Thromb Haemost 1961; 6(01): 086-097
DOI: 10.1055/s-0038-1654542
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Macroscopie Studies of Platelet Aggregation. Nature of an Aggregating Factor in Red Blood Cells and Platelets

E Øllgaard
1   Laboratory of the Health Board, Aarhus, Denmark
› Author Affiliations
Further Information

Publication History

Publication Date:
12 July 2018 (online)

Summary

In in-vitro experiments, it has been shown that red blood cells and platelets contain a factor which, on addition to a sample of platelet-containing plasma and subsequent rocking of the test tube, causes an aggregation of the platelets which is visible to the naked eye. In equal volumes, the concentration of this factor has been found to be about 5 times as high in platelets as in red cells. The factor is thermostabile, non-protein in nature, and exerts its action independently of the process of coagulation. It is assumed to be carbohydrate in nature. White cells and, to a less degree, plasma and serum seem to be able to destroy the aggregating factor by an enzymatic process.

The aggregation is reversible, since white cells as well as certain enzyme poisons and Na+ can reverse the process without any apparent change in the appearance of the platelets. The process observed thus actually seems to be a form of aggregation.

 
  • References

  • (1) Wright J. H, Minot G. R. The viscous metamorphosis of the blood platelets. J. exp. Med. 26: 395 1917;
  • (2) Ackroyd J. F. Cause of thrombocytopenia in sedormid purpura. Clin. Sei. 8: 269 1949;
  • (3) Grandjean L. C. Case of purpura hemorrhagica after administration of quinine with specific thrombocytolysis demonstrated in vitro. Acta med. scand. (Suppl. 213) 131: 165 1948;
  • (4) Evans R. S, Takashi K, Duane R. T, Payne R, Liu Chi-kong. Primary thrombocytopenic purpura and acquired hemolytic anemia. Arch. intern. Med. 87: 48 1951;
  • (5) Stefanini M, Plitman G, Dameshek W, Chatterjea J, Mednicoff I. B. Studies on platelets XL Antigenicity of platelets and evidence of platelet groups and types in man. J. Lab. clin. Med. 42: 723 1953;
  • (6) Brinkhous K. M, leRoy E. C, Cornell W. T, Brown R. C, Hazle-hurst J. L, Vennart G. P. Macroscopic studies of platelet agglutination. Nature of thrombocyte agglutinating activity of plasma. Proc. Soc. exp. Biol. (N. Y.) 98: 379 1958;
  • (7) Øllgaard E. Clot retraction as a quantitative test of the function and agglutinability of the blood platelets. Acta haemat. (Basel) 6: 220 1951;
  • (8) Koppel J. L, Olwin J. H. Dehydrogenase activities of human platelets. Proc. Soc. exp. Biol. (N. Y.) 86: 641 1954;
  • (9) Campbell E. W, Small W. J, Dameshek W. Metabolic activity of human blood platelets. J. Lab. clin. Med. 47: 835 1956;
  • (10) Dillard G. H. L, Brecher G, Cronkite E. P. Separation, concentration and transfusion of platelets. Proc. Soc. exp. Biol. (N. Y.) 78: 796 1951;
  • (11) Jürgens R, Braunsteiner H. Zur Pathogenese der Thrombose. Schweiz. med. Wschr. 52: 1388 1950;
  • (12) Roskam J, Hugues J. C. R. Congr. Soc. europ. Hernat. Rome: 1951: 696.
  • (13) Lundevall J. Serological studies of human blood platelets. Scand. J. clin. Lab. Invest. 10 Suppl. 34 1958;
  • (14) Øllgard E. On the agglutination of the blood platelets under normal and pathological conditions. Acta med. scand. 140: 1 1943;
  • (15) Crane R. K. Use of charcoal to separate mixtures of inorganic, ester and nucleotide phosphates. Science 127: 285 1958;
  • (16) Hirst G. K. Nature of virus receptors of red cells, evidence on chemical nature of virus receptors of red cells of existence of closely analogous substance in normal serum. J. exp. Med. 87: 301 1948;
  • (17) Koppel J. L, Novak L. V, Olwin J. H. Relation between platelets integrity and sulfhydryl groups. Proc. Soc. exp. Biol. (N. Y.) 100: 227 1959;
  • (18) Lüscher E. F. Glukose als Cofaktor bei der Retraktion des Blutgerinnsels. Experientia (Basel) 12: 294 1956;