Macromolecular organization of basement membranes

A considerable variety of basement membrane components, including in particular more than ten laminin isoforms and their novel α chains (α3, α4 and α5), has been characterized in recent studies. The functional properties of these components are increasingly being analyzed by recombinant technologies...

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Bibliographic Details
Published in:Current opinion in cell biology 1996-10, Vol.8 (5), p.618-624
Main Author: Timpl, Rupert
Format: Article
Language:English
Subjects:
Animals
Basement Membrane - metabolism
Binding Sites
Epitopes - chemistry
Humans
Laminin - chemistry
Laminin - genetics
Laminin - immunology
Laminin - metabolism
Membrane Proteins - chemistry
Membrane Proteins - metabolism
Receptors, Cell Surface
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
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Summary:A considerable variety of basement membrane components, including in particular more than ten laminin isoforms and their novel α chains (α3, α4 and α5), has been characterized in recent studies. The functional properties of these components are increasingly being analyzed by recombinant technologies and by structural studies at atomic resolution, techniques which led to the elucidation of the nidogen-binding epitope on the laminin γ1 chain. Novel insights into functions of basement membrane components have been obtained from gene-targeting experiments and studies of mutated genes identified in inherited disorders.
ISSN:0955-0674
1879-0410
DOI:10.1016/S0955-0674(96)80102-5