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Characterization of a Membrane-associated Glycoprotein (gp 43) on Human Hepatocellular Carcinoma by a Monoclonal Antibody¹

Hipple Cancer Research Center, Dayton, Ohio [J. P. F., M. J. M., J. N. Y.], and Shanghai Institute of Cell Biology, Shanghai, China [H. X., Z. Y.]

A monoclonal antibody, Hepama-1, produced by immunizing mice with cells of a human hepatocellular carcinoma cell line, has been used to identify and characterize a previously unreported antigen present on the surface of human hepatocellular carcinoma cells. The antigen occurred on the membranes of human hepatoma cell lines and tumor biopsies but was not detectable in tumors of other origin or normal tissues. Binding was determined by enzyme-linked immunoabsorbent assay and immunofluorescence on cell lines and by immunoperoxidase staining of tissue sections. In immunofluorescence studies, Hepama-1 antibodies stained five out of six human hepatoma cell lines, showed only slight binding to breast tumor cell lines, but failed to stain colon tumor or normal cell lines. The antihepatoma antibody exhibited positive immunoperoxidase staining of human liver tumor sections but did not stain tumors of other origin. Hepama-1 bound specifically to a membrane glycoprotein with an approximate molecular weight of 43,000. Western blot and solid phase enzyme-linked immunoabsorbent assay analysis showed that the 43-kD antigen occurred on five of six human hepatoma cell lines and was expressed by every human hepatocellular carcinoma biopsy tested. This cell surface molecule represents a potentially useful target for immunotherapy and localization of human hepatocellular carcinomas.

¹ Supported in part by USPHS Grant CA45885 from the National Cancer Institute.

² To whom requests for reprints should be addressed, at Hipple Cancer Research Center, 4100 South Kettering Boulevard, Dayton, OH 45439-2092.

Received 8/15/90. Accepted 2/ 7/91.