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Akt protein + NAD(P)H
?
-
-
-
-
-
?
bilirubin + NAD(P)+
biliverdin + NAD(P)H + H+
-
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
bilirubin + NADP+
biliverdin + NADPH + H+
bilirubin-IXa + NAD+
biliverdin-IXa + NADH + H+
-
-
-
-
?
bilirubin-IXa + NADP+
biliverdin-IXa + NADPH + H+
-
-
-
-
?
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
biliverdin + NAD(P)H
bilirubin + NAD(P)+
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
biliverdin + NADH + H+
bilirubin + NAD+
biliverdin + NADPH + H+
bilirubin + NADP+
biliverdin IXalpha + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin IXalpha + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin IXalpha + NAD(P)H + H+
bilirubin IXalpha + NAD(P)+
biliverdin IXalpha + NADH + H+
bilirubin IXalpha + NAD+
substrate for isoform BVRA
-
-
r
biliverdin IXalpha + NADPH + H+
bilirubin IXalpha + NADP+
substrate for isoform BVRA
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin IXbeta + NAD+
substrate for isoform BVRB
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin IXbeta + NADP+
substrate for isoform BVRB
-
-
r
casein + NAD(P)H
?
-
BVR functions as an serine/threonine kinase for casein
-
-
?
Elk-1 protein + NAD(P)H
?
-
-
-
-
?
extracellular signal-regulated kinase 1 + NAD(P)H
?
-
-
-
-
?
extracellular signal-regulated kinase 2 + NAD(P)H
?
-
-
-
-
?
insulin receptor substrate 1 + NAD(P)H
?
insulin receptor substrate-1 + NAD(P)H
?
-
the serine residues are targets for BVR phosphorylation
-
-
?
insulin-receptor substrate 1 + NAD(P)H
?
-
BVR functions as an serine/threonine kinase for insulin-receptor substrate 1
-
-
?
mitogen-activated protein kinase kinase 1 + NAD(P)H
?
-
-
-
-
?
myelin basic protein + NAD(P)H
?
-
BVR functions as an serine/threonine kinase for myelin basic protein
-
-
?
phosphatidylinositol 3-kinase + NAD(P)H
?
-
-
-
-
-
?
protein kinase C-betaII + NAD(P)H
?
-
BVR functions as an serine/threonine kinase for protein kinase C-betaII
-
-
?
additional information
?
-
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
-
?
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
?
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
?
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
r
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
-
-
-
-
?
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
specific for biliverdin and IXalpha faster than the biliverdin isomers IXbeta, IXr or IXdelta
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
activity with NADPH is 50 times greater than with NADH
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
high but no absolute specificity for natural IXalpha isomeric form
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
it is proposed that the propionate side chains bridging the C10 position on the tetrapyrrole interact with the positively charged residues on biliverdin reductase A to promote binding and subsequent catalysis
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
human enzyme is a leucine zipper-like DNA-binding protein and functions in transcriptional activation of heme oxygenase-1 by oxidative stress
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
NADH and NADPH can be replaced by 3-acetyl-NADPH and deamino-NADPH (biliverdin I and biliverdin IX reduction)
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
two and four propionates in the biliverdin structure give a biliverdin with substrate activity but biliverdins carrying methyl, ethyl and one propionate residue in their structure and biliverdins with one propionate and one acetate residue or with two acetate residues are no substrates
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
specificity of the different molecular forms
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
study with different biliverdin types
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
pig spleen: IXalpha-biliverdin: most effective substrate among the 4 biliverdin isomers
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
not: IXalpha-biliverdin methylester (pig spleen)
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
pig spleen: strictly specific to biliverdin, no other oxidoreductase activities
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
importance in linear tetrapyrrole metabolism
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
Syncerus sp.
-
-
-
-
r
biliverdin + NAD(P)H
bilirubin + NAD(P)+
Syncerus sp.
-
bile pigment formation
-
r
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
-
?
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin IXalpha + NAD(P)H + H+
bilirubin IXalpha + NAD(P)+
substrate of BVRA but not of BVRB isoform
-
-
ir
biliverdin IXalpha + NAD(P)H + H+
bilirubin IXalpha + NAD(P)+
substrate of BVRA but not of BVRB isoform
-
-
ir
insulin receptor substrate 1 + NAD(P)H
?
-
-
-
-
?
insulin receptor substrate 1 + NAD(P)H
?
phosphorylates serine residues in insulin receptor substrate 1
-
-
?
insulin receptor substrate 1 + NAD(P)H
?
phosphorylates serine residues in insulin receptor substrate 1
-
-
?
additional information
?
-
-
enzyme advances the role of heme oxidase 1 in cytoprotection and also affords cytoprotection independent of heme degradation
-
-
?
additional information
?
-
-
enzyme may be an essential component of normal physiologic gastrointestinal defense
-
-
?
additional information
?
-
-
enzyme physiologically regenerates bilirubin in a catalytic cycle, providing antioxidant cytoprotection
-
-
?
additional information
?
-
-
role of enzyme in regulation of activating protein 1 and cAMP-regulated genes and in cell signaling
-
-
?
additional information
?
-
biliverdin IXalpha is no substrate BVRB isoform
-
-
?
additional information
?
-
biliverdin IXalpha is no substrate BVRB isoform
-
-
?
additional information
?
-
BVR has also serine/threonine/tyrosine kinase activity
-
-
?
additional information
?
-
BVR has also serine/threonine/tyrosine kinase activity
-
-
?
additional information
?
-
BVR is a substrate for insulin receptor tyrosine kinase
-
-
?
additional information
?
-
BVR is a substrate for insulin receptor tyrosine kinase
-
-
?
additional information
?
-
-
BVR is likely to affect the activation of nuclear factor kappaB both in its capacity as a reductase as well as a kinase
-
-
?
additional information
?
-
-
BVR is an S/T/Y kinase
-
-
?
additional information
?
-
-
the enzyme shows dual cofactor- and pH-dependency in activity
-
-
?
additional information
?
-
-
hBVR binds to Goodpasture antigen-binding protein and down-regulates its TNF-alpha-stimulated kinase activity
-
-
?
additional information
?
-
-
protein kinase Cdelta is activated by the enzyme. Protein kinase Cdelta is not a substrate for the enzyme in vitro
-
-
?
additional information
?
-
-
heme-oxygenase-1-dependent activation of Akt protein is in part mediated by BVR
-
-
?
additional information
?
-
-
enzyme diverts tetrapyrrole metabolism toward heme synthesis while also reducing heme levels to de-repress synthesis of 5-aminolevulinic acid
-
-
?
additional information
?
-
-
biliverdin IXalpha is no substrate of BVRB isoform
-
-
?
additional information
?
-
biliverdin IXalpha is no substrate of BVRB isoform
-
-
?
additional information
?
-
-
BVR has also serine/threonine/tyrosine kinase activity
-
-
?
additional information
?
-
BVR has also serine/threonine/tyrosine kinase activity
-
-
?
additional information
?
-
-
BVR is a substrate for insulin receptor tyrosine kinase
-
-
?
additional information
?
-
BVR is a substrate for insulin receptor tyrosine kinase
-
-
?
additional information
?
-
-
BVR is an S/T/Y kinase
-
-
?
additional information
?
-
-
the enzyme shows dual cofactor- and pH-dependency in activity
-
-
?
additional information
?
-
-
enzyme may be an essential component of normal physiologic gastrointestinal defense
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
bilirubin + NAD(P)+
biliverdin + NAD(P)H + H+
-
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
bilirubin + NADP+
biliverdin + NADPH + H+
bilirubin-IXa + NAD+
biliverdin-IXa + NADH + H+
-
-
-
-
?
bilirubin-IXa + NADP+
biliverdin-IXa + NADPH + H+
-
-
-
-
?
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
biliverdin + NAD(P)H
bilirubin + NAD(P)+
biliverdin + NADH + H+
bilirubin + NAD+
biliverdin + NADPH + H+
bilirubin + NADP+
biliverdin IXalpha + NAD(P)H + H+
bilirubin + NAD(P)+
-
-
-
-
?
biliverdin IXalpha + NADH + H+
bilirubin IXalpha + NAD+
substrate for isoform BVRA
-
-
r
biliverdin IXalpha + NADPH + H+
bilirubin IXalpha + NADP+
substrate for isoform BVRA
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin IXbeta + NADH + H+
bilirubin IXbeta + NAD+
substrate for isoform BVRB
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin IXbeta + NADPH + H+
bilirubin IXbeta + NADP+
substrate for isoform BVRB
-
-
r
additional information
?
-
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
r
bilirubin + NAD+
biliverdin + NADH + H+
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
-
-
-
-
r
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
-
-
-
-
?
biliverdin + coenzyme F420 + H+
bilirubin + reduced coenzyme F420
-
-
-
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
physiologic degradation of heme to bile pigments
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
-
importance in linear tetrapyrrole metabolism
-
?
biliverdin + NAD(P)H
bilirubin + NAD(P)+
Syncerus sp.
-
bile pigment formation
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
-
-
-
r
additional information
?
-
-
enzyme advances the role of heme oxidase 1 in cytoprotection and also affords cytoprotection independent of heme degradation
-
-
?
additional information
?
-
-
enzyme may be an essential component of normal physiologic gastrointestinal defense
-
-
?
additional information
?
-
-
enzyme physiologically regenerates bilirubin in a catalytic cycle, providing antioxidant cytoprotection
-
-
?
additional information
?
-
-
role of enzyme in regulation of activating protein 1 and cAMP-regulated genes and in cell signaling
-
-
?
additional information
?
-
-
BVR is an S/T/Y kinase
-
-
?
additional information
?
-
-
the enzyme shows dual cofactor- and pH-dependency in activity
-
-
?
additional information
?
-
-
hBVR binds to Goodpasture antigen-binding protein and down-regulates its TNF-alpha-stimulated kinase activity
-
-
?
additional information
?
-
-
enzyme diverts tetrapyrrole metabolism toward heme synthesis while also reducing heme levels to de-repress synthesis of 5-aminolevulinic acid
-
-
?
additional information
?
-
-
BVR is an S/T/Y kinase
-
-
?
additional information
?
-
-
the enzyme shows dual cofactor- and pH-dependency in activity
-
-
?
additional information
?
-
-
enzyme may be an essential component of normal physiologic gastrointestinal defense
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5,5'-dithiobis(2-nitrobenzoate)
Arsenobenzoate
-
1 mM, slight
biliverdin IXalpha
-
with cofactor NADPH, inhibitory above 0.004 mM, with cofactor NADH, inhibitory above 0.018 mM
Ca2+
-
abolishes autophosphorylation of BVR
GATA1
-
transcription factor GATA1 downregulates BVR expression
-
HgCl2
-
irreversible inhibition
Iron-hematoporphyrin
-
competitive, acts as biliverdin-bilirubin analog
Metalloporphyrin complexes
-
-
-
Mg2+
-
abolishes autophosphorylation of BVR
NADH
-
at pH 8.5, competitive to NADPH
NADPH
-
at pH 7.0, competitive to NADH
p-hydroxymercuribenzoate
-
-
potato acid phosphatase
-
human bilverdin reductase expressed in E. coli
-
Protein phosphatase 2A
-
human bilverdin reductase expressed in E. coli, okadaic acid attenuates the inhibition
-
SH-reactive agent
-
34000 Da form extremely sensitive to, larger 68000 Da form lacks sensitivity to
-
Zn2+
-
inhibitory to autophosphorylation of BVR, can not be overcome with Mn2+
additional information
-
since no specific inhibitors for BVR are known, siRNA is used to silence the BVR gene in primary endothelial cells and accordingly suppress its activity
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,5'-dithiobis(2-nitrobenzoate)
-
pretreatment of the enzyme with NADPH and biliverdins fully protects
5,5'-dithiobis(2-nitrobenzoate)
-
-
bilirubin
-
product inhibition
bilirubin
-
inhibits the enzyme in a feedback regulation system, biliverdin inhibits the heme oxygenase activity, overview
bilirubin
-
inhibits the enzyme in a competitive manner
bilirubin
-
product inhibition
Biliverdin
-
substrate inhibition
Biliverdin
-
the enzyme is inhibited by the substrate when the concentration exceeds 0.004-0.005 mM
Biliverdin
-
substrate inhibition
iodoacetamide
-
-
iodoacetamide
-
pretreatment of the enzyme with NADPH and biliverdins fully protects
iodoacetamide
-
1 mM, slight
N-ethylmaleimide
-
-
N-ethylmaleimide
-
pretreatment of the enzyme with NADPH and biliverdins fully protects
N-ethylmaleimide
-
only one of three thiol residues can be alkylated when a ratio N-ethylmaleimide/mol enzyme SH = 90 is used, at a ratio of 300 two thiol residues are alkylated
N-ethylmaleimide
-
1.0 mM
NAD+
-
NAD+
-
product inhibition
NADP+
-
-
NADP+
-
product inhibition
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
pretreatment of the enzyme with NADPH and biliverdins fully protects
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
0.025 mM
SH-reagents
-
-
-
SH-reagents
-
e.g. 5,5'-dithiobis(2-nitrobenzoic acid), N-ethylmaleimide, pretreatment of the enzyme with NADPH and biliverdins fully protects
-
siRNA
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.001 - 0.1633
Biliverdin
0.0004 - 0.023
biliverdin IXalpha
0.001
Biliverdin
-
-
0.001 - 0.002
Biliverdin
-
cosubstrate NADH
0.0013
Biliverdin
-
enzyme has a 6-histidine-tagged amino-terminal fusion
0.0018
Biliverdin
wild type enzyme, at pH 5.8, temperature not specified in the publication
0.0019
Biliverdin
mutant enzyme S184A, at pH 5.8, temperature not specified in the publication
0.003
Biliverdin
-
cosubstrate NADPH
0.003
Biliverdin
-
cosubstrate NADPH, rat liver
0.0032
Biliverdin
-
cosubstrate NADPH, biliverdin reductase C291A
0.0033
Biliverdin
mutant enzyme R188A, at pH 5.8, temperature not specified in the publication
0.0034
Biliverdin
-
cosubstrate NADPH, biliverdin reductase wild-type
0.0034
Biliverdin
mutant enzyme T169A, at pH 5.8, temperature not specified in the publication
0.0038
Biliverdin
mutant enzyme Y98F, at pH 8.9, temperature not specified in the publication
0.004
Biliverdin
mutant enzyme Y102F, at pH 5.8, temperature not specified in the publication
0.0046
Biliverdin
wild type enzyme, at pH 8.9, temperature not specified in the publication
0.0048
Biliverdin
mutant enzyme K237A, at pH 5.8, temperature not specified in the publication
0.0049
Biliverdin
-
cosubstrate NADH, biliverdin reductase wild-type
0.005
Biliverdin
-
cosubstrate NADH
0.0051
Biliverdin
mutant enzyme R246A, at pH 5.8, temperature not specified in the publication
0.0052
Biliverdin
-
cosubstrate NADH, biliverdin reductase C291A
0.0069
Biliverdin
-
at pH 7
0.0069
Biliverdin
mutant enzyme R185A, at pH 5.8, temperature not specified in the publication
0.0097
Biliverdin
-
cosubstrate NADH, biliverdin reductase C280A
0.0102
Biliverdin
-
cosubstrate NADPH, biliverdin reductase C280A
0.0117
Biliverdin
mutant enzyme Y97F, at pH 8.9, temperature not specified in the publication
0.0126
Biliverdin
mutant enzyme R185K, at pH 5.8, temperature not specified in the publication
0.0207
Biliverdin
wild type enzyme, at pH 8.9, temperature not specified in the publication
0.0244
Biliverdin
mutant enzyme R171A, at pH 8.9, temperature not specified in the publication
0.0457
Biliverdin
mutant enzyme R171E, at pH 8.9, temperature not specified in the publication
0.0877
Biliverdin
mutant enzyme R172A, at pH 8.9, temperature not specified in the publication
0.1633
Biliverdin
mutant enzyme R171K, at pH 8.9, temperature not specified in the publication
0.0004
biliverdin IXalpha
-
cosubstrate NADPH
0.0006
biliverdin IXalpha
-
pH 7.0, 37°C, cosubstrate NADPH
0.0015
biliverdin IXalpha
-
cosubstrate NADH
0.0068
biliverdin IXalpha
-
pH 7.0, 37°C, cosubstrate NADH
0.023
biliverdin IXalpha
-
-
0.107
NADH
mutant enzyme R35S, at pH 7.2 and 30°C
0.108
NADH
mutant enzyme R35A, at pH 7.2 and 30°C
0.118
NADH
wild type enzyme, at pH 7.2 and 30°C
0.15
NADH
mutant enzyme R78A, at pH 7.2 and 30°C
0.186
NADH
mutant enzyme W116A, at pH 7.2 and 30°C
0.305
NADH
mutant enzyme R39A, at pH 7.2 and 30°C
0.319
NADH
mutant enzyme W116F, at pH 7.2 and 30°C
0.33
NADH
in the absence of urea, at pH 7.2 and 25°C
0.333
NADH
-
in the presence of 0.005 mM biliverdin, biliverdin reductase wild-type
0.394
NADH
-
in the presence of 0.005 mM biliverdin, biliverdin reductase C280A
0.567
NADH
-
in the presence of 0.005 mM biliverdin, biliverdin reductase C291A
1.5 - 2
NADH
-
pig spleen, rat liver
2
NADH
in the presence of 3 M urea, at pH 7.2 and 25°C
0.001
NADPH
in the absence of urea, at pH 7.2 and 25°C
0.0011
NADPH
mutant enzyme W116F, at pH 7.2 and 30°C
0.0016
NADPH
mutant enzyme R39A, at pH 7.2 and 30°C
0.0017
NADPH
mutant enzyme W116A, at pH 7.2 and 30°C
0.0023
NADPH
-
in the presence of 0.005 mM biliverdin, biliverdin reductase C280A
0.0024
NADPH
wild type enzyme, at pH 7.2 and 30°C
0.0029
NADPH
-
in the presence of 0.005 mM biliverdin, biliverdin reductase wild-type
0.003
NADPH
in the presence of 3 M urea, at pH 7.2 and 25°C
0.003
NADPH
mutant enzyme R174A, at pH 7.2 and 30°C
0.003 - 0.005
NADPH
-
pig spleen
0.0045
NADPH
mutant enzyme R124A, at pH 7.2 and 30°C
0.0047
NADPH
mutant enzyme R78A, at pH 7.2 and 30°C
0.0049
NADPH
mutant enzyme H132A, at pH 7.2 and 30°C
0.0058
NADPH
mutant enzyme S111L, at pH 7.2 and 25°C
0.0067
NADPH
mutant enzyme S111A, at pH 7.2 and 25°C
0.0083
NADPH
wild type enzyme, at pH 7.2 and 25°C
0.0133
NADPH
-
in the presence of 0.005 mM biliverdin, biliverdin reductase C291A
0.029
NADPH
mutant enzyme R35S, at pH 7.2 and 30°C
0.059
NADPH
mutant enzyme R35A, at pH 7.2 and 30°C
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0.7
Biliverdin
mutant enzyme R171E, at pH 8.9, temperature not specified in the publication
0.7
Biliverdin
mutant enzyme R185A, at pH 5.8, temperature not specified in the publication
0.9
Biliverdin
mutant enzyme R185K, at pH 5.8, temperature not specified in the publication
2 - 3.7
Biliverdin
mutant enzyme K237A, at pH 5.8, temperature not specified in the publication
2.7
Biliverdin
mutant enzyme Y102F, at pH 5.8, temperature not specified in the publication
6
Biliverdin
mutant enzyme R171A, at pH 8.9, temperature not specified in the publication
7.1
Biliverdin
wild type enzyme, at pH 5.8, temperature not specified in the publication
11
Biliverdin
mutant enzyme R246A, at pH 5.8, temperature not specified in the publication
11.3
Biliverdin
mutant enzyme S184A, at pH 5.8, temperature not specified in the publication
13.1
Biliverdin
mutant enzyme T169A, at pH 5.8, temperature not specified in the publication
13.4
Biliverdin
mutant enzyme R188A, at pH 5.8, temperature not specified in the publication
13.6
Biliverdin
mutant enzyme Y97F, at pH 8.9, temperature not specified in the publication
14.7
Biliverdin
mutant enzyme R171K, at pH 8.9, temperature not specified in the publication
16.8
Biliverdin
mutant enzyme Y98F, at pH 8.9, temperature not specified in the publication
17.9
Biliverdin
mutant enzyme R172A, at pH 8.9, temperature not specified in the publication
69.3
Biliverdin
wild type enzyme, at pH 8.9, temperature not specified in the publication
94.8
Biliverdin
wild type enzyme, at pH 8.9, temperature not specified in the publication
1.7
NADH
-
without Cl-
0.01
NADPH
mutant enzyme S111L, at pH 7.2 and 25°C
0.025
NADPH
mutant enzyme S111A, at pH 7.2 and 25°C
0.097
NADPH
mutant enzyme R124A, at pH 7.2 and 30°C
0.171
NADPH
wild type enzyme, at pH 7.2 and 25°C
0.237
NADPH
mutant enzyme H132A, at pH 7.2 and 30°C
0.237
NADPH
wild type enzyme, at pH 7.2 and 30°C
0.4
NADPH
mutant enzyme R174A, at pH 7.2 and 30°C
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20
Biliverdin
mutant enzyme R171E, at pH 8.9, temperature not specified in the publication
70
Biliverdin
mutant enzyme R185K, at pH 5.8, temperature not specified in the publication
100
Biliverdin
mutant enzyme R171K, at pH 8.9, temperature not specified in the publication
100
Biliverdin
mutant enzyme R185A, at pH 5.8, temperature not specified in the publication
200
Biliverdin
mutant enzyme R171A, at pH 8.9, temperature not specified in the publication
200
Biliverdin
mutant enzyme R172A, at pH 8.9, temperature not specified in the publication
700
Biliverdin
mutant enzyme Y102F, at pH 5.8, temperature not specified in the publication
1200
Biliverdin
mutant enzyme Y97F, at pH 8.9, temperature not specified in the publication
2200
Biliverdin
mutant enzyme R246A, at pH 5.8, temperature not specified in the publication
3900
Biliverdin
mutant enzyme T169A, at pH 5.8, temperature not specified in the publication
3900
Biliverdin
wild type enzyme, at pH 5.8, temperature not specified in the publication
4100
Biliverdin
mutant enzyme R188A, at pH 5.8, temperature not specified in the publication
4400
Biliverdin
mutant enzyme Y98F, at pH 8.9, temperature not specified in the publication
4600
Biliverdin
wild type enzyme, at pH 8.9, temperature not specified in the publication
4900
Biliverdin
mutant enzyme K237A, at pH 5.8, temperature not specified in the publication
5900
Biliverdin
mutant enzyme S184A, at pH 5.8, temperature not specified in the publication
15100
Biliverdin
wild type enzyme, at pH 8.9, temperature not specified in the publication
1.7
NADPH
mutant enzyme S111L, at pH 7.2 and 25°C
3.7
NADPH
mutant enzyme S111A, at pH 7.2 and 25°C
21
NADPH
wild type enzyme, at pH 7.2 and 25°C
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-
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brenda
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-
brenda
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brenda
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brenda
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brenda
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-
brenda
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brenda
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-
brenda
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brenda
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brenda
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-
brenda
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brenda
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brenda
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-
-
brenda
fusion protein Tat-biliverdin reductase A (Tat-BLVRA) is effiently transduced into HT-22 cells
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
Syncerus sp.
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brenda
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brenda
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brenda
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low activity
brenda
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-
brenda
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-
brenda
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brenda
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brenda
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-
brenda
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shows increased BVR level
brenda
-
increased activity of BVR, but only in the presence of NADH
brenda
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-
brenda
-
-
brenda
-
pulmonary arterial smooth muscle cell
brenda
-
-
brenda
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inflamed lesions, increased in rats with clinical autoimmune encephalomyelitis, also present in both white and gray matter
brenda
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-
brenda
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-
brenda
-
-
brenda
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-
brenda
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sparingly expressed
brenda
-
-
brenda
additional information
-
the BVR activity progressively increases after birth and reaches adult levels by postpartum day 28
brenda
-
-
brenda
-
protein detected in the infiltrating monocytes, macrophages, T cells and neutrophils as well as in circulating lymphocytes
brenda
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-
brenda
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-
brenda
-
brenda
-
BVR expression patterns, overview
brenda
-
brenda
-
six hours after middle cerebral artery occlusion, increased immunoreactivity for biliverdin reductase is noted in neurons in the peri-ischemic areas, intraischemic cortical layers 3 and 5, as well as in neurons in regions distant from the borders of vascular distribution of the MCA, such as those in substantia nigra, in the Purkinje layer of the cerebellum and in the central nucleus of inferior colliculus
brenda
-
cellular localization reveals age-related pattern of expression of the reductase in selected regions such as cortex, substantia nigra, hippocampus and in the cerebellum
brenda
-
immuno-chemical localization of biliverdin reductase protein in normal brain correlates well with the presence of HO-1 and HO-2 throughout the forebrain, diencephalon, cerebellum and brainstem regions
brenda
-
abundantly expressed
brenda
-
co-expression with heme oxygenases HO-1 and HO-2, BVR expression patterns, overview
brenda
-
-
brenda
-
-
brenda
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-
brenda
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mucosal epithelial cells and endothelium of intramural vessels of, all intrinsic nerve cell bodies of both submucous and myenteric plexuses
brenda
mucosal epithelial cells and endothelium of intramural vessels
brenda
-
-
brenda
-
mucosal epithelial cells and endothelium of intramural vessels of, all intrinsic nerve cell bodies of both submucous and myenteric plexuses
brenda
-
-
brenda
-
brenda
-
-
brenda
-
brenda
-
-
brenda
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-
brenda
-
-
-
brenda
-
-
brenda
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-
brenda
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-
brenda
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kidney tissue with or without renal carcinoma, the enzyme activity is nearly doubled in the tumor tissue
brenda
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-
brenda
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brenda
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-
brenda
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brenda
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immunocytochemical analysis reveals that biliverdin reductase is localised in proximal tubules of the inner cortex of the rat kidney
brenda
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abundantly expressed
brenda
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-
brenda
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-
brenda
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-
brenda
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brenda
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brenda
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brenda
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brenda
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-
brenda
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abundantly expressed
brenda
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brenda
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-
brenda
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brenda
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brenda
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lung
brenda
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increased expression in macrophages of primary spontaneous pneumothorax of smokers compared to non-smokers
brenda
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-
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-
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-
brenda
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brenda
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-
brenda
-
-
brenda
-
-
brenda
-
abundantly expressed
brenda
-
-
brenda
-
-
brenda
-
sparingly expressed
brenda
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drug target
the enzyme (BVR-A) is a potential therapeutic target to prevent brain insulin resistance in Alzheimer disease
malfunction
-
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
-
BVR is part of the heme oxygenase protection system, overview
metabolism
-
HIF-1alpha regulates the expression of BVR and other enzymes involved in oxidative stress response in lung macrophages, overview
metabolism
-
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
-
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
-
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
physiological function
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
-
blockage of BVR protein expression by retroviral siBVR inhibits the HO-2 protein induction but not vice versa
physiological function
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
BVR-A up-regulation and post-translational modifications significantly correlate with beta-secretase protein levels in the brain
physiological function
-
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
-
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
-
TNF-alpha alpha-NF-kappaB-dependent expression of Goodpasture antigen-binding protein is regulated by biliverdin reductase
physiological function
-
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
additional information
-
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
-
bilirubin is an important component of cellular defense mechanisms with cytoprotective features
additional information
-
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
-
pharmacodynamics of the heme oxygenase/biliverdin reductase system, overview
additional information
the BVR activity and expression is not affected by MAP kinase inhibitors, overview
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30400 - 31400
-
various forms, two dimensional PAGE
34600
-
1 * 39900 + 1 * 34600, in vitro translated proteins, SDS-PAGE
37000
-
x * 37000, SDS-PAGE
38000
-
the HY2 gene encodes a soluble protein precursor with a putative N-terminal plastid transit peptide, this protein is phytochromobilin synthase, a ferredoxin-dependent biliverdin reductase, SDS-PAGE
39900
-
1 * 39900 + 1 * 34600, in vitro translated proteins, SDS-PAGE
41000 - 42000
-
the purified protein resolves into two molecular weight forms of 40700 and 39600, two-dimensional electrophoresis
54000
-
liver (form 2), HPLC
56000
-
minor form 2, SDS-PAGE
60000
-
expression of rat biliverdin reductase as a gluthatione-S-transferase protein, SDS-PAGE
69000
-
in vitro translated reductase, 12% native polyacryamide gel
21000
BVRB, SDS-PAGE
32000
-
gel filtration
32000
-
kidney, gel filtration
33000
-
SDS-PAGE
33000
-
x * 33000, SDS-PAGE
33000
x * 33000, SDS-PAGE
33500
BVRA, SDS-PAGE
34000
-
-
34000
-
major form 1, SDS-PAGE
34000
-
form 1 in liver, kidney and spleen, SDS-PAGE
34000
-
form 1 in liver, kidney and spleen, SDS-PAGE
34000
-
converted to a larger 68000 Da form when rats are treated with SH-reactive agents
34000
-
x * 34000, SDS-PAGE
34000
-
1 * 34000, multiple forms, SDS-PAGE
34000
-
2 * 34000, liver (form I), minor dimeric form, SDS-PAGE
36000
-
-
46000
-
form 2 in liver, SDS-PAGE
46000
-
form 2 in liver, SDS-PAGE
46000
-
liver (form 2), SDS-PAGE
68000
-
-
68000
-
major form 1 from liver is converted into a second major form by a NAD+ -dependent peroximal dehydrogenase, SDS-PAGE
68000
-
liver (form 3), HPLC
68000
-
x * 68000, SDS-PAGE
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apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50 mM Tris-HCl (pH 7.25), 0.2 M sodium acetate and 0.2 mM Cymal-2
hanging drop vapor diffusion method, using 27% (w/v) PEG 3350, 0.2M MgCl2 and 0.1 M BisTris at pH 5.5
-
apo enzyme and in complex with NADH
apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2
BVR-NADH complex, NH2-terminal domain in dinucleotide binding
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crystals of the biliverdin reductase obtained by sitting-drop vapour-diffusion method, enzyme diffraction data collected to 1.6 A, crystals belong to the orthorhombic space group P212121 with unit-cell parameters a=58.89, b=70.41, c=87.76 A
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an X-ray diffraction experiment using a native BVR crystal is performed on the BL38B1 beamline. The crystal belongs to the orthorhombic space group P2-1-2-1-2-1, with unit-cell parameters a = 58.8, b = 88.4, c = 132.6 A. A complete data set is collected to a resolution of 2.34 A
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apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2
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H132A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R124A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R172A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R174A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
R35A
the mutant exhibits a strongly increased Km value for NADPH compared to the wild type enzyme
R35S
the mutant exhibits a strongly increased Km value for NADPH compared to the wild type enzyme
R39A
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
R78A
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme
S111A
the mutant shows strongly reduced activity compared to the wild type enzyme
S111L
the mutant shows strongly reduced activity compared to the wild type enzyme
V11A/V12A/V13A/V14A
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not only fails to activate protein kinase C but also decreases its activity by 22%
W116A
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
W116F
the mutant exhibits a reduced Km value for NADPH compared to the wild type enzyme
Y198F
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mutant, phosphorylation site
Y98F
the mutant shows about wild type catalytic efficiency
E47A
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mutant, does affect the edge of the beta2 strand of substrate and cofactor binding in the pocket, which likely influences the strength of their interaction with BVR
E97A
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mutant, data strongly support this site as important for conversion of biliverdin to bilirubin and for transmission of signaling by BVR
C280A
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although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 280 principally functions in substrate binding
C291A
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although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 291 is predominantly involved in cofactor binding.
C73A
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the modification of the amino-proximal cysteine, which is flanked by a tyrosine residue, completely inactivates the enzyme with NADH at pH 6.75 and NADPH at pH 8.7
R171A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171E
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y98F
the mutant shows about wild type catalytic efficiency
K237A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R185A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R185K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R188A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
R246A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
S184A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T169A
the mutant shows wild type catalytic efficiency
Y102F
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
C281A/C292A/C293A
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mutant is defective for protein-protein-dependent interaction and haematin binding
C281A/C292A/C293A
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C-terminal fragment 272-296 in which cysteine residues are replaced by alanine do not interact with Goodpasture antigen-binding protein whereas wild-type C-terminal fragment 276-296 does
G17A
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does not effectively bind ATP, hence kinase-dead, is not as effective as the wild-type in potentiating protein kinase C activity
G17A
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mutant is defective for ATP binding
R18Stop
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heterozygous nonsense mutation predicted to truncate the protein N-terminally to the active site tyrosine 97, discovered in nucleotide 52 of exon I of the DNA isolated from a hyperbiliverdinaemic patient
R18Stop
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a naturally occuring mutation of BVR leading to a severely truncated enzyme, liver cirrhosis and death
Y97F
50% of activity compared to wild type
Y97F
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
additional information
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cells transfected with small interfering RNA directed to enzyme gene display a fourfold increase in apoptotic cells when treated with 0.01 mM sodium arsenite
additional information
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point mutation of residues that in BVR interact with the adenine nucleotide, all inactivate the enzyme, S149 essential for acitvity
additional information
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point mutations of serine residues in the kinase domain of the enzyme inhibits phosphotransferase activity
additional information
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inhibition of isoproterenol-induced expression of BVR using siBVR
additional information
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since no specific inhibitors for BVR are known, siRNA is used to silence the BVR gene in primary endothelial cells and accordingly suppress its activity
additional information
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expression of enzyme in Nicotiana tabacum, expression in dark-grown plants leads to reduced accumulation of protochlorophyllide and transcripts for the two committed enzymes for 5-aminolevulinic acid synthesis, enzyme dependent inhibition of chlorophyll biosynthesis in light-grown plants depends mainly on misregulated tetrapyrrole metabolism
additional information
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changing C73 to alanine inactivates the enzyme, as it is involved in substrate/cofactor binding
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biliverdin reductase cDNA cloned into pUC18, used for expression and purification
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expressed in Escherichia coli
expressed in Escherichia coli and HeLa cells
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expressed in Escherichia coli BL-21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)-RIL cells
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expressed in Escherichia coli C41(DE3) cells
expressed in HEK-293 cells
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expressed in HEK293A and MCF-7 cells
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expression in H9C2 cell
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expression in HEK-293A cells
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expression in SH-SY5Y cells
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human biliverdin reductase expressed in Escherichia coli
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into pcDNA3 and expressed in 293A cells pcDNA3, into pGEX4-T2 and expressed in Escherichia coli
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into the pGEM-T easy vector, subcloned into the vectors pcDNA3 and pESC-LEU
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into vector pcDNA3, transformed into Escherichia coli DH5alpha, pGEX-4T2/human BVR vector
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kidney form of the enzyme cloned into the expression vector pGEX-KG
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overexpressed in Escherichia coli as a His-tagged fusion protein
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recombinant biliverdin reductase expressed in Escherichia coli
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recombinant BVR is used
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reversible overexpression of BVR in mouse fibroblasts, doxycycline-dependent overexpression of BVR in NIH 3T3 BVR-Tet-On cells confers protection against cytotoxic drugs cisplatin and doxorubicin
the expression of rat kidney biliverdin reductase is targeted by translational fusion of the chloroplast transit peptide sequence of the soybean small subunit of ribulose bisphosphate carboxylase gene to the enzyme cDNA, with this method transgenic Arabidopsis plants are cloned which express constitutive biliverdin reductase and display aberrant photomorphogenesis throughout their life-cycle
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using the vector pBIB-KAN a plant transformation vector, containing the CAB3 promoter, a chloroplast targeting sequence and the BVR gene, is constructed, using pMON672 leads to a similar construct containing the MERI5 promoter
expressed in Escherichia coli
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expressed in Escherichia coli
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
into the vector pcDNA3.1
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into the vector pcDNA3.1
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about 56% of the BVR expression in total lung tissue is increased by hypoxia
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atorvastatin significantly increases BVR-A protein levels, phosphorylation and activity only in parietal cortex
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bacterial endotoxin, lipopolysaccharide, initiates an inflammatory response in macrophages coming along with a rapid increase in BVR surface expression
BVR expression is unaffected by heat shock
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BVR is induced by lipopolysaccharides and bromobenzene at a post-transcriptional level
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doxycycline dose-dependently induces BVR gene expression at the level of mRNA as well as a protein, and BVR activity in genetically modified NIH 3T3 fibroblasts
enzyme expression is up-regulated in breast cancer cells
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expression is up-regulated in breast, lung, and liver cancers, but not ovarian cancer
hypoxia positively regulates hBVR promoter
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in fetal liver and maternal liver and placenta ursodeoxycholic acid up-regulates biliverdin-IX reductase
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in HEK-293A cells, hypoxia modestly increases BVR mRNA levels
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in HepG2 and JAr cells taurocholic acid and ursodeoxycholic acid up-regulate biliverdin-IX reductase
increased expression in macrophages of primary spontaneous pneumothorax of smokers compared to non-smokers
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increased levels of heme oxygenase-1 and biliverdin reductase protein in the choroid plexus over the entire period following subarachnoid hemorrhage induction
induction of BVR and HO-2 is mediated by the cAMP-PKA pathway and isoproterenol, overview
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induction of BVR and HO-2 is mediated by the cAMP-PKA pathway and isoproterenol, overview. The beta-adrenergic antagonist propranolol only slightly induces BVR expression in HEK-293A cells
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overexpression of IkappaB increases hBVR mRNA
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oxidative stress induces HO-1, BVR and H-ferritin in lung macrophages, this is involved in development of primary spontaneous pneumothorax disease, overview. HIF-1alpha siRNA transfection completely abrogated the increased HO-1, BVR and H-ferritin mRNA levels
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patients with chronic hepatitis C virus infection show significantly upregulated enzyme expression in peripheral blood leukocytes
the transcript and protein levels are increased in human tumors and the infiltrating T-cells, monocytes and circulating lymphocytes, as well as the circulating and infiltrating macrophages
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TNF-alpha negatively regulates hBVR promoter
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treatment of cultured TALH or IMCD-3 cells with BVR siRNA, 50 or 100 nM, results in an 80% decrease in the level of BVR protein
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up-regulated in levels of protein and mRNA by hypoxia in pulmonary arterial smooth muscle cell
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up-regulation is found in the hippocampus of subjects with Alzheimer disease in its earliest form
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bacterial endotoxin, lipopolysaccharide, initiates an inflammatory response in macrophages coming along with a rapid increase in BVR surface expression
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bacterial endotoxin, lipopolysaccharide, initiates an inflammatory response in macrophages coming along with a rapid increase in BVR surface expression
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diagnostics
antiapoptotic effect of the enzyme in cancers portens strategies for developing novel biomarkers and effective treatment ways for cancer patients
diagnostics
peripheral biomarker for the early diagnosis of Alzheimer's disease
medicine
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BVR may represent a novel strategy for the treatment of multiple sclerosis and other oxidative stress-mediated diseases, treatment with BVR ameliorates both clinical and pathological signs of autoimmune encephalomyelitis more efficiently than treatments with traditional antioxidant enzymes
medicine
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data gathered to date have identified the potential utility of hBVR in modulating cell signaling and the wide range of functions that are regulated by protein kinases that include growth, differentiation, gene transcription and metabolism, regulation of glucose uptake, induction of HO-1, and cytokine and Toll-like receptor signaling are potential target candidates for hBVR-based therapeutic strategies
medicine
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hyperbiliverdinaemia, green jaundice, with green plasma and urine may be caused by a genetic defect in the BVR-A gene in conjunction with decompensated liver cirrosis
medicine
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finding that BVR and HO-2 levels, myocyte apoptosis, and contractile function of the heart can be modulated by small human BVR-based peptides offers a promising therapeutic approach for treatment of cardiac dysfunctions
medicine
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therapeutic potential of human BVR and human HVR-based peptides by affecting the MAPK signaling pathways, overview
medicine
biliverdin reductase B is a prostate cancer marker
medicine
Tat-mediated transduction of biliverdin reductase A may provide a potential tool to ameliorate beta-cell deficit in pancreas with type 2 diabetes mellitus
pharmacology
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)
pharmacology
transduced fusion protein Tat-biliverdin reductase A (Tat-BLVRA) markedly inhibits cell death, DNA fragmentation, and generation of ROS. Transduced Tat-BLVRA inhibits the apoptosis and mitogen activated protein kinase (MAPK) signaling pathway and it passes through the blood-brain barrier (BBB) and significantly prevents hippocampal cell death in an ischemic model. Tat-BLVRA provides a possibility as a therapeutic molecule for ischemia
additional information
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BVR regualtes cellular levels of biliverdin, a potent gene regulator and determinant factor for dorsal axis development in Xenopus larva
additional information
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interacts with the insulin receptor kinase domain, key factor in the MAPK pathway and the PI3K pathway as well as regulating PKC isoforms that link the two pathways, plays a role in the mechanism of insulin resistance
additional information
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potential function in propagation of signals relayed through protein kinase C, binds to protein kinase C betaII, increases its phosphorylation, and is a substrate for the kinase, increases PMA-dependent c-fos activation and protein kinase C translocation to the membrane
additional information
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potential role in the insulin signaling pathway, BVR is both a substrate for insulin receptor tyrosine kinase activity and a kinase for serine phosphorylation of insulin receptor substrate 1
additional information
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regulates oxidative response and HO-1 expression