A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells.
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.
Department of Medical Biochemistry, University of Turku, Finland.
M
M
Salmivirta
M
M
Mali
J
J
Heino
J
J
Hermonen
M
M
Jalkanen
D016475:3T3 Cells; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D002478:Cells, Cultured; D002809:Chondroitin Sulfates / Q000378:metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D018076:DNA, Complementary; D004848:Epithelium / Q000378:metabolism; D005260:Female; D005822:Genetic Vectors; D006025:Glycosaminoglycans / Q000096:biosynthesis / Q000302:isolation & purification; D007797:Laminin / Q000378:metabolism*; D008321:Mammary Glands, Animal / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000096:biosynthesis / Q000378:metabolism*; D008715:Methionine / Q000378:metabolism; D051379:Mice; D011485:Protein Binding; D011509:Proteoglycans / Q000096:biosynthesis / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D012513:Sarcoma, Experimental; D013431:Sulfates / Q000378:metabolism; D013462:Sulfur Radioisotopes; D053668:Syndecan-1; D053667:Syndecans; D014162:Transfection; D014407:Tumor Cells, Cultured
D018076:DNA, Complementary; D006025:Glycosaminoglycans; D007797:Laminin; D008562:Membrane Glycoproteins; D011509:Proteoglycans; D011994:Recombinant Proteins; C508242:Sdc1 protein, mouse; D013431:Sulfates; D013462:Sulfur Radioisotopes; D053668:Syndecan-1; D053667:Syndecans; D002809:Chondroitin Sulfates; D008715:Methionine