Changes in integrin receptors on oncogenically transformed cells.
Oncogenically transformed cells show reduced assembly of fibronectin-rich extracellular matrixes and diminished ability to adhere to fibronectin. The molecular bases of these phenotypic alteration are not fully understood. We report here alterations in the spectrum of integrins, including two fibronectin receptors, on oncogenic transformation of rodent cells. Transformation of rat1, NRK, and Nil8 cells by Rous sarcoma virus or by murine sarcoma viruses encoding ras oncogenes leads to reductions in the level of integrin alpha 5 beta 1, which is a well-defined fibronectin receptor, and of two other integrin receptors. In contrast, another receptor, alpha 3 beta 1, which is a polyspecific receptor for fibronectin, laminin, and collagen, is retained by transformed cells. These results provide explanations for earlier results concerning the interactions of extracellular matrix proteins with the surfaces of tumor cells and offer leads to further understanding of the altered adhesive and migratory behavior of malignant cells.
Plantefaber
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LC
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.
Hynes
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D000818:Animals; D002448:Cell Adhesion; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D005353:Fibronectins / Q000378:metabolism; D011905:Genes, ras; D016023:Integrins; D007700:Kinetics; D008562:Membrane Glycoproteins / Q000502:physiology*; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic / Q000502:physiology*
D005353:Fibronectins; D016023:Integrins; D008562:Membrane Glycoproteins; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic