Identification and interaction repertoire of large forms of the basement membrane protein nidogen.

AUTOR(ES)

Dziadek, M

RESUMO

Nidogen was purified in its genuine form with a mol. wt. of 150 000 (Nd-150) and as fragments with mol. wts. of 100 000 (Nd-100) and 80 000 (Nd-80) from a mouse tumor basement membrane by preventing activity of endogenous proteases with 6 M guanidine and protease inhibitors. The larger forms of nidogen were also identified in stable complexes with laminin in neutral salt extracts of the tumor and in cell culture medium. Purified Nd-150 and Nd-100, but not Nd-80, were shown to interact with laminin in various binding assays, albeit with lower potential than estimated for the genuine complexes formed in situ. Binding of Nd-150 and Nd-100 to fibronectin and to the globular domain of collagen IV was also observed, but not to heparan sulfate proteoglycan.

Documentos Relacionados

• Antibodies to basement membrane protein nidogen in Chagas' disease and American cutaneous leishmaniasis.
• The Absence of Nidogen 1 Does Not Affect Murine Basement Membrane Formation
• Gene Structure and Functional Analysis of the Mouse Nidogen-2 Gene: Nidogen-2 Is Not Essential for Basement Membrane Formation in Mice
• Amino acid sequence of mouse nidogen, a multidomain basement membrane protein with binding activity for laminin, collagen IV and cells.
• Interaction of lipopolysaccharides of Helicobacter pylori with basement membrane protein laminin.