期刊
FEBS LETTERS
卷 518, 期 1-3, 页码 124-128出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02673-X
关键词
insulin-like growth factor binding protein-3; circulating fragment; peptide library; glycosylation
Proteolysis of insulin-like growth factor binding protein-3 (IGFBP-3), the major carrier of IGFs in the circulation, is an essential mechanism to regulate IGF bioavailability. To analyze naturally occurring IGFBP-3 fragments a peptide library established from human hemofiltrate was screened. Three IGFBP-3 fragments were detected with apparent molecular masses of 34, 16, and 11 kDa. Mass spectrometric and sequence analysis identified the 16 and I I kDa peptides as glycosylated and non-glycosylated N-terminal fragments spanning residues Gly(1)-Ala(98) of IGFBP-3. Both the circulating forms and those secreted from IGFBP-3(1-98) overexpressing cells bound IGF. Additionally, two smaller fragments (IGFBP-3(139-157) and IGFBP-3(139-159)) were identified in the hemofiltrate. The data indicate that proteolysis of circulating IGFBP-3 occurs in the variable domain at residues alanine 98, phenylalanine 138, glutamine 157, and tyrosine 159. (C) 2002 Published by Elsevier Science B.V.. on behalf of the Federation of European Biochemical Societies.
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