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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1993-4-1
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pubmed:abstractText |
Fibroblasts interact with the extracellular matrix through cell-surface receptors belonging to the integrin family. In this report, we present evidence that cultured normal human fibroblasts express the integrin alpha 4 beta 1 and that this receptor facilitates fibroblast attachment to fibronectin. Fluorescence-activated cell sorter analysis and immunoprecipitation with monoclonal antibodies demonstrated that normal dermal fibroblasts express the alpha 4-subunit on the cell surface, primarily in association with the beta 1-subunit. Cell-attachment assays demonstrated that normal human fibroblasts can attach to the 40-kDa fibronectin fragment containing the type III connecting segment domain recognized by alpha 4 beta 1. Adhesion to this fragment was inhibited by anti-alpha 4 antibody. Furthermore, our results indicate that alpha 4 beta 1 collaborates with another fibronectin receptor, alpha 5 beta 1, during fibroblast attachment to full-length fibronectin. The region of fibronectin recognized by alpha 5 beta 1 contains the amino acid sequence arg-gly-asp (RGD). A short synthetic RGD peptide, or the 120-kDa fibronectin fragment containing the RGD sequence, only partially inhibited attachment to full-length fibronectin, suggesting that fibroblasts utilize more than the RGD recognition sequence for binding to fibronectin. Accordingly, RGD peptide combined with anti-alpha 4 antibody produced more potent inhibition of cell attachment than either reagent alone. These observations show for the first time that functional alpha 4 beta 1 fibronectin receptor is not restricted to lymphoid cells and transformed cells.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0022-202X
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
100
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
323-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8440915-Amino Acid Sequence,
pubmed-meshheading:8440915-Antibodies, Monoclonal,
pubmed-meshheading:8440915-Cell Adhesion,
pubmed-meshheading:8440915-Cell Separation,
pubmed-meshheading:8440915-Fibroblasts,
pubmed-meshheading:8440915-Flow Cytometry,
pubmed-meshheading:8440915-Humans,
pubmed-meshheading:8440915-Integrins,
pubmed-meshheading:8440915-Male,
pubmed-meshheading:8440915-Molecular Sequence Data,
pubmed-meshheading:8440915-Oligopeptides,
pubmed-meshheading:8440915-Precipitin Tests,
pubmed-meshheading:8440915-Receptors, Fibronectin,
pubmed-meshheading:8440915-Skin
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pubmed:year |
1993
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pubmed:articleTitle |
Expression of functional alpha 4 beta 1 integrin by human dermal fibroblasts.
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pubmed:affiliation |
Department of Dermatology, State University of New York, Stony Brook 11794-8165.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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