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Veränderungen der hochmolekularen Membranglykoproteine bei Thrombasthenie als Ursache der fehlenden Plättchenausbreitung?

Failure of platelet spreading in thrombasthenia due to changes of high molecular weight membrane glycopeptides

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Summary

Rabbit and thrombasthenic platelet membranes were examined by SDS polyacrylamide gel electrophoresis. Both rabbit and thrombasthenic platelets failed to spread on siliconized glass surfaces and revealed platelet membrane glycoprotein patterns quite different from those of normal human platelet membranes. Typical for normal platelet membranes are four high molecular weight glycoprotein bands. The platelet membranes from rabbits and from one thrombasthenic patient showed only the first major glycopolypeptide with an apparent molecular weight of 135 000 and 120 000 D respectively.

Other platelet membrane glycopeptides (both the carbohydrate and polypeptide moiety) were completely absent in thrombasthenia. The rabbit platelet membrane yet contains two strong polypeptides in this high molecular weight region, however, without corresponding carbohydrate moieties. Therefore, we support the view that the carbohydrate chains from two high molecular weight glycoproteins are of importance for platelet spreading on glass surfaces.

Zusammenfassung

Die Membranen von Kaninchenthrombocyten und thrombasthenischen Plättchen wurden in der Polyacrylamid-SDS-Gelelektrophorese analysiert. Beide Plättchenarten breiten sich nicht an silikonisierten Glasoberflächen aus und lassen ein Glykoproteinmuster der Membran erkennen, das deutlich von dem normaler Thrombocyten abweicht. Die normale Plättchenmembran zeigt vier hochmolekulare Glykoproteinbanden im Polyacrylamidgel. Die Membranen von Kaninchenthrombocyten und thrombasthenischen Plättchen weisen nur das erste große Glykoprotein mit einem Molekulargewicht von ca. 135 000 bzw. 120 000 D auf.

Die übrigen Membranglykopolypeptide (sowohl Kohlenhydrat- als auch Proteinanteil) fehlen bei Thrombasthenie vollständig. Die Thrombocytenmembran von Kaninchen enthält in diesem hochmolekularen Bereich zwei große Polypeptide, — vergleichbar den Humanthrombocyten, — jedoch ohne entsprechende Kohlenhydratketten. So kann angenommen werden, daß der Kohlenhydratanteil dieser Glykoproteine für die Plättchenausbreitung maßgeblich ist.

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Literatur

  1. Barber, A.J., Jamieson, G.A.: Isolation and characterisation of plasma membranes from human platelets. J. biol. Chem.245, 6357 (1970)

    PubMed  Google Scholar 

  2. Baumgartner, H.R., Muggli, R.: Effect of acetylsalicylic acid on platelets adhesion to subendothelium and on the formation of mural platelet thrombi. Thrombos. Diathes. haemorrh. (Stuttg.) Suppl.60, 345 (1974)

    Google Scholar 

  3. Caen, J.P., Vainer, H., Gautier, A.: Thrombasthenie. In: K.M. Brinkhous, J.S. Wright, J.P. Soulier, H. Roberts, S. Hinnon (Ed.) Platelets: Their role in hemostasis and thrombosis Schattauer: Stuttgart 1967

  4. Caen, J.P., Michel, H.: Platelet shape change and aggregation. Nature240, 148 (1972)

    PubMed  Google Scholar 

  5. Caen, J.P., Cronberg, S., Levy-Toledano, S., Kubisz, P., Pinkhas, J.: New data on Glanzmann's thrombasthenia. Proc. Soc. exp. Biol.136, 1082 (1971)

    Google Scholar 

  6. Fairbanks, G., Steck, T.L., Wallach, D.F.H.: Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochem.10, 2606 (1971)

    Google Scholar 

  7. Marton, L.S.G., Garvin, J.: Subunit structure of the major human erythrocyte glycoprotein: Depolymerization by heating ghosts with sodium dodecyl sulfate. Biochem. biophys. Res. Commun.52, 1457 (1973)

    PubMed  Google Scholar 

  8. Nachmann, R.L., Ferris, B.: Studies on the proteins of human platelet membranes. J. biol. Chem.247, 4469 (1972)

    Google Scholar 

  9. Nurden, A.T., Caen, J.P.: An abnormal platelet glycoprotein pattern in three cases of Glanzmann's thrombasthenia. Brit. J. Haemat.28, 253 (1974)

    PubMed  Google Scholar 

  10. Phillips, D.R., Agin, P.P.: Thrombin substrates and the proteolytic site of thrombin action on human-platelet plasma membranes. Biochim. biophys. Acta352, 218 (1974)

    PubMed  Google Scholar 

  11. Phillips, D.R.: Effect of trypsin on the exposed polypeptides and glycoproteins in the human platelet membrane. Biochem.11, 4582 (1972)

    Google Scholar 

  12. Podolsak, B.: Die spontane standardisierte Thrombocytenadhäsion und -aggregation in der Zählkammer. Acta haemat. (Basel)49, 96 (1973)

    PubMed  Google Scholar 

  13. Segrest, J.P., Kahane, I., Jackson, R.L., Marchesi, V.T.: Major glycoprotein of the human erythrocyte membrane. Evidence for an amphipatic molecular structure. Arch. Biochem.155, 167 (1973)

    PubMed  Google Scholar 

  14. Weber, K., Osborn, M.: The reliability of molecular weight determination by dodecyl sulfate-polyacrylamide gel electrophoresis. J. biol. Chem.244, 4406 (1969)

    PubMed  Google Scholar 

  15. Zacharius, R.M., Zell, T.E., Morrison, J.H., Woodlock, J.J.: Glycoprotein staining following electrophoresis on acrylamide gels. Analyt. Biochem.30, 148 (1969)

    PubMed  Google Scholar 

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Podolsak, B., Brunswig, D. Veränderungen der hochmolekularen Membranglykoproteine bei Thrombasthenie als Ursache der fehlenden Plättchenausbreitung?. Klin Wochenschr 54, 613–617 (1976). https://doi.org/10.1007/BF01469026

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