Abstract
THE haemostatic role of the blood platelet is largely dependent on its ability to adhere to exposed subendothelial components in the event of vessel damage1 and respond to specific aggregation-inducing stimuli, such as adenosine diphosphate (ADP), which seem to act at defined receptor sites on the platelet membrane2. The early stages of platelet adhesion and aggregation are surface-mediated phenomena and much interest has centred on determining which of the surface groupings are involved in these mechanisms. Iodination techniques3,4 have revealed that a limited number of proteins are exposed on the surface of the platelet and that among these are the major membrane glycoproteins. A possible involvement of carbohydrate groupings in the mechanisms of aggregation as induced by ADP and 5-hydroxytryptamine was described by Mester et al.5 who showed that the velocity of aggregation was altered by changes in the sialic acid content of the platelet.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Baumgartner, H. R., Thromb. Diath. Haemorrh. Supp., 11, 161–176 (1972).
Born, G. V. R., in Human Blood Coagulation, Haemostasis and Thrombosis (edit. by Biggs, R.), 159–175 (Blackwell, Oxford, 1972).
Phillips, D. R., Biochemistry, 11, 4582–4588 (1972).
Tanner, M. J. A., Boxer, D. H., Cumming, J., and Verrier-Jones, J., Biochem. J., 141, 909–911 (1974).
Mester, L., Szabados, L., Born, G. V. R., and Michal, F., Nature new Biol., 236, 213–214 (1972).
Nachman, R. L., and Ferris, B., J. biol. Chem. 247, 4468–4475 (1972).
Nurden, A. T., and Caen, J. P., Br. J. Haemat., 28, 253–260 (1974).
Lombart, C., Okumura, T., and Jamieson, G. A., FEBS Lett., 4l, 30–34 (1974).
Phillips, D. R., and Poh Agin, P., Biochim. biophys. Acta, 352, 218–227 (1974).
Hagen, I., biochim. biophys. Acta, 273, 141–148 (1972).
Weiss, H. J., et al., Am. J. Med., 57, 920–931 (1974).
Howard, M. A., Hutton, R. A., and Hardisty, R. M., Br. Med. J., 2, 586–588 (1973).
Grottum, K. A., and Solum, N. O., Br. J. Haemat., 16, 275–290 (1969).
Hardisty, R. M., in Human Blood Coagulation, Haemostasis and Thrombosis (edit. by Biggs, R.), 175–187 (Blackwell, Oxford, 1972).
Caen, J. P., and Michel, H., Nature, 240, 148–149 (1972).
Evans, W. H., Nature, 250, 391–394 (1974).
Behnke, O., J. Ultrastruct. Res., 24, 51–69 (1968).
Hoover, R. L., Expl Cell Res., 87, 265–276 (1974).
Weber, K., and Osborn, M., J. biol. Chem., 244, 4406–4412 (1969).
Zacharius, R. M., Zell, T. E., Morrison, J. H., and Woodlock, J. J., Analyt. Biochem., 30, 148–152 (1969).
Aminoff, D., Biochem. J., 81, 384–390 (1961).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
NURDEN, A., CAEN, J. Specific roles for platelet surface glycoproteins in platelet function. Nature 255, 720–722 (1975). https://doi.org/10.1038/255720a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/255720a0
- Springer Nature Limited
This article is cited by
-
Critical shifts in lipid metabolism promote megakaryocyte differentiation and proplatelet formation
Nature Cardiovascular Research (2023)
-
Lectin-based carbohydrate profile of megakaryocytes in murine fetal liver during development
Scientific Reports (2023)
-
A Cdc42/RhoA regulatory circuit downstream of glycoprotein Ib guides transendothelial platelet biogenesis
Nature Communications (2017)
-
Platelet-targeted gene therapy with human factor VIII establishes haemostasis in dogs with haemophilia A
Nature Communications (2013)
-
Inhibition of Platelet GPIbα and Promotion of Melanoma Metastasis
Journal of Investigative Dermatology (2010)