Advertisement

Bulletin of Experimental Biology and Medicine

, Volume 167, Issue 6, pp 805–808 | Cite as

Effect of the Hemoxygenase—Carbon Monoxide (HO—CO) System on the Reactivity of Uterine Artery Branches in Rats

  • A. E. Kotsyuba
  • V. M. ChertokEmail author
  • I. A. Khramova
Article
  • 4 Downloads

First to fourth-order branches of the uterine artery in sexually mature female Wistar rats were studied by biomicroscopy. After administration of a CO donor hemin (60 mM), the diameters of large uterine branches with a well-developed muscle layer markedly increased, while the increase in diameter of small vessels with one often interrupted layer of smooth muscle cells increased insignificantly. Zinc protoporphyrin IX (30 mM) in all cases blocked this effect. However, zinc protoporphyrin IX does not affect NO-mediated reaction of the branches of the uterine artery caused by administration of L-arginine (60 mM), and L-NAME did not significantly affect reactivity of uterine artery branches associated with the hemoxygenase—CO system. In contrast to NO, CO produced less potent and rapid, but more sustained effect. The target for the hemoxygenase—CO system is mainly arteries with developed muscular layer, while the target for the NO synthase—NO is small vessels where endothelium plays a Rdecisive role in the regulation of vasomotor reactions.

Key Words

biomicroscopy hemoxygenase—carbon monoxide first to third-order branches of the uterine artery donors and blockers of CO generation 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Kotsyuba AE, Chertok VM, Chertok AG. Age-Specific Characteristics of CO-Mediated Reaction of the Pial Arteries of Various Diameters in Rats. Bull. Exp. Biol. Med. 2017;162(5):658-663. doi:  https://doi.org/10.1007/s10517-017-3681-6 CrossRefPubMedGoogle Scholar
  2. 2.
    Khramova IA, Chertok VM, Kotsyuba AE, Chertok AG. Structural organization of the uterus circulatory system. Tikhookean. Med. Zh. 2018;(3):13-23. Russian.CrossRefGoogle Scholar
  3. 3.
    Chertok VM, Kotsyuba AE. Immunolocation of Heme Oxygenases in the Walls of Cerebral Arteries of Various Diameters in Rats. Bull. Exp. Biol. Med. 2017;163(2):276-279. doi:  https://doi.org/10.1007/s10517-017-3783-1 CrossRefPubMedGoogle Scholar
  4. 4.
    Chertok VM, Kotsyuba EP. Localization and Quantitative Assessment of Oxygen-Sensitive Hypoxia-Inducible Factor 1α in the Brain of the Mitten Crab Eriocheir Japonica in Normal Conditions and Acute Anoxia (an immunohistochemical study). Neurosc. Behav. Physiol. 2017;47(1):12-16.CrossRefGoogle Scholar
  5. 5.
    Chertok VM, Nemkov YuK, Chertok AG. Intraorgan vasculature of the uterus. Vladivostok, 2018. Russian.Google Scholar
  6. 6.
    Andresen JJ, Shafi NI, Durante W, Bryan RM Jr. Effects of carbon monoxide and heme oxygenase inhibitors in cerebral vessels of rats and mice. Am. J. Physiol. Heart Circ. Physiol. 2006;291(1):H223-H230.CrossRefGoogle Scholar
  7. 7.
    Fredenburgh LE, Merz AA, Cheng S. Haeme oxygenase signalling pathway: implications for cardiovascular disease. Eur. Heart J. 2015;36(24):1512-1518.CrossRefGoogle Scholar
  8. 8.
    Gagov H, Kadinov B, Hristov K, Boev K, Itzev D, Bolton T, Duridanova D. Role of constitutively expressed heme oxygenase-2 in the regulation of guinea pig coronary artery tone. Pflugers Arch. 2003;446(4):412-421.CrossRefGoogle Scholar
  9. 9.
    Leffler CW, Parfenova H, Jaggar JH. Carbon monoxide as an endogenous vascular modulator. Am. J. Physiol. Heart Circ. Physiol. 2011;301(1):H1-H11.CrossRefGoogle Scholar
  10. 10.
    Levitt DG, Levitt MD. Carbon monoxide: a critical quantitative analysis and review of the extent and limitations of its second messenger function. Clin. Pharmacol. 2015;7:37-56.PubMedPubMedCentralGoogle Scholar
  11. 11.
    Polizio AH, Santa-Cruz DM, Balestrasse KB, Gironacci MM, Bertera FM, Höcht C, Taira CA, Tomaro ML, Gorzalczany SB. Heme oxygenase-1 overexpression fails to attenuate hypertension when the nitric oxide synthase system is not fully operative. Pharmacology. 2011;87(5-6):341-349.CrossRefGoogle Scholar
  12. 12.
    Tiwari S, Ndisang JF. Heme oxygenase system and hypertension: a comprehensive insight. Curr. Pharm. Des. 2014; 20(9):1354-1369.CrossRefGoogle Scholar
  13. 13.
    Ushiyama M, Morita T, Katayama S. Carbon monoxide regulates blood pressure cooperatively with nitric oxide in hypertensive rats. Heart Vessels. 2002;16(5):189-195.CrossRefGoogle Scholar
  14. 14.
    Wesseling S, Fledderus JO, Verhaar MC, Joles JA. Beneficial effects of diminished production of hydrogen sulfide or carbon monoxide on hypertension and renal injury induced by NO withdrawal. Br. J. Pharmacol. 2015;172(6):1607-1619.CrossRefGoogle Scholar
  15. 15.
    Wu ML, Ho YC, Lin CY, Yet SF. Heme oxygenase-1 in inflammation and cardiovascular disease. Am. J. Cardiovasc. Dis. 2011;1(2):150-158.PubMedPubMedCentralGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2019

Authors and Affiliations

  • A. E. Kotsyuba
    • 1
  • V. M. Chertok
    • 1
    Email author
  • I. A. Khramova
    • 2
  1. 1.Department of Human AnatomyVladivostokRussia
  2. 2.Department of Obstetrics and GynecologyPacific State Medical UniversityVladivostokRussia

Personalised recommendations