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Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78606

Sasaki,  T.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78797

Timpl,  R.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Salmivirta, K., Talts, J. F., Olsson, M., Sasaki, T., Timpl, R., & Ekblom, P. (2002). Binding of mouse nidogen-2 to basement membrane components and cells and its expression in embryonic and adult tissues suggest complementary functions of the two nidogens. Experimental Cell Research, 279(2), 188-201.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6E2E-C
Abstract
Nidogen-1 binds several basement membrane components by well- defined, domain-specific interactions. Organ culture and gene targeting approaches suggest that a high-affinity nidogen- binding site of the laminin gamma1 chain (y1III4) is important for kidney development and for nerve guidance. Other proteins may also bind gamma1III4, although human nidogen-2 binds poorly to the mouse laminin gamma1 chain. We therefore characterized recombinant mouse nidogen-2 and its binding to basement membrane proteins and cells. Mouse nidogen-1 and -2 interacted at comparable levels with collagen IV, perlecan, and fibulin-2 and, most notably, also with laminin-1 fragments P1 and gamma1III3-5, which both contain the gamma1III4 module. In embryos, nidogen-2 mRNA was produced by mesenchyme at sites of epithelial-mesenchymal interactions, but the protein was deposited on epithelial basement membranes, as previously shown for nidogen-1. Hence, binding of both nidogens to the epithelial laminin gamma1 chain is dependent on epithelial- mesenchymal interactions. Epidermal growth factor stimulated expression of both nidogens in embryonic submandibular glands. Both nidogens were found in all studied embryonic and adult basement membranes. Nidogen-2 was more adhesive than nidogen-1 for some cell lines and was mainly mediated by alpha3beta1 and alpha6beta1 integrins as shown by antibody inhibition. These findings revealed extensive coregulation of nidogen-1 and -2 expression and much more complementary functions of the two nidogens than previously recognized. (C) 2002 Elsevier Science (USA).