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The specificity of integrin‐ligand interactions in cultured human renal epithelium
Author(s) -
Rahilly Maeve A.,
Fleming Stewart
Publication year - 1993
Publication title -
the journal of pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.964
H-Index - 184
eISSN - 1096-9896
pISSN - 0022-3417
DOI - 10.1002/path.1711700313
Subject(s) - integrin , fibronectin , epithelium , laminin , microbiology and biotechnology , cell adhesion , cell adhesion molecule , epithelial polarity , receptor , biology , adhesion , chemistry , cell surface receptor , cell , extracellular matrix , biochemistry , genetics , organic chemistry
Members of the β1 integrin family are present at the basolateral membrane of human renal tubuiar epithelium in vivo and at the ventral surfaces of cultured renal epithelial cells, at‐the sites appropriate for cell substratum adhesion. In this study we have proven that these molecules are indeed functional in mediating cell substratum attachment in normal human renal epithelium by using monoclonal antibodies to integrin α subunits to block initial cell attachment. The importance of arginine‐glycine‐aspartic acid (RGD) recognition by cell surface receptors in various extracellular ligands was also examined using synthetic peptides. RGDS peptide strongly inhibited attachment to plain plastic or fibronectin‐coated substrata but had no effect on cell adhesion to laminin‐coated coverslips.