1.3.1.24: biliverdin reductase
This is an abbreviated version!
For detailed information about biliverdin reductase, go to the full flat file.
Word Map on EC 1.3.1.24
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1.3.1.24
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heme
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oxygenase-1
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monoxide
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cytoprotective
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repolarization
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beat-to-beat
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rosenthal
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hyperbilirubinemia
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palliation
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tetrapyrrole
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tdp
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torsades
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diagnostics
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proarrhythmia
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medicine
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galenic
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univentricular
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pharmacology
- 1.3.1.24
- heme
- oxygenase-1
-
monoxide
-
cytoprotective
-
repolarization
-
beat-to-beat
-
rosenthal
-
hyperbilirubinemia
-
palliation
- tetrapyrrole
- tdp
-
torsades
- diagnostics
-
proarrhythmia
- medicine
-
galenic
-
univentricular
- pharmacology
Reaction
Synonyms
biliverdin IXalpha reductase, biliverdin IXbeta reductase, biliverdin reductase, biliverdin reductase A, biliverdin reductase B, Biliverdin reductase-A, biliverdin-IXalpha reductase, BLVR subtype B, BLVRA, BLVRB, BV reductase, BVR, BVR-A, BVR-B, BVRA, BVRB, F-BVR, F420H2-dependent biliverdin reductase, hBVR, hBVR-A, reductase, biliverdin, Rv2074, slr1784
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General Information
General Information on EC 1.3.1.24 - biliverdin reductase
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drug target
the enzyme (BVR-A) is a potential therapeutic target to prevent brain insulin resistance in Alzheimer disease
malfunction
metabolism
physiological function
additional information
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using BVR siRNA, blocking generation of bilirubin, reverses the effect of hypoxia on enhancing cell survival and apoptotic protein (Bcl-2, procasepase-9, procasepase-3) expression, preventing nuclear shrinkage, DNA fragmentation and mitochondrial depolarization in starved pulmonary arterial smooth muscle cell, which are recovered by exogenous bilirubin. The inhibitory effect of bilirubin on pulmonary arterial smooth muscle cell apoptosis under hypoxic condition is blocked by the inhibitor of ERK1/2 pathway
malfunction
impairment of biliverdin reductase-A (BVR-A) is an early event leading to brain insulin resistance in Alzheimer disease. Cells lacking the enzyme (BVR-A) develop insulin resistance if treated with insulin and can be recovered from insulin resistance only if treated with a BVR-A-mimetic peptide
malfunction
the loss of biliverdin reductase A results in the reduction of mitochondria number, decreased expression of markers of mitochondrial biogenesis, uncoupling, oxidation, and fusion, which paralleles reduced mitochondrial oxygen consumption. Biliverdin reductase A KO cells exhibit increased levels of ROS generation and decreased levels of superoxide dismutase mRNA expression
metabolism
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HIF-1alpha regulates the expression of BVR and other enzymes involved in oxidative stress response in lung macrophages, overview
metabolism
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the heme oxygenase/biliverdin reductase axis is the main metabolic pathway for heme degradation. Activation during stress results in increased heme degradation and acceleration of biliverdin transformation to bilirubin
metabolism
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the heme oxygenase/biliverdin reductase axis is the main metabolic pathway for heme degradation. Activation suirng stress results in increased heme degradation and acceleration of biliverdin transformation to bilirubin
metabolism
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it is shown that the rates of sHO-1 (shortened form of heme oxygenase-1) metabolism in the presence and absence of BVR are equal
metabolism
isoform BVRA interacts with components in both the PI3-kinase/Akt and the IRK/IRS/PI3-kinase/MAPK pathyway
metabolism
the enzyme is a coactivator of Akt1 and a key mediator of the Akt1/glycogen synthase kinase 3 pathway
metabolism
critical role for biliverdin reductase A in protecting against lipid accumulation and oxidative stress in hepatocytes which may serve as a future therapeutic target for non-alcoholic fatty liver disease (NAFLD) and its progression to non-alcoholic steatohepatitis (NASH)
metabolism
key enzymes of the hemoglobin degradation cascade. Biliverdin reductase is probably also involved in protecting choroid plexus epithelial cells and the blood-cerebrospinal fluid barrier from the negative effects of subarachnoid hemorrhage
metabolism
the enzyme catalyzes the reduction of heme-derived biliverdin into bilirubin, which is a powerful endogenous free radical scavenger
biliverdin reductase converts biliverdin to bilirubin. Additionally, acting as a transcription factor and possessing a capacity of a serine/threonine kinase, it may modulate signaling pathways. BVR exhibits cytoprotection, important role of PKCa/b kinase in BVR-mediated improvement in cell survival
physiological function
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blockage of BVR protein expression by retroviral siBVR inhibits the HO-2 protein induction but not vice versa
physiological function
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BV reductase regulates cell growth and apoptosis, its knockdown increases apoptosis. The BVR also phosphorylates the insulin receptor substrate 1, IRS-1, on serine residues preventing its phosphorylation by insulin receptor, which represent a physiological mechanism for increasing glucose uptake. And BVR is a nuclear transporter of ERK1/2 with metabolic regulatory role
physiological function
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BV reductase regulates cell growth and apoptosis, its knockdown increases apoptosis. The BVR also phosphorylates the insulin receptor substrate 1, IRS-1, on serine residues preventing its phosphorylation by insulin receptor, which represent a physiological mechanism for increasing glucose uptake. And BVR is a nuclear transporter of ERK1/2 with metabolic regulatory role
physiological function
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BVR is required for heme degradation. BVR plays a role in bile pigment metabolism, in cell protection, and in signal transduction, detailed overview. BVR reverses the inhibitory effect of biliverdin on PKC enzymes
physiological function
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coordinated increased expression of biliverdin reductase and heme oxygenase-2 promotes cardiomyocyte survival, a reductase-based peptide counters beta-adrenergic receptor ligand-mediated cardiac dysfunction
physiological function
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primary spontaneous pneumothorax, PSP, in smokers is associated with lung macrophage oxidative stress. The response to this condition involves HIF-1alpha-mediated induction of HO-1, BVR and H-ferritin. Cigarette smoke is a risk factor of recurrence of the disease, overview
physiological function
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the significant effect of biliverdin on decrease in extracellular oxidative stress in BVR-deficient cells may be related to direct scavenging of extracellular reactive oxygen and nitrogen species by biliverdin
physiological function
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BLVRA may be among the most effective physiological reactive oxygen species scavenging systems and may play an important role in regulating cellular senescence
physiological function
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BVR-A up-regulation and post-translational modifications significantly correlate with beta-secretase protein levels in the brain
physiological function
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H2O2 markedly induces BLVRA activity in young human diploid fibroblasts, but not in senescent human diploid fibroblasts(HDF). Depletion of BLVRA reduces the H2O2-dependent induction of heme oxygenase-1 (HO-1) in young human diploid fibroblasts, but not in senescent cells. Lentiviral RNAi transfected stable primary HDFs with reduced BLVRA expression show upregulation of the CDK inhibitor family members p16, p53, and p21, followed by cell cycle arrest in G0-G1 phase with high expression of senescence-associated beta-galactosidase
physiological function
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hBVR suppresses Goodpasture antigen-binding protein autophosphorylation in a concentration-dependent manner. The inhibitory effect of hBVR on GPBP kinase activity extended to its ability to phosphorylate its substrate, GPA-derived peptide
physiological function
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TNF-alpha alpha-NF-kappaB-dependent expression of Goodpasture antigen-binding protein is regulated by biliverdin reductase
physiological function
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the cytoprotective role of the enzyme may be permissive for cancer/tumor growth. The enzyme plays a role in transporting kinases to the membrane and nucleus and can also transport heme within the cell. The enzyme suppresses the activity of Goodpasture antigen-binding protein and hence limits the exposure of the epitope of Goodpasture antigen, thus limiting autoimmunity
physiological function
the enzyme mediates interleukin-10 expression in macrophages
physiological function
the enzyme protects against glucose intolerance and diabetes by affecting the pancreatic islet. Isoform BVRA enhances protein kinase CbetaII localization at the cellular membrane and also modulates protein kinase Cdelta and protein kinase Czeta
physiological function
a biliverdin reductase-A (BLVRA)-dependent mechanism regulates inflammatory responses and splenocyte death after germinal matrix hemorrhage (GMH)
physiological function
the enzyme exerts a protective role in oxidative stress-induced hippocampal neuronal cell damage by regulating the apoptosis and MAPK signaling
physiological function
the enzyme is involved in the pathogenesis of neurodegenerative, metabolic, cardiovascular and immune-inflammatory diseases as well as in cancer
physiological function
the enzyme regulates the molecular mechanism underlying cancer development
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bilirubin is a superior antioxidant in isolated mitochondria and neutrophils as compared to biliverdin, overview. XO-derived superoxide is decreased in a concentration-dependent fashion by bilirubin whereas biliverdin has no inhibitory effect and even significantly increases the signal pointing towards pro-oxidative effects
additional information
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bilirubin is an important component of cellular defense mechanisms with cytoprotective features
additional information
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isoproterenol, ISO, stimulation of BVR levels enhances the stability of heme oxygenase 2, HO-2. Interaction between HO-2 and BVR is a survival factor for cardiomyocytes during ISO stimulation
additional information
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pharmacodynamics of the heme oxygenase/biliverdin reductase system, overview
additional information
the BVR activity and expression is not affected by MAP kinase inhibitors, overview