Interactions of basement membrane components.
The binding of laminin, type IV collagen, and heparan sulfate proteoglycan to each other was assessed. Laminin binds preferentially to native type IV (basement membrane) collagen over other collagens. A fragment of laminin (Mr 600 000) containing the three short chains (Mr 200 000) but lacking the long chain (Mr 400 000) showed the same affinity for type IV collagen as the intact protein. The heparan sulfate proteoglycan binds well to laminin and to type IV collagen. These studies show that laminin, type IV collagen and heparan sulfate proteoglycan interact with each other. Such interactions in situ may determine the structure of basement membranes.
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism*; D011508:Chondroitin Sulfate Proteoglycans / Q000378:metabolism*; D002846:Chromatography, Affinity; D003094:Collagen / Q000378:metabolism*; D004797:Enzyme-Linked Immunosorbent Assay; D006025:Glycosaminoglycans / Q000378:metabolism*; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate / Q000378:metabolism*; D007700:Kinetics; D007797:Laminin / Q000378:metabolism*; D008565:Membrane Proteins / Q000302:isolation & purification; D008970:Molecular Weight; D011485:Protein Binding; D011509:Proteoglycans / Q000378:metabolism*
D011508:Chondroitin Sulfate Proteoglycans; D003094:Collagen; D006025:Glycosaminoglycans; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate; D007797:Laminin; D008565:Membrane Proteins; D011509:Proteoglycans