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Gene Review

Hmox1  -  heme oxygenase (decycling) 1

Rattus norvegicus

Synonyms: HEOXG, HO-1, HSP32, Heme oxygenase 1, Heox, ...
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Disease relevance of Hmox1


Psychiatry related information on Hmox1

  • We suggest that increases in HO-1 transcript and protein reflect a means to elevate levels of antioxidants in cells with compromised defense mechanisms caused by stress [4].
  • HBP23 was constitutively expressed in KC and up-regulated on the protein and messenger RNA (mRNA) level by LPS with a time response distinct from that of TNFalpha, but in coordination with that of heme oxygenase-1 (HO-1), which is the inducible isoform of the rate-limiting enzyme of heme degradation [5].
  • Notably, the HO reaction proceeds without product inhibition by CO, which is generated in the conversion reaction of alpha-hydroxyheme to verdoheme, although CO is known to be a potent inhibitor of HO and other heme proteins [6].
  • Icv injection of the NOS inhibitor Nomega-nitro-L-arginine-methylester (L-NAME; 50 microg) or the HO inhibitor tin protoporphyrin (SnPP; 20-25 microg) significantly blunted the plasma ACTH response to a 45-min session of intermittent electroshocks [7].
  • Intrahippocampal, but not intra-amygdala, infusion of an inhibitor of heme oxygenase causes retrograde amnesia in the rat [8].

High impact information on Hmox1


Chemical compound and disease context of Hmox1


Biological context of Hmox1

  • However, the distinct stress models led to a strikingly different cell-type specific and sublobular expression pattern of HO-1 gene expression [3].
  • The acute administration of an inhibitor of HO to cirrhotic rats, at a dose that normalized aortic HO activity, was associated with significantly greater effects on arterial pressure, total peripheral vascular resistance, and cardiac index, compared with effects in sham rats [2].
  • In contrast, the other HO-1 products failed to block apoptosis or GADD153 expression during ER stress [17].
  • The capacity of ER stress to stimulate the HO-1/CO system provides a novel mechanism by which this organelle regulates cell survival [17].
  • Luciferase reporter assays indicated that ER stress stimulated HO-1 promoter activity via the antioxidant response element [17].

Anatomical context of Hmox1

  • Six hours after heat shock, an intense increase in HO-1-like protein was observed in both Purkinje cells of the cerebellum and epithelial cells lining the cerebral aqueduct of the brain [1].
  • HO-1 was mainly located in vascular smooth muscle cells of the arterial wall [2].
  • Although both non-parenchymal cell fractions expressed HO-1 transcripts, HO-1 immunoreactive protein was restricted to Kupffer cells in the normal liver [3].
  • To address this question, the expression and activity of HO in arterial vessels was studied in rats at 1, 2, and 4 weeks after bile duct ligation (BDL) or sham operation [2].
  • A progressively increased expression of HO-1 was found in aorta and mesenteric arteries of BDL rats in a close chronologic relationship with the progression from acute cholestatic liver injury (1 week) to the fully developed cirrhosis with intense systemic arterial vasodilation (4 weeks) [2].

Associations of Hmox1 with chemical compounds


Physical interactions of Hmox1


Regulatory relationships of Hmox1

  • These results suggest that ADM induces HO-1 gene expression and cGMP formation in rat VSMCs [22].
  • We conclude that HO isoform expression is segmented within the kidney and along the nephron and that treatment with an HO-1 inducer suppressed the levels of CYP4A and COX-2 proteins in a tissue-specific manner with concomitant effects on their activity [23].
  • The iNOS inhibitor aminoguanidine significantly suppressed the induction of HO-1 [19].
  • HO-1 was undetectable in CsA-treated rats compared to control while there was no change in HO-2 [24].
  • Furthermore, TGF-beta1 downregulated HO-1 mRNA after its induction by IL-1beta in vascular smooth muscle cells in culture [25].

Other interactions of Hmox1


Analytical, diagnostic and therapeutic context of Hmox1

  • The induction of a 1.8-kilobase HO-1 mRNA resulted in a pronounced increase in HO-1 protein 6 h after hyperthermia, as detected by both Western immunoblot and RIA [1].
  • Immunocytochemistry of rat brain showed discrete localization of HO-1-like protein only in neurons of select brain regions [1].
  • Because FGF-1 potently activates astroglia and exerts a direct neuroprotection after spinal cord injury or axotomy, we examined whether it regulated the expression of inducible and cytoprotective heme oxygenase-1 (HO-1) enzyme in astrocytes [30].
  • Two days following five cycles of 10 min ischemia and 10 min reperfusion, heme oxygenase (HO) and calcium-dependent nitric oxide synthase (cNOS) activities were increased 2- and 2.5-fold (p <.05), respectively [31].
  • Removal of NOS activity completely removed the benefit afforded microvascular perfusion, while inhibition of HO activity prevented the parenchymal protection [31].


  1. Rapid induction of heme oxygenase 1 mRNA and protein by hyperthermia in rat brain: heme oxygenase 2 is not a heat shock protein. Ewing, J.F., Maines, M.D. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  2. Increased vascular heme oxygenase-1 expression contributes to arterial vasodilation in experimental cirrhosis in rats. Chen, Y.C., Ginès, P., Yang, J., Summer, S.N., Falk, S., Russell, N.S., Schrier, R.W. Hepatology (2004) [Pubmed]
  3. Expression pattern of heme oxygenase isoenzymes 1 and 2 in normal and stress-exposed rat liver. Bauer, I., Wanner, G.A., Rensing, H., Alte, C., Miescher, E.A., Wolf, B., Pannen, B.H., Clemens, M.G., Bauer, M. Hepatology (1998) [Pubmed]
  4. Normal and heat-induced patterns of expression of heme oxygenase-1 (HSP32) in rat brain: hyperthermia causes rapid induction of mRNA and protein. Ewing, J.F., Haber, S.N., Maines, M.D. J. Neurochem. (1992) [Pubmed]
  5. Up-regulation of heme-binding protein 23 (HBP23) gene expression by lipopolysaccharide is mediated via a nitric oxide-dependent signaling pathway in rat Kupffer cells. Immenschuh, S., Stritzke, J., Iwahara, S., Ramadori, G. Hepatology (1999) [Pubmed]
  6. CO-trapping site in heme oxygenase revealed by photolysis of its co-bound heme complex: mechanism of escaping from product inhibition. Sugishima, M., Sakamoto, H., Noguchi, M., Fukuyama, K. J. Mol. Biol. (2004) [Pubmed]
  7. Nitric oxide and carbon monoxide have a stimulatory role in the hypothalamic-pituitary-adrenal response to physico-emotional stressors in rats. Kim, C.K., Rivier, C.L. Endocrinology (2000) [Pubmed]
  8. Intrahippocampal, but not intra-amygdala, infusion of an inhibitor of heme oxygenase causes retrograde amnesia in the rat. Fin, C., Schmitz, P.K., Da Silva, R.C., Bernabeu, R., Medina, J.H., Izquierdo, I. Eur. J. Pharmacol. (1994) [Pubmed]
  9. Heme oxygenase: a novel target for the modulation of the inflammatory response. Willis, D., Moore, A.R., Frederick, R., Willoughby, D.A. Nat. Med. (1996) [Pubmed]
  10. Carbon monoxide: a putative neural messenger. Verma, A., Hirsch, D.J., Glatt, C.E., Ronnett, G.V., Snyder, S.H. Science (1993) [Pubmed]
  11. Tin: a potent inducer of heme oxygenase in kidney. Kappas, A., Maines, M.D. Science (1976) [Pubmed]
  12. Suppression of hyperbilirubinemia in the rat neonate by chromium-protoporphyrin. Interactions of metalloporphyrins with microsomal heme oxygenase of human spleen. Drummond, G.S., Kappas, A. J. Exp. Med. (1982) [Pubmed]
  13. Heme-oxygenase-1 induction in glia throughout rat brain following experimental subarachnoid hemorrhage. Matz, P., Turner, C., Weinstein, P.R., Massa, S.M., Panter, S.S., Sharp, F.R. Brain Res. (1996) [Pubmed]
  14. Paraquat-generated oxidative stress in rat liver induces heme oxygenase-1 and aminolevulinic acid synthase. Noriega, G.O., Gonzales, S., Tomaro, M.L., Batlle, A.M. Free Radic. Res. (2002) [Pubmed]
  15. Glutamine is highly effective in preventing in vivo cobalt-induced oxidative stress in rat liver. Gonzales, S., Polizio, A.H., Erario, M.A., Tomaro, M.L. World J. Gastroenterol. (2005) [Pubmed]
  16. Heme oxygenase activity and some indices of antioxidant protection in rat liver and kidney in glycerol model of rhabdomyolysis. Kaliman, P.A., Strel'chenko, E.V., Nikitchenko, I.V., Filimonenko, V.P. Bull. Exp. Biol. Med. (2003) [Pubmed]
  17. Endoplasmic reticulum stress stimulates heme oxygenase-1 gene expression in vascular smooth muscle. Role in cell survival. Liu, X.M., Peyton, K.J., Ensenat, D., Wang, H., Schafer, A.I., Alam, J., Durante, W. J. Biol. Chem. (2005) [Pubmed]
  18. Effects of antioxidants in diabetes-induced oxidative stress in the glomeruli of diabetic rats. Koya, D., Hayashi, K., Kitada, M., Kashiwagi, A., Kikkawa, R., Haneda, M. J. Am. Soc. Nephrol. (2003) [Pubmed]
  19. Oxidative stress induces vascular heme oxygenase-1 expression in ovariectomized rats. Lee, Y.M., Cheng, P.Y., Hong, S.F., Chen, S.Y., Lam, K.K., Sheu, J.R., Yen, M.H. Free Radic. Biol. Med. (2005) [Pubmed]
  20. Heme oxygenase-1 ameliorates ischemia/reperfusion injury by targeting dendritic cell maturation and migration. Kotsch, K., Martins, P.N., Klemz, R., Janssen, U., Gerstmayer, B., Dernier, A., Reutzel-Selke, A., Kuckelkorn, U., Tullius, S.G., Volk, H.D. Antioxid. Redox Signal. (2007) [Pubmed]
  21. Selective regulation of heme oxygenase-1 expression and function by insulin through IRS1/phosphoinositide 3-kinase/Akt-2 pathway. Geraldes, P., Yagi, K., Ohshiro, Y., He, Z., Maeno, Y., Yamamoto-Hiraoka, J., Rask-Madsen, C., Chung, S.W., Perrella, M.A., King, G.L. J. Biol. Chem. (2008) [Pubmed]
  22. Adrenomedullin induces heme oxygenase-1 gene expression and cGMP formation in rat vascular smooth muscle cells. Qi, Y.F., Dong, L.W., Pan, C.S., Zhang, J., Geng, B., Zhao, J., Tang, C.S. Peptides (2005) [Pubmed]
  23. Regulation of cyclooxygenase- and cytochrome p450-derived eicosanoids by heme oxygenase in the rat kidney. Botros, F.T., Laniado-Schwartzman, M., Abraham, N.G. Hypertension (2002) [Pubmed]
  24. Protective effects of heme-oxygenase expression in cyclosporine A--induced injury. Rezzani, R., Rodella, L., Bianchi, R., Goodman, A.I., Lianos, E.A. Current neurovascular research. (2005) [Pubmed]
  25. Induction of heme oxygenase-1 during endotoxemia is downregulated by transforming growth factor-beta1. Pellacani, A., Wiesel, P., Sharma, A., Foster, L.C., Huggins, G.S., Yet, S.F., Perrella, M.A. Circ. Res. (1998) [Pubmed]
  26. Phosphorylation of c-Jun and its localization with heme oxygenase-1 and cyclooxygenase-2 in CA1 pyramidal neurons after transient forebrain ischemia. Matsuoka, Y., Okazaki, M., Zhao, H., Asai, S., Ishikawa, K., Kitamura, Y. J. Cereb. Blood Flow Metab. (1999) [Pubmed]
  27. Expression of antioxidant protective proteins in the rat retina during prenatal and postnatal development. Chen, W., Hunt, D.M., Lu, H., Hunt, R.C. Invest. Ophthalmol. Vis. Sci. (1999) [Pubmed]
  28. Antioxidant mechanism of heme oxygenase-1 involves an increase in superoxide dismutase and catalase in experimental diabetes. Turkseven, S., Kruger, A., Mingone, C.J., Kaminski, P., Inaba, M., Rodella, L.F., Ikehara, S., Wolin, M.S., Abraham, N.G. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  29. Interaction between endothelial heme oxygenase-2 and endothelin-1 in altered aortic reactivity after hypoxia in rats. Govindaraju, V., Teoh, H., Hamid, Q., Cernacek, P., Ward, M.E. Am. J. Physiol. Heart Circ. Physiol. (2005) [Pubmed]
  30. Fibroblast growth factor-1 induces heme oxygenase-1 via nuclear factor erythroid 2-related factor 2 (Nrf2) in spinal cord astrocytes: consequences for motor neuron survival. Vargas, M.R., Pehar, M., Cassina, P., Martínez-Palma, L., Thompson, J.A., Beckman, J.S., Barbeito, L. J. Biol. Chem. (2005) [Pubmed]
  31. Protective mechanisms during ischemic tolerance in skeletal muscle. Badhwar, A., Bihari, A., Dungey, A.A., Scott, J.R., Albion, C.D., Forbes, T.L., Harris, K.A., Potter, R.F. Free Radic. Biol. Med. (2004) [Pubmed]
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