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

• Our previous studies have revealed serine/threonine kinase activity of BVR [4].
• Serine residues in IRS-1 are targets for BVR phosphorylation, and point mutation of serine residues in the kinase domain of the reductase inhibits phosphotransferase activity [4].
• We describe here the tyrosine kinase activity of human biliverdin reductase (BVR) and its potential role in the insulin-signaling pathway [4].
• Presently, small interference (si) RNA constructs were used to investigate the role of human BVR in sodium arsenite (As)-mediated induction of HO-1 and in cytoprotection against apoptosis [5].
• Ad-INV-hBVR did not effect ATF-2 expression [6].

Biological context of BLVRA

• Presently, regulation of gene expression by hBVR was examined [6].
• Activation of BVR involved increased serine/threonine phosphorylation but not its protein or transcript levels [5].
• We propose a role for BVR in the signaling cascade for AP-1 complex activation necessary for HO-1 oxidative stress response [7].
• The dimeric form, but not purified hBVR, binds to a 100-mer DNA fragment corresponding to the mouse HO-1 (hsp32) promoter region encompassing two activator protein (AP-1) sites [7].
• Fluorescence resonance energy transfer (FRET) studies indicated that HO-1(S188D) bound to cytochrome P450 reductase (CPR) and biliverdin reductase (BVR) with a slightly lower Kd than wild-type HO-1 [8].

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

• Biliverdin IXalpha reductase (BVR) catalyzes reduction of the HO activity product, biliverdin, to bilirubin. hBVR is a serine/threonine kinase that contains a bZip domain [6].
• Human biliverdin reductase (hBVR) is a serine/threonine kinase that catalyzes reduction of the heme oxygenase (HO) activity product, biliverdin, to bilirubin [7].
• In hBVR, a lysine replaces L(3) [7].
• The BVR immunoprecipitated from COS cell lysates was a phosphoprotein, and its activity and phosphorylation levels increased in response to H(2)O(2) [11].
• BVR is unique among enzymes characterized to date in that it has dual pH/cofactor (NADH, NADPH) specificity [1].

Other interactions of BLVRA

• In hBVR-infected cells, levels of HO-1 mRNA and protein were increased [6].
• Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization [12].
• A cDNA clone encoding human BVR was isolated from a gamma library using a probe generated via reverse transcription and the polymerase chain reaction from human placental RNA [1].
• Biliverdin reductase (BVR) then catalyzes the reduction of biliverdin, generating the potent intracellular antioxidant, bilirubin [13].
• Biliverdin reductase is classified into two isoforms in substrate specificity; biliverdin-IX alpha reductase and biliverdin-IX beta reductase with a molecular mass of 22 kDa and 34-42 kDa, respectively [14].

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].

References