to the molecule. Using polymerase chain-reaction methodology, we determined the primary sequence of cat IAPP. Amino acid region 20-29 shows specific similarities and differences compared with human and rodent IAPP, respectively. A synthetic cat IAPP20-29 decapeptide formed amyloid fibrils spontaneously in vitro. Comparison between the structure and amyloid fibril-forming activity of various synthetic peptides suggests that the amino acid residues at positions 25-26 in mature IAPP are important for the amyloidogenic properties of the molecule.

Original languageEnglish (US)
Pages (from-to)118-122
Number of pages5
JournalDiabetes
Volume39
Issue number1
DOIs
StatePublished - Jan 1990

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