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Inhibition of Human Platelet Glycoprotein IIB/IIIA Binding to Fibrinogen by Tumor Cell Membrane Proteins¹

Blood Research Institute, Saint Michael's Medical Center, Newark 07102, New Jersey [M. K., K. C., J. L., Y. S. A.], and Seton Hall University School of Graduate Medical Education, South Orange 07079 [M. K., Y. S. A.], New Jersey

² To whom requests for reprints should be addressed, at Blood Research Institute, Saint Michael's Medical Center, 268 Dr. Martin Luther King Jr. Boulevard, Newark, NJ 07102.

Immunochemical and functional characteristics of tumor cell membrane proteins and human platelet glycoproteins were studied. Immunoblotting revealed that membrane proteins of a cultured breast tumor cell line (BT-20) had three protein bands, which were each recognized by monoclonal antibodies to human platelet glycoprotein Ib, IIb, and IIIa, suggesting some immunochemical similarities between the tumor cell membrane proteins and platelet glycoproteins. The monoclonal antibodies failed to bind to an extract of a lung tumor cell line (A549). Neither tumor extract induced platelet aggregation. However, tumor-associated antigens isolated from the breast tumor cells markedly inhibited platelet glycoprotein IIb/IIIa binding to fibrinogen. In contrast, tumor-associated antigens from the lung tumor cells had no effect. These results suggest that tumor cells which have immunological and/or structural similarities to platelets may affect hemostasis and coagulation in vivo.

¹ Supported in part by the Department of Health, State of New Jersey Health Service Contract no. 92-130SCH-00.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Received 10/ 6/92. Accepted 11/24/92.