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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2005-9-5
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pubmed:abstractText |
The extracellular matrix provides a framework for cell adhesion, supports cell movement, and serves to compartmentalize tissues into functional units. Fibronectin is a core component of many extracellular matrices where it regulates a variety of cell activities through direct interactions with cell surface integrin receptors. Fibronectin is synthesized by many adherent cells which then assemble it into a fibrillar network. The assembly process is integrin-dependent and fibronectin-integrin interactions initiate a step-wise process involving conformational activation of fibronectin outside and organization of the actin cytoskeleton inside. During assembly, fibronectin undergoes conformational changes that expose fibronectin-binding sites and promote intermolecular interactions needed for fibril formation. In this review, the main steps of fibronectin assembly are described and recent studies on fibronectin conformational changes are discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0945-053X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
389-99
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16061370-Actins,
pubmed-meshheading:16061370-Animals,
pubmed-meshheading:16061370-Binding Sites,
pubmed-meshheading:16061370-CHO Cells,
pubmed-meshheading:16061370-Cell Adhesion,
pubmed-meshheading:16061370-Cricetinae,
pubmed-meshheading:16061370-Cytoskeleton,
pubmed-meshheading:16061370-Dimerization,
pubmed-meshheading:16061370-Extracellular Matrix,
pubmed-meshheading:16061370-Fibronectins,
pubmed-meshheading:16061370-Humans,
pubmed-meshheading:16061370-Integrin alpha5beta1,
pubmed-meshheading:16061370-Integrins,
pubmed-meshheading:16061370-Macromolecular Substances,
pubmed-meshheading:16061370-Models, Biological,
pubmed-meshheading:16061370-Models, Molecular,
pubmed-meshheading:16061370-Protein Conformation,
pubmed-meshheading:16061370-Protein Folding,
pubmed-meshheading:16061370-Protein Structure, Tertiary,
pubmed-meshheading:16061370-Rats,
pubmed-meshheading:16061370-Signal Transduction
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pubmed:year |
2005
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pubmed:articleTitle |
Fibronectin fibrillogenesis, a cell-mediated matrix assembly process.
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pubmed:affiliation |
Department of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, United States.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, N.I.H., Extramural
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