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Gene Review

HO2  -  heme oxygenase 2

Sus scrofa

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High impact information on HO2


Biological context of HO2


Anatomical context of HO2

  • The present study revealed by means of immunohistochemistry the presence of BVR and HO-2 in mucosal epithelial cells and in the endothelium of intramural vessels of both human and porcine gastric fundus [5].
  • Piglet cerebral microvessels and endothelial and smooth muscle cells grown on microcarrier beads were used to address the hypothesis that glutamate increases endothelial CO production by increasing HO-2 catalytic activity [6].
  • Furthermore, the vascular endothelium of the intramural vessels of the urethra, bladder and OGJ, and the extramural vessels of the bladder, displayed HO-2 immunoreactivity [7].
  • 2. HO-2 immunoreactivity was observed in coarse nerve trunks within the smooth muscle of the urethra and OGJ, and in nerve cell bodies of the enteric plexuses of the OGJ [7].
  • The similarities between heme oxygenase-2 (HO-2) and nitric oxide synthase (nNOS) and the transient expression of nNOS during development led us to investigate whether both systems are similarly affected by changes that occur during development and by regional differences along the small intestine [8].

Associations of HO2 with chemical compounds

  • 0. The rate constants for the oxidation of the LDH-NADH by HO2 and O2 determined at 23 degrees are 1.2 times 10-6 M(-1) s(-1) and 3.6 times 10-4 M(-1) s(-1), respectively [9].
  • Kinetic study by pulse radiolysis of the lactate dehydrogenase-catalyzed chain oxidation of nicotinamide adenine dinucleotide by HO2 and O2-RADICALS [9].
  • 0. The rate constant for the oxidation of the glyceraldehyde-3-phosphate dehydrogenase.NADH complex by HO2 was estimated to be 2 X 10(7) M-1 S-1 at ambient temperatures (23-24 degrees C) [10].
  • These data suggest that glutamate may activate NOS producing NO that leads to CO synthesis via a cGMP-dependent elevation of HO-2 catalytic activity [11].
  • Inhibition of protein tyrosine phosphatases increased HO-2 catalytic activity [4].

Analytical, diagnostic and therapeutic context of HO2

  • The lactate dehydrogenase-catalyzed chain oxidation of NADH (LDH-NADH) by the superoxide radicals, HO2 and O2, has been studied with pulse radiolysis in the pH range between 4.5 and 9 [9].


  1. Heme oxygenase 2: endothelial and neuronal localization and role in endothelium-dependent relaxation. Zakhary, R., Gaine, S.P., Dinerman, J.L., Ruat, M., Flavahan, N.A., Snyder, S.H. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. The mechanism of autooxidation of myoglobin. Brantley, R.E., Smerdon, S.J., Wilkinson, A.J., Singleton, E.W., Olson, J.S. J. Biol. Chem. (1993) [Pubmed]
  3. Glutamate induces oxidative stress and apoptosis in cerebral vascular endothelial cells: contributions of HO-1 and HO-2 to cytoprotection. Parfenova, H., Basuroy, S., Bhattacharya, S., Tcheranova, D., Qu, Y., Regan, R.F., Leffler, C.W. Am. J. Physiol., Cell Physiol. (2006) [Pubmed]
  4. Regulation of CO production in cerebral microvessels of newborn pigs. Leffler, C.W., Balabanova, L., Sullivan, C.D., Wang, X., Fedinec, A.L., Parfenova, H. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  5. Immunohistochemical localization of the antioxidant enzymes biliverdin reductase and heme oxygenase-2 in human and pig gastric fundus. Colpaert, E.E., Timmermans, J.P., Lefebvre, R.A. Free Radic. Biol. Med. (2002) [Pubmed]
  6. Mechanism of glutamate stimulation of CO production in cerebral microvessels. Leffler, C.W., Balabanova, L., Fedinec, A.L., Waters, C.M., Parfenova, H. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  7. Carbon monoxide-induced relaxation and distribution of haem oxygenase isoenzymes in the pig urethra and lower oesophagogastric junction. Werkström, V., Ny, L., Persson, K., Andersson, K.E. Br. J. Pharmacol. (1997) [Pubmed]
  8. Stereologic description of the changing expression of constitutive nitric oxide synthase and heme oxygenase in the enteric plexuses of the pig small intestine during development. van Ginneken, C., van Meir, F., Sys, S., Weyns, A. J. Comp. Neurol. (2001) [Pubmed]
  9. Kinetic study by pulse radiolysis of the lactate dehydrogenase-catalyzed chain oxidation of nicotinamide adenine dinucleotide by HO2 and O2-RADICALS. Bielski, B.H., Chan, P.C. J. Biol. Chem. (1975) [Pubmed]
  10. Glyceraldehyde-3-phosphate dehydrogenase-catalyzed chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals. Chan, P.C., Bielski, B.H. J. Biol. Chem. (1980) [Pubmed]
  11. Nitric oxide increases carbon monoxide production by piglet cerebral microvessels. Leffler, C.W., Balabanova, L., Fedinec, A.L., Parfenova, H. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
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