Human insulin-like growth factor binding protein-6 is O-glycosylated
| Autor: | Leon A. Bach, N. Rao Thotakura, Matthew M. Rechler |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Insulin-Like Growth Factor Binding Protein 6
Glycosylation Glycoside Hydrolases Molecular Sequence Data Carbohydrates Biophysics Oligosaccharides Mannose Binding Competitive Biochemistry Fucose chemistry.chemical_compound Somatomedins Insulin-Like Growth Factor II Glucosamine Lectins Humans Insulin-Like Growth Factor I Molecular Biology Binding protein Cell Biology Sialic acid Molecular Weight Carbohydrate Sequence chemistry Galactosamine Electrophoresis Polyacrylamide Gel Carrier Proteins Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 186:301-307 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(05)80807-1 |
| Popis: | 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 approximately 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 x 10(11) 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. |
| Databáze: | OpenAIRE |
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