GLYCOSYLATION OF THE ACTIVE SEQUENCE SER-ILE-LYS-VAL-ALA-VAL FROM THEALPHA-1 CHAIN OF LAMININ REDUCES TUMOR-CELL ATTACHMENT ACTIVITY

Authors
BARCHI JJ RUSS P JOHNSON B OTAKA A NOMIZU M YAMADA Y
Citation
Jj. Barchi et al., GLYCOSYLATION OF THE ACTIVE SEQUENCE SER-ILE-LYS-VAL-ALA-VAL FROM THEALPHA-1 CHAIN OF LAMININ REDUCES TUMOR-CELL ATTACHMENT ACTIVITY, Bioorganic & medicinal chemistry letters, 5(7), 1995, pp. 711-714
Citations number
18
Categorie Soggetti
Chemistry Inorganic & Nuclear","Chemistry Medicinal
Journal title
Bioorganic & medicinal chemistry letters → ACNP
ISSN journal
0960894X
Volume
5
Issue
7
Year of publication
1995
Pages
711 - 714
Database
ISI
SICI code
0960-894X(1995)5:7<711:GOTASS>2.0.ZU;2-K
Abstract
N-terminal serine O-glycopeptides of SIKVAV-, a sequence located on th e long arm of the alpha 1 chain of laminin, were synthesized to study the effect of glycosylation on the adhesive properties of this biologi cally relevant peptide. The data show that covalently linked carbohydr ates decrease the cell-attachment activity in a structurally dependent manner.