Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV.
The laminin-nidogen complex and purified nidogen both bind collagen IV but not other collagens, as shown by solid-state ligand-binding and inhibition assays. Laminin purified from the dissociated complex and a variety of laminin proteolytic fragments failed to bind collagen IV. Complexes formed in solution between nidogen or laminin-nidogen and collagen IV were visualized by rotary shadowing which identified one major binding site about 80 nm away from the C-terminus of the collagen triple helix. A second, weaker binding site may exist closer to its N-terminus. Binding sites of nidogen were assigned to its C-terminal globular domain which also possesses laminin-binding structures. A more diverse collagen-IV-binding pattern was observed for the laminin nidogen complex, whereby interactions may involve both nidogen and short-arm structures of laminin.
Aumailley
M
M
Max-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
Wiedemann
H
H
Mann
K
K
Timpl
R
R
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D003094:Collagen / Q000378:metabolism* / Q000648:ultrastructure; D019791:Guanidine; D006146:Guanidines; D007106:Immune Sera; D007700:Kinetics; D007797:Laminin / Q000302:isolation & purification / Q000378:metabolism*; D008024:Ligands; D008562:Membrane Glycoproteins; D008565:Membrane Proteins / Q000378:metabolism* / Q000648:ultrastructure; D051379:Mice; D008854:Microscopy, Electron; D009363:Neoplasm Proteins / Q000378:metabolism*; D011485:Protein Binding
D006146:Guanidines; D007106:Immune Sera; D007797:Laminin; D008024:Ligands; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009363:Neoplasm Proteins; C029967:nidogen; D003094:Collagen; D019791:Guanidine