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Involvement of Platelet Membrane Glycoprotein Ib and Glycoprotein IIb/IIIa Complex in Thrombin-dependent and -independent Platelet Aggregations Induced by Tumor Cells

Department of Cardiovascular Research, Tokyo Metropolitan Institute of Medical Science [H. K., N. Y., K. T., H. Y.], and Tokyo Metropolitan Komagome Hospital [G. K.], 3-18-22 Honkomagome, Bunkyo-ku, 113, Tokyo, Japan

Involvement of platelet membrane glycoproteins (GP) in interactions between platelets and tumor cells was studied by using two human tumor cell lines and two monoclonal antibodies against platelet membrane GP. HMV-I cells derived from vaginal melanoma induced platelet aggregation in heparinized plasma, which was not followed by coagulation. M7609 cells derived from colon adenocarcinoma also induced platelet aggregation in heparinized plasma, which, on the contrary, was followed by coagulation. Aggregating activities of the HMV-I cells were abolished by pretreatment with neuraminidase or trypsin, but M7609 activity was not labile to these enzymes. Aggregations induced by M7609 were inhibited by hirudin or MD805, while those by HMV-I were not. M7609 cells dose dependently shortened the recalcification time of normal as well as Factor IX-deficient plasmas, while they were not effective in shortening the time of Factor II- or Factor VII-deficient plasmas. The procoagulant activity of HMV-I cells was 1000 times less than M7609 on the basis of cell numbers. When human platelets were preincubated with monoclonal anti-GPIb or anti-GPIIb/IIIa complex antibodies, neither cell line could cause aggregations.

These findings suggest that both GPIb and the GPIIb/IIIa complex on the platelet surface are involved in the thrombin-dependent and -independent platelet aggregations induced by tumor cells.

¹ To whom requests for reprints should be addressed.

Received 5/ 2/88. Revised 9/29/88. Accepted 10/11/88.

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