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PMID: 2653817 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Structure and biological activity of basement membrane proteins.

European journal of biochemistry ·Vol. 180 ·No. 3 ·1989-04-01 ·Pages 487-502

Timpl R

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.

MeSH Terms
Animals Basement Membrane/analysis Humans Membrane Proteins/analysis Structure-Activity Relationship
Chemicals
Membrane Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Timpl R
Max-Planck-Institut für Biochemie, Martinsried.
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1989-04-01
Pages
487-502
Language
English
Region
England
NLM ID
0107600
Subset
IM
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