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Review
. 1989 Apr 1;180(3):487-502.
doi: 10.1111/j.1432-1033.1989.tb14673.x.

Structure and biological activity of basement membrane proteins

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Free article
Review

Structure and biological activity of basement membrane proteins

R Timpl. Eur J Biochem. .
Free article

Abstract

Collagen type IV, laminin, heparan sulfate proteoglycans, nidogen (entactin) and BM-40 (osteonectin, SPARC) represent major structural proteins of basement membranes. They are well-characterized in their domain structures, amino acid sequences and potentials for molecular interactions. Such interactions include self-assembly processes and heterotypic binding between individual constituents, as well as binding of calcium (laminin, BM-40) and are likely to be used for basement membrane assembly. Laminin, collagen IV and nidogen also possess several cell-binding sites which interact with distinct cellular receptors. Some evidence exists that those interactions are involved in the control of cell behaviour. These observations have provided a more defined understanding of basement membrane function and the definition of new research goals in the future.

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