Medical Hypotheses
Volume 56, Issue 2 , Pages 259-261 , February 2001

Possible involvement of sulfane sulfur in homocysteine-induced atherosclerosis

Received 21 July 2000 ,Accepted 5 September 2000.

References 

    REFERENCES
  1. Mudd SH, Finkelstein JD, Irreverre F, Laster DW. Homocysteinuria: an enzymatic defect. Science. 1964;143:1443–1445
  2. Carson NA, Neill DW. Metabolic abnormalities detected in a survey of mentally-backward individuals in Northern Ireland. Arch Dis Child. 1962;37:505–513
  3. Gerritsen T, Vaugh JG, Waisman HA. The identification of homocystine in the urine. Biochem Biophys Res Commun. 1962;9:493–496
  4. Gibson JB, Carson NA, Neill DW. Pathological findings in homocystinuria. J Clin Pathol. 1964;17:427–437
  5. Mudd SH, Levy HL, Abeles RH. A derangement in B12metabolism leading to homocystinemia, cystathioninuria, and methylmalonic aciduria. Biochem Biophys Res Commun. 1969;35:121–126
  6. McKully KS. Vascular pathology of homocysteinemia: implications for the pathogenesis of arteriosclerosis. Am J Pathol. 1969;5:111–121
  7. Colloquium: Homocyst(e)ine, vitamins and arterial occlusive disease. J. Nutr, 1996, 126, 1235, 1300
  8. Mansoor MA, Svardal AM, Ueland PM. Determination of in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma. Anal Biochem. 1992;200:218–219
  9. Toohey JI. Sulfane sulfur in biological systems: a possible regulatory role. Biochem J. 1989;264:625–632
  10. Roisin M, Chatagner F. Homocysteine desulfhydrase from rat liver. Identification as cystathionase. Bull Soc Chim Biol. 1969;51:481–493
  11. Cavallini D, deMarco C, Mondovi B, Mori BG. The cleavage of cystine by cystathionase and the transsulfuration of hypotaurine. Enzymologia. 1960;22:161–173
  12. Flavin M, Slaughter C. The derepression and function of enzymes of reverse transsulfuration in Neurospora. Biochim Biophys Acta. 1967;132:406–411
  13. Lang T, Kessler D. Evidence for cysteine persulfide as reaction product of L-cysteine C-S lyase from Synechocystis. J Biol Chem. 1999;274:189–195
  14. Ricci G, Nardini M, Federici G, Cavallini D. The transamination of L-cystathionine, L-cystine and related compounds by bovine kidney transaminase. Eur J Biochem. 1986;157:57–63
  15. Chen SS, Walgate JH, Duerre JA. Oxidative deamination of sulfur amino acids by bacterial and snake venom L-amino acid oxidase. Arch Biochem Biophys. 1971;146:54–63
  16. Buckberry LD, Patel R, Hollingworth L, Teesdale-Spittle RH. Cysteine conjugate beta-lyase activity of amino acid decarboxylases. Biochem Soc Trans. 1998;26:S269
  17. Toohey JI. Persulfide sulfur is a growth factor for cells defective in sulfur metabolism. Biochem Cell Biol. 1986;64:758–765
  18. Tsai J, Perrela MS, Yoshizumi M, Hsieh C, Haber E, Schlegel R, et al. Promotion of vascular smooth muscle cell growth by homocysteine: a link to atherosclerosis. Proc Natl Acad Sci USA. 1994;91:6369–6373
  19. Fritzer-Szekeres M, Blom HJ, Boers GH, Szekeres T, Lubec C. Growth promotion by homocysteine but not homocysteic acid: a role for excessive growth in homocystinuria or proliferation in hyperhomocysteinemia?. Biochim Biophys Acta. 1998;1407:1–6
  20. Watanabe M, Osada J, Aratani Y. Mice deficient in cystathionine beta-synthase: animal models for mild and severe homocysteinemia. Proc Natl Acad Sci USA. 1995;92:1585–1589

PII: S0306-9877(00)91209-X

doi: 10.1054/mehy.2000.1209

Medical Hypotheses
Volume 56, Issue 2 , Pages 259-261 , February 2001