THROMBOSIS RESEARCH Printed in the United
States
Vol. 8, pp. 725-730,1976 Pergamon
Press,
Inc.
LETTER TO THE EDITORS-IN-CHIEF THE ROLE OF LEUKOCYTESAND PLATELETS IN THE PRECIPITATION OF FIBRIN IN VIVO: MECHANISMSOF THE GENERATIONOF MICROCLOTS FROM SOLUBLE FIBRIN
Gert Miiller-Berghaus,
Thomas Eckhardt and Wilfried
Kramer
Department of Medicine, Justus Liebig-Universitgt, Klinikstr. 36, 63 Giessen, Germany
(Received 2.2.1976; in revised form 1.4.1976. Accepted by Editor A.L. Copley)
Polymorphonuclear leukocytes as well as platelets contain cationic proteins which exhibit different activities influencing blood coagulation. In recent years, the antiheparin activity and the fibrin precipitating-polymerizing activity of these cationic protein preparations have extensively been studied because of their potential significance in generalized intravascular coagulation. Platelets contain a basic glycoprotein, known as heparin-neutralizing factor or platelet factor 4 which is released during platelet aggregation (I-4). It can be detected in the plasma in the course of generalized intravascular coagulation and the generalized Shwartzman reaction (4, 5). Data have been published indicating the precipitation of soluble fibrin monomer complexes by platelet factor 4 -in vitro (2, 5). Lipinski et al. (6) postulated that soluble fibrin may interact with certain basic proteins as to form fibrin-like material by a non-enzymatic mechanism. This suggestion was supported by electron microscope studies showing fibrin precipitation and polymerization by basic proteins (‘7, 8). The investigations published by Copley (9, 10) also favor the concept that precipitation of proteins represents the primary process of thrombosis. In contrast to Lipinski et al. (61, Copley (9, 10) proposed the concept that the precipitation and polymerization of preferably fibrinogen represents the primary process of thrombosis. Based on their findings Lipinski et al. (5, 1 I) presented the theory that soluble fibrin is -in vivo precipitated by platelet factor 4 released after endotoxin injection. R.ecent studies by Kgser-Glanzmann et al. (12), however, have demonstrated that the originally observed effect in precipitating soluble fibrin is caused by zinc impurities in the platelet factor 4 preparation. In spite of that, further basic proteins capable of inducing the paracoagulation phenomenon are located in platelets (13, 14) and may be released after endotoxin reaction.
72
States
Vol. 8, pp. 725-730,1976 Pergamon
Press,
Inc.
LETTER TO THE EDITORS-IN-CHIEF THE ROLE OF LEUKOCYTESAND PLATELETS IN THE PRECIPITATION OF FIBRIN IN VIVO: MECHANISMSOF THE GENERATIONOF MICROCLOTS FROM SOLUBLE FIBRIN
Gert Miiller-Berghaus,
Thomas Eckhardt and Wilfried
Kramer
Department of Medicine, Justus Liebig-Universitgt, Klinikstr. 36, 63 Giessen, Germany
(Received 2.2.1976; in revised form 1.4.1976. Accepted by Editor A.L. Copley)
Polymorphonuclear leukocytes as well as platelets contain cationic proteins which exhibit different activities influencing blood coagulation. In recent years, the antiheparin activity and the fibrin precipitating-polymerizing activity of these cationic protein preparations have extensively been studied because of their potential significance in generalized intravascular coagulation. Platelets contain a basic glycoprotein, known as heparin-neutralizing factor or platelet factor 4 which is released during platelet aggregation (I-4). It can be detected in the plasma in the course of generalized intravascular coagulation and the generalized Shwartzman reaction (4, 5). Data have been published indicating the precipitation of soluble fibrin monomer complexes by platelet factor 4 -in vitro (2, 5). Lipinski et al. (6) postulated that soluble fibrin may interact with certain basic proteins as to form fibrin-like material by a non-enzymatic mechanism. This suggestion was supported by electron microscope studies showing fibrin precipitation and polymerization by basic proteins (‘7, 8). The investigations published by Copley (9, 10) also favor the concept that precipitation of proteins represents the primary process of thrombosis. In contrast to Lipinski et al. (61, Copley (9, 10) proposed the concept that the precipitation and polymerization of preferably fibrinogen represents the primary process of thrombosis. Based on their findings Lipinski et al. (5, 1 I) presented the theory that soluble fibrin is -in vivo precipitated by platelet factor 4 released after endotoxin injection. R.ecent studies by Kgser-Glanzmann et al. (12), however, have demonstrated that the originally observed effect in precipitating soluble fibrin is caused by zinc impurities in the platelet factor 4 preparation. In spite of that, further basic proteins capable of inducing the paracoagulation phenomenon are located in platelets (13, 14) and may be released after endotoxin reaction.
72
