Macromolecular organization of basement membranes.
A considerable variety of basement membrane components, including in particular more than ten laminin isoforms and their novel alpha chains (alpha3, alpha4 and alpha5), 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 gamma1 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.
Timpl
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Department of Protein Chemistry, Max-Planck-Institut für Biochemie, 82152 Martinsried, Germany. TIMPL@vms.biochem.mpg.de
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D001665:Binding Sites; D000939:Epitopes / Q000737:chemistry; D006801:Humans; D007797:Laminin / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D000939:Epitopes; D007797:Laminin; D008565:Membrane Proteins; D011956:Receptors, Cell Surface; D011994:Recombinant Proteins