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          Institute: MPI für Biochemie     Collection: Emeriti Groups     Display Documents



ID: 41659.0, MPI für Biochemie / Emeriti Groups
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
Authors:Salmivirta, K.; Talts, J. F.; Olsson, M.; Sasaki, T.; Timpl, R.; Ekblom, P.
Language:English
Date of Publication (YYYY-MM-DD):2002-10-01
Title of Journal:Experimental Cell Research
Journal Abbrev.:Exp. Cell Res.
Volume:279
Issue / Number:2
Start Page:188
End Page:201
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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).
Free Keywords:nidogen; laminin; basement membrane; epithelial-mesenchymal interactions; cell adhesion
Comment of the Author/Creator:Date: 2002, OCT 1
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Emeriti Groups/Protein Chemistry (R. Timpl)
MPI für Biochemie/Molecular Medicine (R. Fässler)/Extracellular Matrix Proteins (T. Sasaki)
External Affiliations:Uppsala Univ, Dept Cell & Mol Biol, Uppsala, Sweden; Uppsala Univ, Dept Cell & Mol Biol, Uppsala, Sweden;Lund Univ, Dept Cell & Mol Biol, S-22184 Lund, Sweden
Identifiers:ISI:000178224700003 [ID No:1]
ISSN:0014-4827 [ID No:2]
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