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April 1, 1989European Journal of Biochemistry972 citationsOpen Access

Structure and biological activity of basement membrane proteins

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RTRupert Timpl

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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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Cite This Study

Rupert Timpl (1989) studied this question.

synapsesocial.com/papers/6a20b557e2a660d176234d52https://doi.org/10.1111/j.1432-1033.1989.tb14673.x
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Type IV collagen from chicken muscular tissues. Isolation and characterization of the pepsin-resistant fragments1980 · 73 citations
  2. 2Laminin, a multidomain protein. The A chain has a unique globular domain and homology with the basement membrane proteoglycan and the laminin B chains.1988 · 482 citations
  3. 3Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains.1988 · 134 citations
  4. 4Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor1986 · 157 citations
  5. 5Two distinct cell-binding domains in laminin can independently promote nonneuronal cell adhesion and spreading [published erratum appears in J Cell Biol 1989 Jun;108(6):following 2546]1987 · 195 citations