The specificity of integrin-ligand interactions in cultured human renal epithelium

Maeve A. Rahilly, Stewart Fleming

    Research output: Contribution to journalArticle

    6 Citations (Scopus)

    Abstract

    Members of the ß1 integrin family are present at the basolateral membrane of human renal tubular 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 alpha 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.
    Original languageEnglish
    Pages (from-to)297-303
    Number of pages7
    JournalJournal of Pathology
    Volume170
    Issue number3
    DOIs
    Publication statusPublished - 1993

    Fingerprint

    Integrins
    Epithelium
    Ligands
    Kidney
    Cell Adhesion
    arginyl-glycyl-aspartyl-serine
    Integrin alpha Chains
    Cell Surface Receptors
    Laminin
    Fibronectins
    Aspartic Acid
    Glycine
    Plastics
    Arginine
    Epithelial Cells
    Monoclonal Antibodies
    Peptides
    Membranes

    Cite this

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    title = "The specificity of integrin-ligand interactions in cultured human renal epithelium",
    abstract = "Members of the {\ss}1 integrin family are present at the basolateral membrane of human renal tubular 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 alpha 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.",
    author = "Rahilly, {Maeve A.} and Stewart Fleming",
    year = "1993",
    doi = "10.1002/path.1711700313",
    language = "English",
    volume = "170",
    pages = "297--303",
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    }

    The specificity of integrin-ligand interactions in cultured human renal epithelium. / Rahilly, Maeve A.; Fleming, Stewart.

    In: Journal of Pathology, Vol. 170, No. 3, 1993, p. 297-303.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - The specificity of integrin-ligand interactions in cultured human renal epithelium

    AU - Rahilly, Maeve A.

    AU - Fleming, Stewart

    PY - 1993

    Y1 - 1993

    N2 - Members of the ß1 integrin family are present at the basolateral membrane of human renal tubular 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 alpha 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.

    AB - Members of the ß1 integrin family are present at the basolateral membrane of human renal tubular 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 alpha 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.

    U2 - 10.1002/path.1711700313

    DO - 10.1002/path.1711700313

    M3 - Article

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    VL - 170

    SP - 297

    EP - 303

    JO - Journal of Pathology

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