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.
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January 01 1990
Structure of Cat Islet Amyloid Polypeptide and Identification of Amino Acid Residues of Potential Significance for Islet Amyloid Formation
Christer Betsholtz;
Christer Betsholtz
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Lars Christmanson;
Lars Christmanson
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Ulla Engström;
Ulla Engström
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Fredrik Rorsman;
Fredrik Rorsman
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Kathy Jordan;
Kathy Jordan
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Timothy D O'Brien;
Timothy D O'Brien
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Michael Murtaugh;
Michael Murtaugh
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Kenneth H Johnson;
Kenneth H Johnson
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Per Westermark
Per Westermark
Department of Pathology, University Hospital, and Ludwig Institute for Cancer Research, Uppsala Branch
Uppsala, Sweden
; Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Minnesota
St. Paul, Minnesota
; and Department of Pathology, University Hospital
Linköping, Sweden
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Address correspondence and reprint requests to Christer Betsholtz, Department of Pathology, University Hospital, S-751 85 Uppsala, Sweden.
Diabetes 1990;39(1):118–122
Article history
Received:
August 14 1989
Revision Received:
September 14 1989
Accepted:
September 14 1989
PubMed:
2210054
Citation
Christer Betsholtz, Lars Christmanson, Ulla Engström, Fredrik Rorsman, Kathy Jordan, Timothy D O'Brien, Michael Murtaugh, Kenneth H Johnson, Per Westermark; Structure of Cat Islet Amyloid Polypeptide and Identification of Amino Acid Residues of Potential Significance for Islet Amyloid Formation. Diabetes 1 January 1990; 39 (1): 118–122. https://doi.org/10.2337/diacare.39.1.118
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