Inhibition of human platelet glycoprotein IIB/IIIA binding to fibrinogen by tumor cell membrane proteins

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 hum...

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Bibliographic Details
Published in:Cancer research (Chicago, Ill.) Ill.), 1993-01, Vol.53 (2), p.221-223
Main Authors: KAMIYAMA, M, CHEN, K, LYNCH, J, ARKEL, Y. S
Format: Article
Language:English
Subjects:
Binding, Competitive
Biological and medical sciences
Fibrinogen - metabolism
Host-tumor relations. Immunology. Biological markers
Humans
In Vitro Techniques
Medical sciences
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - metabolism
Molecular Weight
Neoplasm Proteins - chemistry
Neoplasm Proteins - metabolism
Platelet Aggregation
Platelet Membrane Glycoproteins - metabolism
Tumor Cells, Cultured
Tumors
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Summary: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.
ISSN:0008-5472
1538-7445