Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide: implications for islet amyloid formation
K Park, CB Verchere - Journal of Biological Chemistry, 2001 - ASBMB
Islet amyloid deposits are a characteristic pathologic lesion of the pancreas in type 2
diabetes and are composed primarily of the islet beta cell peptide islet amyloid polypeptide
(IAPP or amylin) as well as the basement membrane heparan sulfate proteoglycan perlecan.
Impaired processing of the IAPP precursor has been implicated in the mechanism of islet
amyloid formation. The N-and C-terminal cleavage sites where pro-IAPP is processed by
prohormone convertases contain a series of basic amino acid residues that we …
diabetes and are composed primarily of the islet beta cell peptide islet amyloid polypeptide
(IAPP or amylin) as well as the basement membrane heparan sulfate proteoglycan perlecan.
Impaired processing of the IAPP precursor has been implicated in the mechanism of islet
amyloid formation. The N-and C-terminal cleavage sites where pro-IAPP is processed by
prohormone convertases contain a series of basic amino acid residues that we …
