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Expression of functional alpha-4-beta-1 integrin by human dermal fibroblasts

, : Expression of functional alpha-4-beta-1 integrin by human dermal fibroblasts. Journal Of Investigative Dermatology. 100(3): 323-328

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 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 peptide, or the 120-kDa fibronectin fragment containing the RGD sequence, only partially inhibited attachment to full-length fibronectin, suggesting the 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.


PMID: 8440915

DOI: 10.1111/1523-1747.ep12470011

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