Laminin, proteoglycan, nidogen and collagen IV: structural models and molecular interactions.
Major components of basement membranes, including collagen IV, laminin, heparan sulphate proteoglycan and nidogen, were isolated from the matrix of the EHS sarcoma. The purified components were analysed for their domain structure and for the participation of distinct domains in molecular interactions and cell binding. Collagen IV consists of four domains which have triple helical or non-collagenous structures. Self-assembly of the protein into a network-like organization occurs by specific interactions between N-terminal triple helical segments and between the C-terminal globules. Cell binding requires a central triple helical segment. Laminin has the shape of an asymmetrical cross; different globular domains within this structure mediate binding to proteoglycan and to cells. The proteoglycan consists of four heparan sulphate chains attached to a small protein core. These chains have the potential to bind laminin, fibronectin and collagen IV. Nidogen was isolated in several molecular forms which showed either self-aggregation or binding to laminin.
D000818:Animals; D001485:Basement Membrane / Q000648:ultrastructure*; D002448:Cell Adhesion; D003094:Collagen / Q000378:metabolism*; D005109:Extracellular Matrix / Q000648:ultrastructure*; D007797:Laminin / Q000378:metabolism*; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism*; D008854:Microscopy, Electron; D011485:Protein Binding; D011487:Protein Conformation; D011509:Proteoglycans / Q000378:metabolism*
D007797:Laminin; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D011509:Proteoglycans; C029967:nidogen; D003094:Collagen