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  • Title: A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells.
    Author: Salmivirta M, Mali M, Heino J, Hermonen J, Jalkanen M.
    Journal: Exp Cell Res; 1994 Nov; 215(1):180-8. PubMed ID: 7957667.
    Abstract:
    Syndecan-1, a cell surface proteoglycan, binds many extracellular matrix components via its heparan sulfate side chains. In previous studies syndecan-1 has failed to bind laminin, although both syndecan-1 and laminin are expressed at sites of early matrix accumulation, like in basement membranes of epithelial-mesenchyma boundaries and in condensing mesenchymes during embryonic development. In order to study whether syndecan-1 regulates the adhesion of mesenchymal cells to laminin, syndecan-1 was expressed in NIH-3T3 cells by transfection. Syndecan-1-transfected cells showed increased binding to laminin in comparison to control transfected cells. We then compared the properties of syndecan-1 isolated from transfected NIH-3T3 cells and from NMuMG mammary epithelial cells. In solid-phase binding assays, syndecan-1 from NIH-3T3 cells, but not NMuMG cells, bound to laminin. NIH-3T3-derived syndecan contained more chondroitin sulfate than NMuMG-derived syndecan-1, and our results revealed that both heparan sulfate and chondroitin sulfate mediate syndecan-1 binding to laminin. E3 domain revealed highest binding for syndecan-1 among the elastase-derived fragments of laminin. These results suggest that induction of syndecan-1 in mesenchymal cells may be involved in cellular recognition of laminin during developmental processes.
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