Is homocysteine a pro-oxidant?

References

• Mudd S.H., Levy L.H., Skobvy F. Disorders on transsulfuration. The Metabolic Basis of Inherited Disease6th ed., C.R. Scriver, A.L. Beaudet, W.S. Sly, D. Valle. Mcgraw Hill, New York 1995; 1279–1327, In
   Google Scholar
• Ueland P.M., Refsum H. Plasma homoysteine, a risk factor for vascular disease: plasma levels in health, disease and drug therapy. Journal of Laboratory and Clinical Medicine 1989; 81: 2004–2006
   Google Scholar
• Malinow M.R. Homocyst(e)ine and arterial occlusive diseases. Journal Internal Medicine 1994; 17: 236–603
   Google Scholar
• D'Angelo A., Selhub J. Homocysteine and thrombotic disease. Blood 1997; 90: 1–11
   PubMed Web of Science ®Google Scholar
• De Stefano V., Zappacosta B., Persichilli S., Rossi E., Casorelli I., Paciaroni K., Chiusolo P., Leone A.M., Giardina B., Leone G. Prevalence of mild hyperhomocysteinemia and association with thrombofilic genotypes (Factor V Leiden and prothrombin G20210A) in Italian patients with venous thromboembolic disease. British Journal Haematology 1999; 106: 564–568
   PubMedGoogle Scholar
• Ratnoff O.D. Activation of Hageman factor by l-homocysteine. Science 1968; 162: 1007–1009
   PubMed Web of Science ®Google Scholar
• Rodgers G.M., Kane W.H. Activation of endogenous factor V by homocysteine-induced vascular endothelial cell activator. Journal Clinical Investigation 1986; 77: 1909–1916
   PubMed Web of Science ®Google Scholar
• Rodgers G.M., Conn M.T. Homocysteine, an atherogenic stimulus, reduces protein C activation by arterial and venous endothelial cells. Blood 1990; 75: 895–901
   PubMed Web of Science ®Google Scholar
• Stamler J.S., Osborne J.A., Jaraki O., Rabbani L.E., Mullins M., Singel D., Loscalzo J. Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen. Journal Clinical Investigation 1993; 91: 308–318
   PubMed Web of Science ®Google Scholar
• Tsai, J.C., Parrella, M.A., Yoshizumi, M., et al. Promotion of vascular smooth muscle cell growth by homocysteine: a link to atherosclerosis. Proceedings of the National Academy of Sciences of the USA 1994; 91: 6369–6373
   PubMed Web of Science ®Google Scholar
• Starkebaum G., Harlan J.M. Endothelial cell injury due copper-catalyzed hydrogen peroxide generation from homocysteine. Journal Clinical Investigation 1986; 77: 1370–1376
   PubMed Web of Science ®Google Scholar
• Loscalzo J. The oxidant stress of hyperhomocysteinemia. Journal Clinical Investigation 1996; 98: 5–7
   PubMed Web of Science ®Google Scholar
• Olszewski A.J., McCully K.S. Homocysteine metabolism and the oxidative modification of proteins and lipids. Free Radicals in Biology and Medicine 1993; 14: 683–693
   PubMedGoogle Scholar
• Pryor W.A., Squadrito G.L. The chemistry of peroxinitrite: a product from the reaction of nitric oxide with superoxide. American Journal Physiology 1995; 268: L699–L722
   PubMed Web of Science ®Google Scholar
• Crow J.P., Beckman J.S. Nitric Oxide: Biochemistry, Molecular Biology and Therapeutic Implications, L. Ignarro, F. Murad. Academic, CA 1995; 17–43, In
   Google Scholar
• Dudman N.P.B., Hicks C., Wang J., Wilcken D.E.L. Human arterial endothelial cell detachment in vitro: its promotion by homocysteine and cysteine. Atherosclerosis 1991; 91: 77–83
   PubMed Web of Science ®Google Scholar
• Zhang F., Slungaard A., Vercellotti G.M., Iadecola G. Superoxide-dependent cerebrovascular effects of homocysteine. American Journal Physiology 1998; 43: R1704–R1711
   Google Scholar
• Zappacosta B., Mordente A., Persichilli S., Giardina B., De Sole P. Effect of homocysteine on polymorphonuclear leukocytes activity and luminol-dependent chemiluminescence. Luminescence 2000; 16: 165–168
   Google Scholar
• Olinescu R., Kummerow F.A., Handler B., Fleischer L. The haemolytic activity of homocysteine is increased by the activated polymorphonuclear leukocytes. Biochemical and Biophysical Research Communications 1996; 226: 912–916
   PubMed Web of Science ®Google Scholar
• Zhou M., Diwu Z., Panchuk-Voloshina N., Haugland R.P. A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Analytical Biochemistry 1995; 253: 162–168
   Google Scholar
• Giulivi C., Cadenas E. Ferrylmyoglobin: Formation and chemical reactivity toward electron donating compounds. Methods in Enzymology 1994; 133: 404–409
   Google Scholar
• Araki A., Sako Y. Determination of free and total homocysteine in human plasma by high-performance liquid chromatography with fluorescence detector. Journal of Chromatography 1987; 422: 43–52
   PubMed Web of Science ®Google Scholar
• Galaris D., Cadenas E., Hochstein P. Redox cycling of myoglobin and ascorbate: a potential protective mechanism against oxidative reperfusion injury in muscle. Archives Biochemistry and Biophysics 1989; 273: 497–504
   PubMed Web of Science ®Google Scholar
• Crow J.P., Beckman J.S., McCord J.M. Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxinitrite. Biochemistry 1995; 34: 3544–3552
   PubMed Web of Science ®Google Scholar
• Heinecke J.W., Kawamura M., Suzuki L., Chait A. Oxidation of low density lipoprotein by thiols: superoxide-dependent and -independent mechanisms. Journal of Lipid Research 1993; 34: 2051–2061
   PubMed Web of Science ®Google Scholar
• Green R. Homocysteine and occlusive vascular disease: culprit or bystander?. Preventive Cardiology 1998; 3: 31–33
   Google Scholar
• Klebanoff S.J., Clark R.C. The Neutrophil: Function and Clinical Disordes. North-Holland, Amsterdam 1978
   Google Scholar
• Cavallini D., Denmarco C., Duprè S., Rotilio G. The copper catalyzed oxidation of cysteine to cystine. Archives Biochemistry and Biophysics 1969; 130: 354–361
   PubMed Web of Science ®Google Scholar
• Dudman N.P.B. An alternative view of homocysteine. Lancet 1999; 354: 2072–2074
   PubMed Web of Science ®Google Scholar