pubmed-article:8440915 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C0221928 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C1334087 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C1416496 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
pubmed-article:8440915 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
pubmed-article:8440915 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:8440915 | pubmed:dateCreated | 1993-4-1 | lld:pubmed |
pubmed-article:8440915 | 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. | lld:pubmed |
pubmed-article:8440915 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8440915 | pubmed:language | eng | lld:pubmed |
pubmed-article:8440915 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8440915 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8440915 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8440915 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8440915 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8440915 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8440915 | pubmed:month | Mar | lld:pubmed |
pubmed-article:8440915 | pubmed:issn | 0022-202X | lld:pubmed |
pubmed-article:8440915 | pubmed:author | pubmed-author:ClarkR ARA | lld:pubmed |
pubmed-article:8440915 | pubmed:author | pubmed-author:GailitJJ | lld:pubmed |
pubmed-article:8440915 | pubmed:author | pubmed-author:Pierschbacher... | lld:pubmed |
pubmed-article:8440915 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8440915 | pubmed:volume | 100 | lld:pubmed |
pubmed-article:8440915 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8440915 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8440915 | pubmed:pagination | 323-8 | lld:pubmed |
pubmed-article:8440915 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:8440915 | pubmed:meshHeading | pubmed-meshheading:8440915-... | lld:pubmed |
pubmed-article:8440915 | pubmed:year | 1993 | lld:pubmed |
pubmed-article:8440915 | pubmed:articleTitle | Expression of functional alpha 4 beta 1 integrin by human dermal fibroblasts. | lld:pubmed |
pubmed-article:8440915 | pubmed:affiliation | Department of Dermatology, State University of New York, Stony Brook 11794-8165. | lld:pubmed |
pubmed-article:8440915 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8440915 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8440915 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:3676 | entrezgene:pubmed | pubmed-article:8440915 | lld:entrezgene |
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