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ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2003; 49(6): 14-21

Cardioprotective effect of heme oxigenase-1induction by hemin on the isolated heart of rat at ischemia/reperfusion

T.V. Kukoba, O.O. Moybenko, A.V. Kotsjuruba

    Bogomoletz Institute of Physiology National Academy ofSciences of Ukraine,A.V. Palladin Institute of Biochemistry National Academy ofSciences of Ukraine



Abstract

The aim of the study was to determine the role of both an inducible isoform of heme oxygenase (HO-1) and products of heme catabolism (carbon monoxide (CO), cardiac bilirubin and Fe2+) in protecting myocardium against post-ischemic myocardial dysfunction. Rat hearts were isolated and per- fused according to the Langendorff technique to evaluate the recovery of myocardial function after total ischemia (20 min) and reperfusion (40 min) and production of reactive oxygen forms at a reperfusion phase. Ischemia/reperfusion caused impairment in myocardial function: left ventricular develop- ing pressure (LVDP) was shown to be decreased , while end- diastolic pressure (EDP) and both coronary perfusion pres- sure and coronary resistance increased. Free oxygen radicals were generated at the reperfusion phase which led to injuries to cardiomyocytes and creatine kinase efflux into perfusate. We have found that upregulation of HO-1 by preliminary (24 h before ischemia) injections of 25 mg/kg hemin (i.p) resulted in improving the myocardial function due to increas- ing the enzyme activity and forming the cardial bilirubine, while generation of reactive oxygen forms was inhibited, as well as the contents of creatine kinase reduced. As a result, impairment in cardiomyocytes diminished, and coronary vessels dilated to improve the functional paramrtres of the heart work

Full text: (PDF, in Ukrainian)

References

  1. Калиман П.А., Никитченко И.В., Сокол О.А., Стрельченко Е.В. Регуляция гемоксигеназной активности в печени крыс при оксидативном стрессе, вызванном хлоридом кобальта и хлоридом ртути // Биохимия. – 2001. – 66, вып. 1. – C. 98 – 104.
  2. Стрельченко Е.В., Никитченко И.В., Калиман П.А. Гемоксигеназная активность в органах крыс при введении хлорида кадмия // Укр. біохім. журн. – 2002. – 74, №5. – C. 107 – 111.
  3. Тимошин А.А., Лакомкин В.Л., Рууге Э.К. Свободнорадикальные центры в ткани изолированного миокарда крысы в условиях перфузии безсубстратным раствором с нормальной оксигенацией // Биофизика – 1996. – 41, вып. 6. – C. 1305 – 1308.
  4. Berenshtein E., Vaisman B., Goldberg-Langerman C. et al. Roles of ferritin and iron in ischemic preconditioning of the heart // Mol. Cell. Biochem. – 2002. – 234-235, №1-2. – P. 283 – 292.
  5. Brouard S., Otterbein L.E., Anrather J. et al. Carbon Monoxide Generated by Heme Oxygenase 1 Suppresses Endothelial Cell Apoptosis // J. Exp. Med. – 2000. – 192, № 7. – P. 1015 – 1026.
  6. Clark J.E., Foresti R., Sarathchandra P. et al. – Heme oxygenase-1-derived bilirubin ameliorates postischemic myocardial dysfunction // Amer. J. Physiol. – 2000. – 278, Issue 2. – P. H643-H651
  7. Coceani F. Carbon Monoxide in Vasoregulation The Promise and the Challenge // Circulat. Res. – 2000. – 86, № 12. – P. 1184 – 1186.
  8. Conte D., Narindrasorasak S., Sarkar B. In Vivo and in Vitro iron-replaced Zinc Finger Generates Free Radicals and Causes DNA Damage // J. Boil. Chem. – 1996. – 271, №9. – P. 5125 – 5130.
  9. 9. Eisenstein R.S., Garcia-Mayol D., Pettingell W., Munro H.N. Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron // PNAS. – 1991. – 88, № 3. – P. 688 – 692.
  10. 10. Furchgott R.F., Jothianandan D. Endothelium-dependent and independent vasodilation involving cyclic GMP: re- laxation induced by nitric oxide, carbon monoxide and light // Blood. Vessels. –1991. – 28, № 1-3. – P. 52 – 61.
  11. Gopinathan V., Miller N.J., Milner A.D. et al. – Bilirubin and ascorbate antioxidant activity in neonatal plas- ma // FEBS Lett. – 1994. – 349, № 2. – P. 197 – 200.
  12. Hangaishi M., Ishizaka N., Aizawa T. et al. Induction of heme oxygenase-1 can act protectively against cardiac is- chemia/reperfusion in vivo // Biochem. Biophys. Res. Com- mun. – 2000. – 279, №2. – P. 582 – 588.
  13. Huwiler M., Kohler H. Pseudo-catalytic degradation of hydrogen peroxide in the lactoperoxidase/ Н2О2 iodide system // Eur. J. Biochem. – 1984. – 141, №1. – P. 68 – 74.
  14. Lee P.J., Alam J., Wiegand G.W. et al. – Overexpression of heme oxygenase-1 expression in human pulmonary epithelial cells results in cell growth arrest and increased resistance to hyperoxia // Ibid. – 1996. – 93, № 19. – P. 10393 – 10398.
  15. Maines M.D., Ibrahim N.G., Kappas A. Solubilisation and partial purification of heme oxigenase from liver // J. Biol. Chem. – 1977. – 252, № 16. – P. 5900 – 5903.
  16. McCord J.M., Fridovich I.A. A quatitativ test for superoxide radicals produced in biological systems // Biochem. J. – 1982. – 203, №3. – P. 551 – 558.
  17. Otterbein L.E., Bach F.H., Alam J. et al. – Carbon monoxide has anti-inflammatory effects involving the mitogen-activated protein kinase pathway // Natur. Med. – 2000. – 6, № 4. – P. 422 – 428.
  18. Panchenko M.V., Farber H.W., Korn J.H. Induction of heme oxygenase-1 by hypoxia and free radicals in human dermal fibroblasts // Amer. J. Physiol. – 2000. – 278, Issue 1. – P. C92 – C101.
  19. 19. Petrache I., Otterbein LE., Alam J. et al. Heme oxygenase1 inhibits TNF-?-induced apoptosis in cultured fibroblast // Amer. J. Physiol. Lung Cell Mol. Physiol. – 2000. – 278, Issue 2. – P. 312L – 319.
  20. 20. Ryter S.W., Tyrrell R.M. The heme synthesis and degraТ. В. Кукоба, О.О. Мойбенко, А.В. Коцюруба dation pathways: role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties // Free Radic. Biol. Med. – 2000. – 28, № 2. – P. 289 – 309.
  21. Snyder S.H., Jaffrey S.R., Zakhary R. Nitric oxide and carbon monoxide: parallel roles as neural messengers // Brain. Res. Rev. – 1998. – № 2-3. – P. 167 – 175.
  22. Stocker R., Yamamoto Y., McDonagh A.F. et al. – Bilirubin is an antioxidant of possible physiological importance // Science. – 1987. – 235, № 4792. – P. 1043 – 1046.
  23. Suttner D.M., Dennery P.A. Reversal of HO-1 related cytoprotection with increased expression is due to reactive iron // FASEB J. – 1999. – 13, № 13. – P. 1800 – 1809.
  24. Verma A., Hirsch D.J., Glatt C.E. et al. – Carbon monoxide: a putative neural messenger // Science. – 1993. – 259, № 5093. – P. 381 – 384.
  25. Vile G.F., Basu-Modak S., Waltner C., Tyrrell M. Hemeoxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts // PNAS. – 1994. – 91, № 7. – P. 2607 – 2610.
  26. Vreman H.J., Wong R.J., Sanesi C.A. et al. Simultaneous production of carbon monoxide and thiobarbituric acid reactive substances in rat tissue preparations by an iron- ascorbate system // Can. J. Physiol. Pharmacol. – 1998. – 76, №12. – P. 1057 – 1065.
  27. Yamada N., Yamaya M., Okinaga S. et al. – Protective Effects of Heme Oxygenase-1 against Oxidant-Induced Injury in the Cultured Human Tracheal Epithelium // Amer. J. Respirat. Cell. Mol. Boil. – 1999. – 21, № 3. – P. 428 –435
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