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

• Published in: The Journal of experimental medicine Vol. 173; no. 5; pp. 1111 - 1119
• Main Authors: CHEN, F. A, REPASKY, E. A, BANKERT, R. B
• Format: Journal Article
• Language: English
• Published: New York, NY Rockefeller University Press 01-05-1991; The Rockefeller University Press
• Subjects: antigen (tumor-associated); Antigens, Tumor-Associated, Carbohydrate - analysis; Antigens, Tumor-Associated, Carbohydrate - genetics; Antigens, Tumor-Associated, Carbohydrate - metabolism; Biological and medical sciences; Biomarkers, Tumor - analysis; Blotting, Northern; carcinoma; Cell Adhesion Molecules - analysis; Cell Adhesion Molecules - genetics; Cell Adhesion Molecules - metabolism; Collagen - metabolism; Electrophoresis, Polyacrylamide Gel; Extracellular Matrix Proteins - chemistry; Extracellular Matrix Proteins - metabolism; Gene Expression Regulation, Neoplastic - physiology; Host-tumor relations. Immunology. Biological markers; Humans; Laminin - metabolism; Lung Neoplasms - etiology; Lung Neoplasms - metabolism; Lung Neoplasms - pathology; Medical sciences; Neoplasm Metastasis - physiopathology; Precipitin Tests; Receptors, Very Late Antigen - analysis; Receptors, Very Late Antigen - genetics; Receptors, Very Late Antigen - metabolism; Tumor Cells, Cultured - metabolism; Tumor Cells, Cultured - pathology; Tumor Cells, Cultured - ultrastructure; Tumors; VLA-2 antigen; Human; Northern blotting; Integrin; Tumor associated antigen; Gel electrophoresis; Pathogenesis; Lung; Extracellular matrix; Tumor; Molecular complex; Identification; Comparative study
• ISSN: 0022-1007; 1540-9538
• DOI: 10.1084/jem.173.5.1111

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.