ADPase Activity of Normal and Atherosclerotic Human Aorta intima

A. du P Heyns; C. J Badenhorst; F. P Retief

doi:10.1055/s-0038-1649251

Thrombosis and Haemostasis, Table of Contents

Thromb Haemost 1977; 37(03): 429-435
DOI: 10.1055/s-0038-1649251

Original Article

Schattauer GmbH

ADPase Activity of Normal and Atherosclerotic Human Aorta intima

A. du P Heyns

¹Department of Haematology and Internal Medicine, Faculty of Medicine, University of the Orange Free State, Bloemfontein, South Africa

,

C. J Badenhorst

¹Department of Haematology and Internal Medicine, Faculty of Medicine, University of the Orange Free State, Bloemfontein, South Africa

,

F. P Retief

¹Department of Haematology and Internal Medicine, Faculty of Medicine, University of the Orange Free State, Bloemfontein, South Africa

› Author Affiliations

Abstract

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Summary

ADP plays a key role in platelet aggregation and the enzymatic removal of this nucleotide may be important in the pathogenesis of intravascular thrombosis and atherosclerosis. Aortic intima extracts have ADPase activity and is able to remove small quantities of ADP efficiently. ADPase activity was assayed by measuring the catabolism of 2 μM ¹⁴C-ADP (final concentration) by the tissue extracts. Extracts prepared from normal, moderately and severely atherosclerotic human aorta intimas showed a significant progressive decrease in ADPase activity with increasing atherosclerosis. ADPase activity of the arch, thoracic and abdominal regions of normal aortas did not vary significantly, and thus did not correlate with the anatomical distribution of atherosclerosis. Vascular ADPase activity seems relevant in thrombogenesis since it may be a link between blood platelets and blood vessel wall interaction.

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References

References
1 Bounameaux Y. L’accolement des plaquettes aux fibres sousendotheliales. Comptes Rendus des Seances de la Societe de Biologie et de ses Filiales (Paris) 1959; 153: 865
2 Clark E, Graef I, Chasis H. Thrombosis of the aorta and coronary arteries with special reference to the “fibrinoid” lesions. Archives of Pathology 1936; 22: 183
3 Dahme E. G. Atherosclerosis and arteriosclerosis in domestic animals. Annals of the New York Academy of Sciences 1965; 127: 657
4 Duguid J. B. Thrombosis as a factor in the pathogenesis of coronary atherosclerosis. Journal of Pathology and Bacteriology 1946; 58: 207
5 Duguid J. B. Thrombosis as a factor in the pathogenesis of aortic atherosclerosis. Journal of Pathology and Bacteriology 1958; 60: 57
6 Gore I. Blood and Lymphatic Vessels. In: Pathology, (Ed.) Anderson W. A. D, Mosby Co C. V. St. Louis: 1966: 572
7 Haslam R. J, Mills D. C. B. The adenylate kinase of human plasma, erythrocytes and platelets in relation to the degradation of adenosine diphosphate in plasma. Biochemical Journal 1967; 103: 773
8 Heyns A, du P. ‘n Ondersoek na bloedplaatjiefunksie met spesiale verwysing na die invloed van weefselekstrakte. . Thesis D. M. University of the Orange Free State, Bloemfontein.; South Africa.: 1973
9 Heyns A, du P, Potgieter G. M, Retief F. P. An inhibitor of platelet aggregation in bloodvessel intima. XIV International Congress of Haematology; abstract 1972: 224
10 Heyns A, du P, van den Berg D. J, Potgieter G. M, Retief F. P. The inhibition of platelet aggregation by an aorta intima extract. Thrombosis et Diathesis Haemorrhagica 1974; 32: 417
11 Holmsen H. Adenine nucleotide metabolism in platelets and plasma. In Kowalski E, Niewiarowski S. (Ed.). Biochemistry of Blood Platelets. Academic Press; New York-London: 1967: 81
12 Holmsen H, Day H. J. Adenine nucleotides and platelet function. Series Haematologica 1971; 1: 28
13 Holmsen H, Stormorken H. Kinetic studies on be breakdown of adenosine diphosphate in human plasma. Scandinavian Journal of Clinical and Laboratory Investigation 1965; 17. Suppl. 84 183
14 Holmsen I, Holmsen H. Partial purification and characterization of an ADP phosphohy-drolase from human plasma. Thrombosis et Diathesis Haemorrhagica 1971; 26: 171
15 Hugues J. Accolement des plaquettes aux collagene. Comptes Rendus des Seances de la Societe de Biologie et de ses Filiales. (Paris) 1960; 154: 866
16 Ireland M. D, Mills D. C. B. Degradation of adenosine diphosphate and related substances in plasma. Biochemical Journal 1964; 99: 283
17 Johnson S. A, Van Horn D. L, Pederson H. J, Marr J. The function of platelets: a review. Transfusion (Philadelphia) 1966; 6: 3
18 Kirk J. E. Enzymes of the Arterial Wall. Academic Press; New York.: 1969
19 Mustard J. F. Hemostasis and Thrombosis. Seminars in Haematology 1968; 5: 91
20 Mustard J. F, Movat H. Z, MacMorine D. R. L, Senyi A. Release of permeability factors from the blood platelet. Proceedings of the Society for Experimental Biology and Medicine 1965; 119: 988
21 Odegaard A. E, Skalhegg B. A, Hellem A. J. Increased activity of “anti Willebrand factor” in diabetic plasma. Thrombosis et Diathesis Haemorrhagica 1964; 11: 27
22 Spaet T. H, Gaynor E. Vascular endothelial damage and thrombosis. Advances in Cardiology 1970; 4: 47
23 Tschopp Th. B, Baumgartner H. R. Enzymatic Removal of ADP from Plasma: Unaltered platelet adhesion but reduced aggregation on subendothelium and collagen fibrils. Thrombosis and Haemostasis 1976; 35: 334
24 Wojcik J. D, Van Horn D. L, Webber A. J, Johnson S. A. Mechanism whereby platelets support the endothelium. Transfusion (Philadelphia) 1969; 9: 324