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[Cancer Research 40, 2153-2159, July 1, 1980]
© 1980 American Association for Cancer Research

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Distribution of a Tumor Cell Surface Protein Common to Several Murine Lung Carcinomas1

Stephen J. Kennel2, Patricia K. Lankford, Linda J. Foote, Frank S. Tsakeres, Laurel M. Adams and Robert L. Ullrich

Biology Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830

In previous work with line 1, a spontaneous BALB/c alveolar carcinoma, we identified a surface protein with a molecular weight of 180,000 (TSP-180) on tumor cells but not on normal mouse cells. This protein was not identical to known cell surface proteins or any C-type virus protein. In this report, we have continued to characterize TSP-180. It can be labeled metabolically with [3H]leucine or [3H]glucosamine, confirming that it is a glycoprotein synthesized by line 1 cells. In addition, a competition radioimmunoassay using radioiodinated TSP-180 from line 1 cells was used to measure the amount of TSP-180 in tissues of tumor-bearing animals as well as in other tissues and cells. It was found that during tumor growth, TSP-180 accumulates in the area of primary tumor to a plateau level. It is not detected in other organs except that small amounts are detected in serum when the primary tumor exceeds 1 cm in diameter. No evidence of cross-reactive material was found using BALB/c fibroblasts, mouse mammary tumor cells, BALB/c embryonic tissues, rat tracheal tumor cells, or human alveolar tumor cells. Complete competition was obtained using line 1 tissue culture cell or extracted tumor proteins. Carcinomas from two other mouse strains were also good competitors while adenomas of BALB/c lung competed weakly. Proteins from six other BALB/c lung carcinoma cell lines derived from radiation- or chemically-induced tumors as well as tumors of spontaneous origin were also found to compete efficiently in the radioimmunoassay. The presence of TSP-180 on the surfaces of these lung carcinoma cell lines was confirmed using radioiodination catalyzed by lactoperoxidase. Partial protease digests of TSP-180 isolated from four of these lines showed identical molecular weight patterns indicating a highly conserved sequence homology. These results strongly suggest that TSP-180 represents a cell surface protein common to several tumors of the lung carcinoma class. The feasibility of using TSP-180 antigenic determinants for early detection of radiation- or chemically-induced tumors, for monitoring progression of metastases, or as targets for directed drug delivery is discussed.

1 This is Paper 2 in a series of papers on this subject. Research sponsored by NIH Grant CA 24553-01 and the Office of Health and Environmental Research, United States Department of Energy, under Contract W-7405-eng-26 with the Union Carbide Corporation.

2 To whom requests for reprints should be addressed.

Received 12/26/79. Accepted 3/21/80.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
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Molecular Cancer Research Cancer Prevention Research
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Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1980 by the American Association for Cancer Research.