Journal of Experimental Medicine, Vol 173, 1111-1119, Copyright © 1991 by Rockefeller University Press

ARTICLES

Human lung tumor-associated antigen identified as an extracellular matrix adhesion molecule

FA Chen, EA Repasky and RB Bankert
Roswell Park Cancer Institute, (Unit of New York State Department of Health), Department of Molecular Immunology, Buffalo, New York 14263.

A single chain glycoprotein with an estimated molecular mass of 160 kD (gp160) was previously identified as a human lung tumor-associated antigen. This tumor marker is shown here to be associated noncovalently with a second 130-kD protein. Sequential immunoprecipitation studies of surface iodinated lung tumor cell lysates reveal that this heterodimeric complex is indistinguishable serologically and structurally from the integrin VLA-2, found originally on activated T lymphocytes and platelets. The VLA-2-like complex expressed on the lung tumors possesses similar characteristic Mg2+ dependent binding of collagen and laminin as observed with VLA-2 on normal cells. RNA analysis indicates that human lung tumors express at least 20 times more VLA-2 alpha chain message than normal adult human lung tissue. The results presented here raise the possibility that the overproduction of VLA-2 may be involved in the pathogenesis of human lung tumors by modulating the invasive and metastatic potential of the tumor.
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