Basal lamina assembly
From studies of the ‘classical’ components, models for the assembly and structure of an idealized basal lamina have been developed. In particular, the evidence supports the concept of enmeshed collagen and laminin polymers, in which nidogen/entactin acts as a bridge between these molecules and provi...
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| Veröffentlicht in: | Current opinion in cell biology 1994-10, Vol.6 (5), p.674-681 |
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| container_title | Current opinion in cell biology |
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| creator | Yurchenco, Peter D. O'Rear, Julian J. |
| description | From studies of the ‘classical’ components, models for the assembly and structure of an idealized basal lamina have been developed. In particular, the evidence supports the concept of enmeshed collagen and laminin polymers, in which nidogen/entactin acts as a bridge between these molecules and provides anchorage for diverse matrix components. Different basement membranes, however, possess different members of the basic basal lamina families, such as the newly described α(IV) collagen, α2(merosin) laminin, and β3 laminin (in kalinin/nicein) chains. Even though these members share homologous domains and sequences, and are likely to share certain functions, they also possess unique characteristics that are expected to provide for basal lamina heterogeneity. A combination of genetic, recombinant and biochemical approaches are now being applied to elucidate the special roles of both old and new components. |
| doi_str_mv | 10.1016/0955-0674(94)90093-0 |
| format | Article |
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A combination of genetic, recombinant and biochemical approaches are now being applied to elucidate the special roles of both old and new components.</description><subject>Animals</subject><subject>Basement Membrane - chemistry</subject><subject>Calcium-Binding Proteins - chemistry</subject><subject>Collagen - chemistry</subject><subject>Collagen - genetics</subject><subject>Drosophila</subject><subject>Heparan Sulfate Proteoglycans</subject><subject>Heparitin Sulfate - chemistry</subject><subject>Humans</subject><subject>Laminin - chemistry</subject><subject>Membrane Glycoproteins - chemistry</subject><subject>Membrane Proteins - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>Proteoglycans - chemistry</subject><issn>0955-0674</issn><issn>1879-0410</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1Lw0AQhhdRaq0evSn0JHqIzn5kd-ciaPELCl70vGw2E1hJmppthf57E1p6VBiYwzzvO_AwdsHhlgPXd4B5noE26hrVDQKgzOCAjbk1mIHicMjGe-SYnaT0BQAaBI7YyFgpQZkxO3_0ydfT2jdx4ac-JWqKenPKjipfJzrb7Qn7fH76mL1m8_eXt9nDPAvS2lVGGLiocgKlisoLr1TQ3ORFqaURwJUSnOdAFgMgCiy1lmhsGUphLQqr5IRdbXuXXfu9prRyTUyB6tovqF0nZ4zhKuf4L8h1bo1A24NqC4auTamjyi272Phu4zi4QZsbnLjBicN-Bm0O-tjlrn9dNFTuQztP_f1-e6fexk-kzqUQaRGojB2FlSvb-PeDX6QmeA8</recordid><startdate>19941001</startdate><enddate>19941001</enddate><creator>Yurchenco, Peter D.</creator><creator>O'Rear, Julian J.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19941001</creationdate><title>Basal lamina assembly</title><author>Yurchenco, Peter D. ; O'Rear, Julian J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c388t-e9c12f5e044bfa2a44c6175bd6372014421150e89c09929d663978dcd28892843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Basement Membrane - chemistry</topic><topic>Calcium-Binding Proteins - chemistry</topic><topic>Collagen - chemistry</topic><topic>Collagen - genetics</topic><topic>Drosophila</topic><topic>Heparan Sulfate Proteoglycans</topic><topic>Heparitin Sulfate - chemistry</topic><topic>Humans</topic><topic>Laminin - chemistry</topic><topic>Membrane Glycoproteins - chemistry</topic><topic>Membrane Proteins - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>Proteoglycans - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yurchenco, Peter D.</creatorcontrib><creatorcontrib>O'Rear, Julian J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Current opinion in cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yurchenco, Peter D.</au><au>O'Rear, Julian J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Basal lamina assembly</atitle><jtitle>Current opinion in cell biology</jtitle><addtitle>Curr Opin Cell Biol</addtitle><date>1994-10-01</date><risdate>1994</risdate><volume>6</volume><issue>5</issue><spage>674</spage><epage>681</epage><pages>674-681</pages><issn>0955-0674</issn><eissn>1879-0410</eissn><abstract>From studies of the ‘classical’ components, models for the assembly and structure of an idealized basal lamina have been developed. 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| ispartof | Current opinion in cell biology, 1994-10, Vol.6 (5), p.674-681 |
| issn | 0955-0674 1879-0410 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Animals Basement Membrane - chemistry Calcium-Binding Proteins - chemistry Collagen - chemistry Collagen - genetics Drosophila Heparan Sulfate Proteoglycans Heparitin Sulfate - chemistry Humans Laminin - chemistry Membrane Glycoproteins - chemistry Membrane Proteins - chemistry Models, Molecular Molecular Structure Proteoglycans - chemistry |
| title | Basal lamina assembly |
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