Platelet Reactions and Immune Processes

F Jobin; France Tremblay; M Morissette

doi:10.1055/s-0038-1654125

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 1970; 23(01): 110-119
DOI: 10.1055/s-0038-1654125

Originalarbeiten – Original Articles – Travaux Originaux

Schattauer GmbH

Platelet Reactions and Immune Processes

III. The Inhibition of Platelet Aggregation by Chymotrypsin Substrates and Inhibitors

Autor*innen

F Jobin

¹Departement de biochimie, Faculté de Médecine, Université Laval and the Service d’Hématologie, Hôpital du Saint-Sacrement, Québec
France Tremblay

¹Departement de biochimie, Faculté de Médecine, Université Laval and the Service d’Hématologie, Hôpital du Saint-Sacrement, Québec
M Morissette

¹Departement de biochimie, Faculté de Médecine, Université Laval and the Service d’Hématologie, Hôpital du Saint-Sacrement, Québec

Abstract

Summary

We have studied the effect of chymotrypsin substrates and inhibitors on the aggregation of human platelets by collagen, latex, and epinephrine :

1. We have found that platelet aggregation was inhibited by most chymotrypsin substrates and inhibitors which we studied.

2. In general, there was a positive correlation between the effectiveness of the compounds as chymotrypsin substrates or inhibitors on one hand, and as platelet aggregation inhibitors on the other hand. However aromatic amino acid derivatives acetylated on the α-amine group were much less effective with platelets than they are with chymotrypsin.

3. Chymotrypsin substrates and inhibitors also inhibit the anaphylactic release of histamine. The view is presented that the platelet release reaction and the mast cell release reaction have several common biological and biochemical features.

4. The possible role of platelet esterases in platelet thrombogenetic reactions is discussed in the light of the present knowledge of the role of cell bound esterase in several inflammatory or immune cellular processes.

Volltext

Referenzen

References
1 Jobin F, Tremblay F. Platelet reactions and immune processes. II. The inhibition of platelet aggregation by complement inhibitors. Thrombos. Diathes. haemorrh. (Stuttg.) 22: 466 1969;
2 Basch R. S. Inhibition of the third component of the complement system by derivatives of aromatic amino acids. J. Immunol 94: 629 1965;
3 Shin H. S, Mayer M. M. The third component of the guinea pig complement system. III. Effect of inhibitors. Biochemistry 7: 3003 1968;
4 Austen K. F, Brocklehurst W. E. Anaphylaxis in chopped guinea pig lung. I. Effect of peptidase substrates and inhibitors. J. exp. Med 113: 521 1961;
5 Keller R, Beeger I. Anaphylaxis in isolated rat mast cells. I. Effect of peptidase substrates and inhibitors. Int. Arch. Allergy 22: 31 1963;
6 Uvnas B. Metabolic and non-metabolic processes in the mechanism of histamine release from mast cells. In: Biochemistry of the acute allergy reactions. Ed. Austen K. F, and Becker E. L. 131 Blackwell Scientific Publications; Oxford: 1968
7 Thon I. L, Uvnas B. Degranulation and histamine release, two consecutive steps in the response of rat mast cells to compound 48/80. Acta physiol. scand 71: 303 1967;
8 Packham M. A, Warrior E. S, Glynn M. F, Senyi A. S, Mustard J. F. Alteration of the response of platelets to surface stimuli by pyrazole compounds. J. exp. Med 126: 111 1967;
9 Markwardt F. Studies on the release of biogenic amines from blood platelets. In: Biochemistry of blood platelets. Ed. Kowalski E, and Niewiarowski S. 105 Academic Press; London: 1967
10 Green N. M, Neurath H. Proteolytic enzymes. In: The proteins. Ed. Neurath H, and Bailey K. 2B 1057 Academic Press Inc.; New York: 1954
11 Goldenberg H, Goldenberg V, McLaren A. D. An inquiry into the enzyme-catalyzed hydrolysis of leucine ethyl ester by chymotrypsin. Biochim. biophys. Acta (Amst.) 7: 110 1951;
12 Neurath H, Gladner J. A. Structural requirements of specific inhibitors for a-chymotrypsin. II. Effects of chain length and cyclic substituents. J. biol. Chem 188: 407 1951;
13 Wallace R. A, Kurtz A. N, Niemann C. Interaction of aromatic compounds with a-chymotrypsin. Biochemistry 2: 824 1963;
14 Johnson C. H, Knowles J. R. The binding of inhibitors to a-chymotrypsin. Biochem. J 101: 56 1966;
15 Blow D. M, Birktoft J. J, Hartley B. S. Role of a buried acid group in the mechanism of action of chymotrypsin. Nature (Lond.) 221: 337 1969;
16 Jerushalmy Z, Skoza L, Zucker M. B. Inhibition of ADP-induced platelet clumping. Fed. Proc 24: 402 1965;
17 Salzman E. W, Chambers D. A. Inhibition of ADP-induced platelet aggregation by substituted amino acids. Blood 25: 602 1965;
18 Morissette M, Jobin F. Inhibition of human platelet aggregation and ADP release by imidazole. (Manuscript in preparation.)
19 O’Brien J. R. A comparison of platelet aggregation produced by seven compounds and a comparison of their inhibitors. J. clin. Path 17: 275 1964;
20 Austen K. F, Brocklehurst W. E. Anaphylaxis in chopped guinea pig lung. III. Effect of carbon monoxide, cyanide, salicylaldoxime and ionic strength. J. exp. Med 114: 29 1961;
21 White J. G. Effects of colchicine and vinca alkaloids on human platelets. 3. Influence on primary internal contraction and secondary aggregation. Amer. J. Path 54: 467 1969;
22 Levy D. A, Carlton J. Inhibition by colchicine of allergic histamine release in vitro . Fed. Proc 27: 315 1968;
23 Lichtenstein L. M, Levy D. A. Studies of reversed anaphylactic reactions in vitro with human leucocytes. Fed. Proc 28: 378 1969;
24 Gillespie E, Levine R. J, Malawista S. E. Histamine release from rat peritoneal mast cells: inhibition by colchicine and potentiation by deuterium oxide. J. Pharmacol, exp. Ther 164: 158 1968;
25 Bounameaux Y, van Cauwenberge H. Action de la cortisone, de l’A.C.T.H. et du salicylate de soude sur les thrombocytes et la coagulation sanguine. Sang 25: 889 1954;
26 O’Brien J. R. Effects of salicylates on human platelets. Lancet I: 779 1968;
27 Evans G, Packham M. A, Nishizaka E. E, Mustard J. F, Murphy E. A. Effect of acetyl-salicylic acid on platelet function. J. exp. Med 128: 877 1968;
28 Mongar J. L, Schild P. L. O. Inhibition of the anaphylactic reaction. J. Physiol. (Lond.) 135: 301 1957;
29 Packham M. A, Warrior E. S, Glynn M. F, Senyi A. S, Mustard J. F. Alterations of the response of platelets to surface stimuli by pyrazole compounds. J. exp. Med 126: 171 1967;
30 Morissette M, Jobin F. Unpublished data.
31 May C. D, Levine B. B, Weissmann G. Chemical factors inhibiting antigenic release of histamine and phagocytic release of β-glucuronidase from leucocytes. Fed. Proc 28: 378 1969;
32 Robinson C. W, Kress S. C, Wagner R. H, Brinkhous K. M. Platelet agglutination and deagglutination with a sulfhydryl inhibitor, methyl mercuric nitrate : relationships to platelet ATPase. Exp. molec. Path 4: 457 1965;
33 Harrison M. J. G, Emmons P. R, Mitchell J. R. A. The effect of sulphydryl and enzyme inhibitors on platelet aggregation in vitro. Thrombos. Diathes. haemorrh. (Stuttg.) 16: 122 1966;
34 Mota I. Effect of antigen and octylamine on mast cells and histamine content of sensitized guinea pig tissues. J. Physiol. (Lond.) 147: 425 1959;
35 Diamant B, Kruger P. G. Histamine release from isolated rat peritoneal mast cells induced by adenosine-5’-triphosphate. Actaphysiol. scand 71: 291 1967;
36 Diamant B. The mechanisms of histamine release from rat mast cells induced by adenosine-triphosphate. Acta pharmacol 25 (Suppl. 04) 33 1967;
37 Chambers D. A, Salzman E. W, Neri L. L. Platelet nucleotide metabolism and platelet aggregation. Exp. biol. Med 3: 62 1968;
38 Diamant B, Kruger P. G. Structural changes of isolated rat peritoneal mast cells induced by adenosinetriphosphate and adenosine diphosphate. J. Histochem. Cytochem 16: 707 1968;
39 Bull B. S, Zucker M. B. Changes in platelet volume produced by temperature, metabolic inhibitors and aggregating agents. Proc. Soc. exp. Biol. (N. Y.) 120: 296 1965;
40 Becker E. L, Austen K. F. A comparison of the specificity of inhibition by phosphonate esters of the first component of complement and the antigen-induced release of histamine from guinea pig lung. J. exp. Med 120: 491 1964;
41 Becker E. L, Austen K. F. Mechanisms of immunologic injury of rat peritoneal mast cells. I. The effect of phosphonate inhibitors on the homocytotropic antibody-mediated histamine release and the first component of rat complement. J. exp. Med 124: 379 1966;
42 Becker E. L, Ward P. A. Partial biochemical characterization of the activated esterase required in the complement-dependent Chemotaxis of rabbit polymorphonuclear leukocytes. J. exp. Med 125: 1021 1967;
43 Ward P. A, Becker E. L. The deactivation of rabbit neutrophils by chemotactic factor and the nature of the activatable esterase. J. exp. Med 127: 693 1968;
44 Becker E. L, Ward P. A. Esterases of polymorphonuclear leukocyte capable of hydrolyzing acetyl-DL-phenylalanine-beta-naphthyl ester. Relationship to activatable esterase of Chemotaxis. J. exp. Med 129: 569 1969;
45 Ward P. A. Chemotaxis of mononuclear cells. J. exp. Med 128: 1201 1968;
46 Becker E. L. Nature and significance of antigen-Lantibody activated esterases. In: Biochemistry of the acute allergic reactions. Ed. Austen K. F, and Becker E. L. 199 Blackwell scientific publications; Oxford: 1968
47 Mustard J. F, Packham M. A, Senyi A. Effect of DFP on platelet function in vitro and in vivo. J. Lab. clin. Med 70: 1003 1967;
48 Kilburn E. P, Firkin B. G. A study of human platelet esterases. Thrombos. Diathes. hae-morrh. (Stuttg.) 20: 366 1968;
49 Vincent D, Maupin B, Marques-Vincent M. C. Sur les esterases des plaquettes du sang humain. C. R. Soc. Biol 156: 34 1962;