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Gene Review

BLVRA  -  biliverdin reductase A

Homo sapiens

Synonyms: BLVR, BVR, BVR A, BVRA, Biliverdin reductase A, ...
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Disease relevance of BLVRA

  • That human BVR is a Zn metalloprotein was further substantiated by 65Zn exchange analysis of both the purified and the fusion protein expressed in Escherichia coli [1].
  • Since BVR regenerates bilirubin in a redox cycle without significantly increasing the concentration of bilirubin, our results suggest that BVR may represent a novel strategy for the treatment of multiple sclerosis and other oxidative stress-mediated diseases [2].

Psychiatry related information on BLVRA

  • According to group comparisons, patients with an MVR improve more than those with a BVR on the mental health subscale [3].

High impact information on BLVRA


Biological context of BLVRA


Anatomical context of BLVRA

  • The potential significance of the AP-1 binding is suggested by the finding that the response of HO-1, in COS cells stably transfected with antisense hBVR, with 66% reduced BVR activity, to superoxide anion (O(2)()) formed by menadione is attenuated, whereas induction by heme is not affected [7].
  • The secondary structure model of hBVR predicts an alpha-helix-turn-beta-sheet for this domain. hBVR translated by the rabbit reticulocyte lysate system appears on a nondenaturing gel as a single band with molecular mass of approximately 69 kDa [7].
  • In addition, caveolae contained endogenous BVR activity, supporting the same compartmentalization of both enzymes [9].
  • OBJECTIVES: The purpose of this study was to localize in cranial ganglia of man the occurrence of the putative gaseous neural messenger carbon monoxide (CO) and the biliverdin degrading enzyme biliverdin reductase (BVR) [10].
  • Double immunostaining revealed that in the human trigeminal ganglion HO-2 and BVR co-localized with calcitonin gene-related peptide [10].

Associations of BLVRA with chemical compounds


Other interactions of BLVRA


Analytical, diagnostic and therapeutic context of BLVRA

  • Titration of protein phosphatase 2A-released phosphates indicated a 1:6 molar ratio of BVR to phosphate [11].
  • Sequence analysis indicated that the human reductase shows approximately 83% identity, at both the nucleotide and amino acid levels, with rat BVR [1].
  • Based on spectroscopic measurements and new BVR photometry, we find that the M dwarf secondary's contribution to the combined light is smaller than previously reported, probably because of the difficulty of avoiding contamination from a third star 3".2 distant [15].
  • Strain-gauge plethysmography of the lower limbs was used to calculate arterial calf blood flow (RF), arterial calf blood flow after post-ischaemic hyperaemia (PF), basal and minimal vascular resistances (BVR and MVR), time to reach peak flow (tPF), time until 50% reduction of peak flow (tT1/2) and total recovery time (tT) [16].
  • Isoelectric focusing of BLVR reveals genetically determined variation among inbred strains of mice [17].


  1. Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes. Maines, M.D., Polevoda, B.V., Huang, T.J., McCoubrey, W.K. Eur. J. Biochem. (1996) [Pubmed]
  2. Biliverdin reductase, a major physiologic cytoprotectant, suppresses experimental autoimmune encephalomyelitis. Liu, Y., Liu, J., Tetzlaff, W., Paty, D.W., Cynader, M.S. Free Radic. Biol. Med. (2006) [Pubmed]
  3. Quality of life before and after heart valve surgery is influenced by gender and type of valve. Taillefer, M.C., Dupuis, G., Hardy, J.F., LeMay, S. Quality of life research : an international journal of quality of life aspects of treatment, care and rehabilitation. (2005) [Pubmed]
  4. Human biliverdin reductase: a member of the insulin receptor substrate family with serine/threonine/tyrosine kinase activity. Lerner-Marmarosh, N., Shen, J., Torno, M.D., Kravets, A., Hu, Z., Maines, M.D. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  5. Small interference RNA-mediated gene silencing of human biliverdin reductase, but not that of heme oxygenase-1, attenuates arsenite-mediated induction of the oxygenase and increases apoptosis in 293A kidney cells. Miralem, T., Hu, Z., Torno, M.D., Lelli, K.M., Maines, M.D. J. Biol. Chem. (2005) [Pubmed]
  6. Biliverdin reductase, a novel regulator for induction of activating transcription factor-2 and heme oxygenase-1. Kravets, A., Hu, Z., Miralem, T., Torno, M.D., Maines, M.D. J. Biol. Chem. (2004) [Pubmed]
  7. Human biliverdin reductase is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress. Ahmad, Z., Salim, M., Maines, M.D. J. Biol. Chem. (2002) [Pubmed]
  8. Protein kinase Akt/PKB phosphorylates heme oxygenase-1 in vitro and in vivo. Salinas, M., Wang, J., Rosa de Sagarra, M., Martín, D., Rojo, A.I., Martin-Perez, J., Ortiz de Montellano, P.R., Cuadrado, A. FEBS Lett. (2004) [Pubmed]
  9. Caveolae compartmentalization of heme oxygenase-1 in endothelial cells. Kim, H.P., Wang, X., Galbiati, F., Ryter, S.W., Choi, A.M. FASEB J. (2004) [Pubmed]
  10. The presence of heme-oxygenase and biliverdin reductase in human cranial ganglia indicates a role for carbon monoxide in neural transmission. Uddman, R., Tajti, J., Sundler, F., Cardell, L.O. Neuro Endocrinol. Lett. (2004) [Pubmed]
  11. Human biliverdin reductase is autophosphorylated, and phosphorylation is required for bilirubin formation. Salim, M., Brown-Kipphut, B.A., Maines, M.D. J. Biol. Chem. (2001) [Pubmed]
  12. Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization. Yamaguchi, T., Komoda, Y., Nakajima, H. J. Biol. Chem. (1994) [Pubmed]
  13. Regulation and expression of heme oxygenase enzymes in aged-rat brain: age related depression in HO-1 and HO-2 expression and altered stress-response. Ewing, J.F., Maines, M.D. Journal of neural transmission (Vienna, Austria : 1996) (2006) [Pubmed]
  14. Cloning and characterization of the cDNA encoding human biliverdin-IX alpha reductase. Komuro, A., Tobe, T., Nakano, Y., Yamaguchi, T., Tomita, M. Biochim. Biophys. Acta (1996) [Pubmed]
  15. The 0.8 day orbit of the precataclysmic binary EUVE J1016-053. Thorstensen, J.R., Vennes, S., Bowyer, S. Astrophys. J. (1996) [Pubmed]
  16. Evaluation of regional haemodynamics and alterations of vascular wall of the lower limbs in hypertensive subjects. Pinto, A., Scaglione, R., Galati, D., Paterna, S., Parrinello, G., Arnone, S., Licata, G. Eur. Heart J. (1995) [Pubmed]
  17. Confirmation of the assignment of human biliverdin reductase to chromosome 7. Parkar, M., Jeremiah, S.J., Povey, S., Lee, A.F., Finlay, F.O., Goodfellow, P.N., Solomon, E. Ann. Hum. Genet. (1984) [Pubmed]
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