Identification of receptors for laminin

点击翻译按钮获取中文摘要

The laminin-5 is localized at skin basement membrane and supports structural stability of epidermo-dermal linkage and regulates various cellular functions. Here we analyze the heparin binding and cell adhesion activities in α3 chain carboxyl terminal globular domain (LG1〜LG5 domain) utilizing recombinant proteins made in mammalian cells as well as synthetic peptides. Immortalized human keratinocyte line HaCat cells and human dermal fibroblasts bound to LG4 domain specifically and in a dose-dependent manner. By inhibition studies, cell binding to the #75' within LG4 was mediated by cell surface heparan sulfate proteoglycan. Solid-phase assays demonstrated that syndecan-2 interacted with the #75'. Cloned 293T cells expressing syndecan specifically attached to #75' as well as to LG4. These data indicate that syndecan mediate cell adhesion to the laminin α3 LG4 domain.