A novel vitronectin receptor integrin (alpha v beta x) is responsible for distinct adhesive properties of carcinoma cells.

Cheresh DA, Smith JW, Cooper HM, Quaranta V
Cell. 1989 57 (1): 59-69

PMID: 2467745 · DOI:10.1016/0092-8674(89)90172-4

Carcinoma cells express a novel integrin involved in cell adhesion to vitronectin, but not to fibrinogen or von Willebrand factor, whereas melanoma and endothelial cells express a vitronectin receptor (alpha v beta 3) that promotes cell attachment to all of these matrix components. The integrin responsible for this adhesive phenotype of carcinoma cells is composed of an alpha subunit that is indistinguishable from the alpha v of the vitronectin receptor and a beta subunit (beta x) that is distinct from any known integrin beta subunit. Accordingly, Northern blot analysis identifies an mRNA for alpha v, but not for beta 3 in carcinoma cells. This receptor appears to mediate cell adhesion to vitronectin as well as fibronectin since an antibody directed to its alpha subunit blocked carcinoma cell adhesion to both of these matrix proteins. These results suggest that homologous integrins with identical alpha subunits and structurally distinct beta subunits can account for the functional recognition of different matrixes by two cell types.

MeSH Terms (20)

Adenocarcinoma Amino Acid Sequence Blotting, Northern Cell Adhesion Cell Line Electrophoresis, Gel, Two-Dimensional Fibrinogen Fibroblasts Fibronectins Glycoproteins Humans Integrins Lung Neoplasms Melanoma Membrane Glycoproteins Receptors, Immunologic Receptors, Vitronectin RNA, Messenger Vitronectin von Willebrand Factor

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