Cancer Research Cancer Epigenetics  EMT and Cancer Progression and Treatment
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online

[Cancer Research 42, 4348-4352, November 1, 1982]
© 1982 American Association for Cancer Research

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bastida, E.
Right arrow Articles by Jamieson, G. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bastida, E.
Right arrow Articles by Jamieson, G. A.

Differentiation of Platelet-aggregating Effects of Human Tumor Cell Lines Based on Inhibition Studies with Apyrase, Hirudin, and Phospholipase1

Eva Bastida2, Antonio Ordinas2, Steven L Giardina and G. A. Jamieson3

American Red Cross Blood Services Laboratories, Bethesda, Maryland 20814

Three different mechanisms have been detected for the aggregation of platelets by tumor cells in a homologous human system based on inhibition studies with apyrase, hirudin, and phospholipase D. In the major group, platelet aggregation induced by the SKBR3 (adenocarcinoma), SKNMC (neuroblastoma), HT29 (adenocarcinoma), and HT144 (melanoma) cell lines was inhibited by apyrase and phospholipase D but not by hirudin, suggesting that adenosine 5'-diphosphate is involved in the first step. However, since the reaction occurs only in heparinized plasma, the mechanism must differ from that of platelet aggregation which can be induced in citrated plateletrich plasma by endogenous or exogenous adenosine 5'-diphosphate. In contrast, the Hut28 (mesothelioma) line was inhibited by hirudin and phospholipase D but not by apyrase, suggesting that the mechanism in this system involves the activation of the clotting system in the early stages. However, the coagulant-dependent mechanism observed with Hut28 can be differentiated from the similar mechanism we have observed previously with the U87MG (glioblastoma) cell line since the latter is unaffected by phospholipase D (Am J. Hematol., 11: 367–378, 1981). Phospholipase C had no effect on platelet aggregation induced by any of the human cell lines examined while both phospholipase A2 and lysolecithin inhibited aggregation in every case. These results suggest that two categories of human tumor cells can be defined based on whether they initiate platelet aggregation by adenosine 5'-diphosphate or coagulant-dependent mechanisms. However, within this latter category, subclassification is possible based on the inhibitory effects of phospholipase D.

1 This work was supported, in part, by USPHS Grants HL 20971, HL 14697, ROICA, 30538 and Biomedical Research Support Grant RR0575. Contribution 515 from the American Red Cross.

2 Permanent address: Hospital Clinico y Provincial, Servicio Hemoterapia y Hemostasia, Universidad de Barcelona, Barcelona, Spain.

3 To whom requests for reprints should be addressed.

Received 4/22/81. Accepted 8/ 4/82.




This article has been cited by other articles:


Home page
Cancer Res.Home page
P. Jurasz, G. Sawicki, M. Duszyk, J. Sawicka, C. Miranda, I. Mayers, and M. W. Radomski
Matrix Metalloproteinase 2 in Tumor Cell-induced Platelet Aggregation: Regulation by Nitric Oxide
Cancer Res., January 1, 2001; 61(1): 376 - 382.
[Abstract] [Full Text]


Home page
JCBHome page
C. Claas, S. Seiter, A. Claas, L. Savelyeva, M. Schwab, and M. Zoller
Association Between the Rat Homologue of CO-029, a Metastasis-associated Tetraspanin Molecule and Consumption Coagulopathy
J. Cell Biol., April 6, 1998; 141(1): 267 - 280.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cancer Prevention Research
Cancer Prevention Journals Portal Cancer Reviews Online
Annual Meeting Education Book Meeting Abstracts Online
Copyright © 1982 by the American Association for Cancer Research.