An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing

T. Sanke, G. I. Bell, Clare Sample, A. H. Rubenstein, D. F. Steiner

Research output: Contribution to journalArticle

193 Citations (Scopus)

Abstract

Amyloid deposits occurring in the islets of Langerhans in patients with noninsulin-dependent diabetes mellitus and some insulinomas contain a 37-amino acid peptide that is structurally related to calcitonin gene-related peptide. We have identified three cDNA clones encoding islet amyloid polypeptide (IAPP) or diabetes-associated peptide (DAP) by oligonucleotide screening of a λgt10 human insulinoma cDNA library. Two of the three cDNAs contained a domain encoding IAPP/DAP but had an intron-like sequence in their 5' region. The other cDNA contained an open reading frame encoding an 89-amino acid precursor having a typical signal peptide followed by a small prohormone-like sequence containing within it the IAPP/DAP peptide bracketed at its NH2 and COOH termini by Lys-Arg and Gly-Lys-Arg, respectively. These data indicate that this amyloid peptide is generated by proteolytic processing similar to that for proinsulin and other islet prohormones and also that the peptide may be carboxyamidated. The isolation of cDNA clones having 5'-unprocessed intron-like sequences suggests that inefficient or alternative splicing of this mRNA occurred in the insulinoma.

Original languageEnglish (US)
Pages (from-to)17243-17246
Number of pages4
JournalJournal of Biological Chemistry
Volume263
Issue number33
StatePublished - 1988

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Amyloid
Amino Acids
Peptides
Medical problems
Islet Amyloid Polypeptide
Insulinoma
Processing
Complementary DNA
Introns
Clone Cells
Proinsulin
Calcitonin Gene-Related Peptide
Amyloid Plaques
Alternative Splicing
Protein Sorting Signals
Islets of Langerhans
Gene Library
Oligonucleotides
Type 2 Diabetes Mellitus
Open Reading Frames

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Sanke, T., Bell, G. I., Sample, C., Rubenstein, A. H., & Steiner, D. F. (1988). An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. Journal of Biological Chemistry, 263(33), 17243-17246.
Sanke, T. ; Bell, G. I. ; Sample, Clare ; Rubenstein, A. H. ; Steiner, D. F. / An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 33. pp. 17243-17246.
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Sanke, T, Bell, GI, Sample, C, Rubenstein, AH & Steiner, DF 1988, 'An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing', Journal of Biological Chemistry, vol. 263, no. 33, pp. 17243-17246.

An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. / Sanke, T.; Bell, G. I.; Sample, Clare; Rubenstein, A. H.; Steiner, D. F.

In: Journal of Biological Chemistry, Vol. 263, No. 33, 1988, p. 17243-17246.

Research output: Contribution to journalArticle

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