Abstract
Tryptophan load test followed by serum kynurenine determination at fasting state and after L-tryptophan loading, as well as serum pyridoxal-5-phosphate (P-5-P), homocysteine and neopterin concentrations at fasting state have been examined in 30 healthy individuals and 87 patients with coronary heart disease (CHD), verified by coronary angiography. Received results have shown that low serum P-5-P concentration as well as P-5-P deficiency identified by tryptophan load test have been found in 78% of CHD patients, while increased homocysteine concentration above 15 µmol/L in 31.8%, and elevated neopterin concentration above 8.7 nmol/L in 32.1% of cases. It allows to conclude that a lot of CHD patients have P-5-P deficiency. Moreover P-5-P deficiency is an earlier indicator of CHD than increased homocysteine level above 15.tmol/L. Elevated serum neopterin concentration above 8.7 nmol/L may be a marker of coronary disease activity rather than a marker of the presence of CHD.
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References
V. Rudzite, G. Sileniece, and J. Jirgensons, Tryptophan ¡ª nicotinic acid pathway in cardiovascular diseases, in: Progress in Tryptophan and Serotonin Research, edited by H.G. Slossberger, W. Kochen, B. Linzen, and H. Steinhart (Walter de Gruyter, Berlin, New York, 1984), pp. 365-38I.
V. Rudzite, G. Sileniece, J. Jirgensons, J. Skards, R. Zime, and A. Dalmane, Bradyarrhytmias and myocardial cell failure induced by kynurenine, in: Progress in Tryptophan and Serotonin Research 1986, edited by D.A. Bender, M.H. Joseph, W. Kochen and H. Steinhart (Walter de Gruyter, Berlin, New York, 1987), pp.131-136.
V. Rudzite, G. Sileniece, E. Jurika, A. Martinsons, A. Dalmane, V. Groma, and L. Vitolina, Kynurenine and the development of heart and renal pathology, in: Advances in Tryptophan Research 1992, edited by I. Ishiguro, R. Kido, T. Nagatsu, Y. Nagamura and Y.Ohta (Fujita Health University Press, Toyoake. 1992), pp. 379-382.
V. Rudzite, E. lurika, J. Arajs, and N. Andrejev, The relationship between kynurenine and arterial blood pressure, in: Progress in Tryptophan and Serotonin Research 1986, edited by D.A. Bender, M.H. Joseph, W. Kochen and H. Steinhart (Walter de Gruyter, Berlin, New York, 1987), pp. I27-130.
E.V. Gorjatchenkova, Viamin B6 (pyridoxine), in: Vitamins,edited by M.J. Smimov (Medicine, Moscow, 1974), pp. 236-263.
R.R. Brown, Tryptophan metabolism in humans: perspectives and prediction, in: Biochemical and Medical Aspects of Tryptophan Metabolism, edited by O. Hayaishi, Y. Ishimura, and R. Kido (North-Holland Biomedical Press, Amsterdam, 1980), pp. 207-235.
D. Bender, Biochemistry of tryptophan in health and disease, Molecular Aspects of Med. 6, 100-197 (1993).
P.M. Ueland, Plasma homocysteine and cardiovascular disease, in: Atherosclerotic Cardiovascular Disease and Endothelial Function edited by R. Francis (Marcel Dekker, New York, 1990), pp. 183-236.
J.C. Tsai, M.A. Perella, M. Yoshizumi, C.M. Hsieh, E. Haber, R. Schlegel, and M.E. Lee, Promotion of vascular smooth muscle cell growth by homocysteine: a link to atherosclerosis, Proc. Nat. Acad. Sci. 91, 6369-6373 (1994).
F. Tatzber, H. Rabl, K. Koriska, U. Erhart, H. Puhl, G. Waeg, A. Krebs, and H. Esterbauer, Elevated serum neopterin levels in atherosclerosis, Atherosclerosis 89, 203-208 (1991).
G. Weiss, E. Willert, S. Kiechl, D. Fuchs, E. Jarosch, F. Oberhollenzer, G. Reibnegger, G.P. Tilz, O.F. Gerstenbrand, and H. Wachter, Increased concentration of neopterin in carotid atherosclerosis, Atherosclerosis, 106, 263-271 (1994).
V. Rudzite, J. Jirgensons, E. Jurika, G. Sileniece, R. Zime, and S. Jirgensone, Besonderheiten der Nikotinsäurebildung bei koronarer Herzkrankheit unter Ber¨¹cksichtung von Herzrhythmusstörungen, Z. gesamte inn. Med. 43, 60-65 (1988).
V. Rudzite, G. Sileniece, J. Jirgensons, A. Dalmane, R. Zime, E. Jurika, and J. Skards, The significance of increased kynurenine level in blood to the development of cardiovascular pathology, Acta Medica Baltica 1, 4-19 (1994).
V. Rudzite, E. Jurika, and J. Jirgensons, Changes in membrane fluidity induced by tryptophan and its metabolites, Advances Exp. Med. Biol. 467, 353-367 (1999).
V. Rudzite, E. Jurika, M. Jäger, D. Fuchs, Impairment of lipid metabolism due to deficiency of pyridoxal-5phosphate and/or activated immune system: its interpretation, Pteridines 11,107-120 (2000).
J.R. Spies, and D.C. Chambers, Chemical determination of tryptophan. Study of color formation of tryptophan, p-dimethylaminobenzaldehyde and sodium nitrite in sulphuric acid solution, Analytical Chem. 20, 30-39 (1948).
M.H. Joseph, and D. Risby, The determination of kynurenine in plasma, Clin. Chim. Acta 63, 197-204 (1975).
W.J. Serfontein, J.B. Ubbink, L.S. DeViller, C.H. Rapley, and P.J. Becker, Plasma pyridoxal-5-phosphate level as a risk index for coronary artery disease, Atherosclerosis 55, 357-361 (1985).
T.M. Schipchandler, and E.G. Moore, Rapid, fully automated measurement of plasma homocysteine with the Abbot IMx analyser, Clin.Chem. 41, 991-994 (1995).
H. Rokos and K. Rokos, A radioimmunoassay for the determination of D-erythroneopterin, in: Chemistry and Biology of Pteridines, edited by J.A. Blair (Walter de Gruyter, Berlin, New York,1983), pp.815-8I9.
E. Weber, Grundriss der biologischen Statistik f¨¹r Naturwissenschaftler, Landvirte und Mediziner, (Gustav Fischer Verlag, Jena, 1957).
B.F. Steele, M.S. Reynolds, and C.A. Baumann, Amino acids in blood and urine of human subjects ingesting different amounts of the sanie proteins, J. Nutrition 40, 145-158 (1950).
E.G. Eccleston, A method for the estimation of free and total acid-soluble plasma tryptophan using an ultrafiltration technique, Clin. Chico. Acta 48, 269-272 (1976).
R.C. Keniston, T. Reyna, W. Becker, M.R. Weir, J.I. Enriquetz Sr, and F. Duncan, Prognostic value of undeproteinizing plasma pyridoxal 5’-phosphate concentrations, in: Clinical and Physiological Applications of vitamin B 6 , edited by J.E. Leklem and R.D. Reynolds (Alan R. Liss Inc., New York,1988), pp. 425-433.
R. Keniston, J. Enriquetz Sr, and I. Delgado, Prognostic value of undeproteinized plasma pyridoxal 5’-phosphate levels in health and disease, Ann. New York Acad. Sci. 585, 496-498 (1990).
D.B. Coursin, Nutritional and clinical aspects, Annals of the New York Acad. Sci. 585, 468-472 (1990).
Ch. Bolander - Gueaille, Focus on homocysteine (Springer Verlag France, Berlin, Heidelberg, New York, 2001).
A. Meister, Biochemistry of amino acids (Publishing of Foreign Literature, Moscow, 1957).
J.B. Ubbink, A. van der Merwe, R.H. Delport, S.P. Stabler, R. Reizler, W.J. Harward-Vermaak, The effect of subnormal vitamin B6 on homocysteine metabolism, J. Clin. Invest. 98, 177-184 (1996).
F. Binkley, G.M. Christensen, and W.V. Jensen, Pyridoxine and the transfer of sulphur, J. Biol. Chem., 194,101-113 (1952).
L.D. Greenberg, Arteriosclerotic, dental and hepatic lesions in pyridoxine-deficient monkeys, Vitamins and Hormones 22, 677-689 (1964).
G. Alfthan, J. Pekkanen, M. Jauhiainen, J. Pitkaniemi, M. Karvonen, J. Tuomilehto, J.T. Salonen, and C. Ehnoholm, Relation of serum homocysteine and lipoprotein(a) concentration to atherosclerotic disease in a prospective Finnish population based study, Atherosclerosis 106, 9-19 (1994).
P. Verhoeffer, C.H. Hennekens, R.H. Allen, S.P. Stabler, W.C. Willett, and M.J. Stampfer. Plasma total homocysteine and risk of angina pectoris with subsequent coronary artery bypass surgery, Am. J. Cardiol. 79, 799-801 (1997).
A.R. Folsom, F.J. Nieto, P.G. McGovern, M.Y. Tsai, M.R. Malinow, J.H. Eckfeldt, D.L. Hess, and C.E. Davis, Prospective study of coronary heart disease incidence in relation to fasting total homocysteine, related genetic polymorphisms, and B vitamins: The atherosclerotic risk in Communities (ARIC) study. Circulation 98,196-197 (1998).
V. Rudzite, G. Sileniece, R. Zime, and E. Jurika, Patient with hypertension and ishemic heart disease previuosly treated with antituberculous drugs, Problems of Tuberculosis, Nr.7, 42-46 (1988).
S. Yamoto, and O. Hayaishi, Tryptophan pyrrolase of rabbit intestine (D- and L-tryptophan clearing enzyme and enzymes), J. Biol. Chem. 242, 5260-5266 (1967)
R. Yoshida, U. Urade, M. Toruda, and O. Hayaishi, Induction of indolamine 2,3-dioxigenase in mouse lung during virus infection, Proc. Nail. Acad. Sci. 76, 4084-4086 (1979).
H. Yasui, K. Takai, R. Yoshida, and O. Hayaishi, Interferon induced tryptophan metabolism by inducing pulmonary indolamine 2,3-dioxigenase: Its possible occurrence in cancer-patients, Proc. Natl. Acad. Sci. 6, 101-197 (1980).
E.R Werner, M. Hirsh-Kaufmann, D. Fuchs, A. Hausen, G. Reibnegger, M. Schweiger, and H. Wachter, Interferon-gamma induced degradation of tryptophan by human cells in vitro, Biol. Chem. HoppeSeyler 368, 1407-1412 (1987).
E.R. Werner, G. Bitterlich, D. Fuchs, A. Hausen, G. Reibnegger, G. Szabo, M.P. Dierich, and H. Wachter, Human macrophages degrade tryptophan upon induction by interferon-gamma, Life Sci. 41, 273-280 (1987).
C. Huber, J.R. Batchelor, D. Fuchs, A. Hausen, A. Lang, D. Niederwieser, G. Reibnegger, P. Swetly. J. Troppmaier, and H. Wachter, Immune response-associated production of neopterin. Release from macrophages primarily under control of interferon gamma, J. Exp. Med. 160, 3010-3016 (1984).
H. Wachter, D. Fuchs, A. Hausen, G. Reibnegger, G. Weiss, E. R. Werner, G. Werner-Felmayer, Neopterin: biochemistry,methods, clinical application (Walter de Gruyter, Berlin, New York, 1992).
H. Wachter, D. Fuchs, A. Hausen, G. Reibnegger, and E.R. Werner, Neopterin as a marker for activation of cellular immunity: immunologic basis and clinical aplication, Advances in Clinical Chemistry 27, 81-141 (1987).
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Rudzite, V. et al. (2003). Prognostic Value of Tryptophan Load Test Followed by Serum Kynurenine Determination. It’s Comparison With Pyridoxal-5-phosphate, Kynurenine, Homocysteine and Neopterin Amounts. In: Allegri, G., Costa, C.V.L., Ragazzi, E., Steinhart, H., Varesio, L. (eds) Developments in Tryptophan and Serotonin Metabolism. Advances in Experimental Medicine and Biology, vol 527. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0135-0_34
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DOI: https://doi.org/10.1007/978-1-4615-0135-0_34
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