Localization of Tissue Thromboplastin in the Human Brain

Summary

Monospecific antisera against the purified protein component of tissue thromboplastin (apoprotein-III) from human brain have been raised in goats and rabbits. The antisera neutralized tissue thromboplastin prepared from brain, thyroid gland and pulmonary tissue, indicating that apoproteins in the various preparations cross-reacted immunologically and therefore were similar or identical.

Comparison of the activities of tissue thromboplastin preparations from 34 different areas of the brain demonstrated a characteristic distribution pattern and a wide range of activities. White and grey matter from the same areas had similar activities. Bulbus and tractus olfac-torius, medulla oblongata, corpus pineale, hippocampus and hypothalamus contained 160–270 % of the average activity, whereas cerebellum, globus pallidus, nucleus ruber and substantia nigra contained 30–60 %. The distinct distribution pattern was unrelated to tissue vascularization, and may suggest that apoprotein-III could serve other functions, apart from the coagulation of blood. The predominance in phylogenetically older brain regions would suggest that it represents a primitive or fundamental feature.

^* Present address: Department of Toxicology, Norwegian Defence Research Establishment, 2007 Kjeller, Norway.

• References

• 1 Astrup T. Assay and content of tissue thromboplastin in different organs. Thrombosis et Diathesis Haemorrhagica 1965; 24: 401
• 2 Astrup T, Albrechtsen O.K, Claassen M, Rasmussen J. Thromboplastic and fibrinolytic activity of the human aorta. Circulation Research 1959; 7: 969
• 3 Astrup T, Buluk K. Thromboplastic and fibrinolytic activities in vessels of animals. Circulation Research 1963; 13: 253
• 4 Aster R.H, Jandl J.M. Platelet sequestration in man. I. Methods. Journal of clinical Investigation 1964; 43: 843
• 5 Bjørklid E, Storm E, Prydz H. The protein component of human brain thromboplastin. Biochemical and Biophysical Research Communications 1973; 55: 969
• 6 Brodal A. Neurological Anatomy in Relation to Clinical Medicine . 2nd edition. 1969. Oxford University Press; New York: 807 pp
• 7 Clarke H.G.M. In: Williams C. A, Chase M.W. (eds.) Methods in Immunology and lm-munochemistry, vol. III. 1971. Academic Press; New York: p. 287
• 8 Davis B.J. Disc electrophoresis II. Method and application to human serum protein. Annals of the New York Academy of Sciences 1964; 121: 404
• 9 Fahey J.L. In: Williams C. A, Chase M. W. (eds.) Methods in Immunology and Im-munochemistry, vol. I. 1967. Academic Press; New York: p. 321
• 10 Fahn S. Regional distribution studies of GABA and other putative neurotransmitters and their enzymes. In: Roberts E, Chase T.N, Tower D. B. GABA in Nervous System Function 1976. Raven Press; New York: p. 169
• 11 Friede R.L. Topographic Brain Chemistry . 1966. Academic Press; New York: p. 543
• 12 Gonmori H, Takeda Y. Properties of canine tissue thromboplastins from brain, lung, arteries and veins. American Journal of Physiology 1975; 229: 618
• 13 Hjort P.F. Intermediate reactions in the coagulation of blood with tissue thromboplastin. Scandinavian Journal of clinical and laboratoy Investigation 1957; 9 suppl. 27
• 14 Hvatum M, Prydz H. Studies on tissue thromboplastin. Its splitting into two separable parts. Thrombosis et Diathesis Haemorrhagica 1969; 21: 217
• 15 Laurell C.B. Antigen-antibody crossed electrophoresis. Analytical Biochemistry 1965; 10: 358