Ontology highlight
ABSTRACT:
SUBMITTER: Sulka B
PROVIDER: S-EPMC2667753 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Sulka Béatrice B Lortat-Jacob Hugues H Terreux Raphael R Letourneur François F Rousselle Patricia P
The Journal of biological chemistry 20090219 16
Heparan sulfate proteoglycan receptor syndecan-1 interacts with the carboxyl-terminal LG4/5 domain in laminin 332 (alpha3LG4/5) and participates in cell adhesion and spreading. To dissect the function of syndecan-1 in these processes, we made use of a cell adhesion model in which syndecan-1 exclusively interacts with a recombinantly expressed alpha3LG4/5 fragment. Plating HT1080 cells on this fragment induces the formation of actin-containing protrusive structures in an integrin-independent mann ...[more]