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Isolation and identification of islet amyloid polypeptide in normal human pancreas.
To identify islet amyloid polypeptide (IAPP) present in normal human pancreas, we isolated the peptide from a soluble peptide fraction of amyloid deposit-free pancreata of two non-diabetic patients by using reverse-phase high performance liquid chromatography coupled with a radioimmunoassay specific for human IAPP. IAPP(1-37) and IAPP(17-37) were isolated and their complete amino acid sequences were determined up to the C-terminus. Identification of IAPP in normal human pancreas suggests the possible biological function of IAPP as a novel pancreatic hormone in humans.
Authors : Nakazato M , Asai J , Miyazato M , Matsukura S , Kangawa K , Matsuo H ,
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WP2107: pathways in human cancer
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Bibliography :
[11145957] Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation.
[2091067] Isolation and identification of islet amyloid polypeptide in normal human pancreas.
[2670595] Islet amyloid polypeptide (IAPP):cDNA cloning and identification of an amyloidogenic region associated with the species-specific occurrence of age-related diabetes mellitus.
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