HUMAN INSULIN-LIKE GROWTH-FACTOR BINDING PROTEIN-6 IS O-GLYCOSYLATED

被引：60

作者：

BACH, LA ^{[1
]}

THOTAKURA, NR ^{[1
]}

RECHLER, MM ^{[1
]}

机构：

[1] NIDDKD, MOLEC & CELLULAR ENDOCRINOL BRANCH, MOLEC REGULAT & NEUROENDOCRINOL SECT, BETHESDA, MD 20892 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 186卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)80807-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Insulin-like growth factor binding protein-6 is abundant in cerebrospinal fluid and has a marked preferential binding affinity for IGF-II over IGF-I. The present study demonstrates that IGFBP-6 is O-glycosylated but not N-glycosylated. Carbohydrate analysis revealed the presence of ∼20-30 carbohydrate residues/molecule. Galactosamine, galactose and sialic acid were most abundant, with glucosamine and fucose present in lower concentrations. Mannose was not detected. Enzymatic deglycosylation did not alter the high affinity of IGF binding protein-6 for IGF-II (Ka 4.4 ± 2.2 × 1011 M-1) or its preference for IGF-II over IGF-I. Glycosylation of IGFBP-6 may affect its secretion, in vivo stability or localization, but does not affect its ligand binding properties. © 1992 Academic Press, Inc.

引用

页码：301 / 307

页数：7

共 16 条

[1] CARBOHYDRATE-SPECIFIC RECEPTORS OF THE LIVER [J].