1.14.14.18: heme oxygenase (biliverdin-producing)
This is an abbreviated version!
For detailed information about heme oxygenase (biliverdin-producing), go to the full flat file.
Word Map on EC 1.14.14.18
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1.14.14.18
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monoxide
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cytoprotective
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endothelial
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necrosis
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dismutase
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protoporphyrin
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erythroid
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2-related
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tnf
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bilirubin
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artery
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malondialdehyde
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lipopolysaccharide
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catalase
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hemin
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neuroprotective
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ischemia
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gsh
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lps
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sod
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anti-oxidant
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mapks
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sirna
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caspase-3
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quinone
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pulmonary
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reperfusion
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lps-induced
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hypoxia
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cyclooxygenase-2
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cox-2
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ferritin
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erk
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nf-e2-related
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anti-apoptotic
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cobalt
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myeloperoxidase
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ischemia-reperfusion
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nrf2-mediated
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pro-oxidant
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kelch-like
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nadph:quinone
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factor-2
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lps-stimulated
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2-like
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erythroid-derived
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oxygenases
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delta-aminolevulinic
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sulforaphane
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hyperbilirubinemia
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medicine
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drug development
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analysis
- 1.14.14.18
- monoxide
-
cytoprotective
- endothelial
- necrosis
- dismutase
- protoporphyrin
-
erythroid
-
2-related
- tnf
- bilirubin
- artery
- malondialdehyde
- lipopolysaccharide
- catalase
- hemin
-
neuroprotective
- ischemia
- gsh
- lps
- sod
-
anti-oxidant
- mapks
- sirna
- caspase-3
- quinone
- pulmonary
-
reperfusion
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lps-induced
- hypoxia
- cyclooxygenase-2
- cox-2
- ferritin
- erk
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nf-e2-related
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anti-apoptotic
- cobalt
- myeloperoxidase
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ischemia-reperfusion
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nrf2-mediated
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pro-oxidant
-
kelch-like
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nadph:quinone
-
factor-2
-
lps-stimulated
-
2-like
-
erythroid-derived
- oxygenases
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delta-aminolevulinic
- sulforaphane
- hyperbilirubinemia
- medicine
- drug development
- analysis
Reaction
Synonyms
biliverdin-producing heme oxygenase, ChuS, ChuZ, EC 1.14.99.3, haem oxygenase, heme oxygenase, heme oxygenase 1, heme oxygenase 2, heme oxygenase-1, heme oxygenase-2, HemO, Hmox1, Hmox1a, Hmox1b, Hmox2, Hmox2a, Hmox2b, HmuO, Hmx1, HO, HO-1, HO-2, Ho1, Ho2, Ho3, HO4, HSP32, HugZ, HY1, inducible heme oxygenase-1, More, MsHO1, ORP33 proteins, oxygenase, heme (decyclizing), pbsA1, PigA, proteins, specific or class, ORP33 (oxygen-regulated protein 33,000-mol.-wt.), Syn HO-1, Syn HO-2
ECTree
1.14.14.18 heme oxygenase (biliverdin-producing)Advanced search results
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results (Engineering
Engineering on EC 1.14.14.18 - heme oxygenase (biliverdin-producing)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D136A
reduced heme degradation activity, formation of ferryl heme
D136F
reduced heme degradation activity, formation of ferryl heme
H20A
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capable of NADPH dependent hydroxylation of heme to alpha-mesohydroxyheme in contrast to human H25A heme oxygenase-1 mutant, ability to catalyze the conversion of verdoheme to biliverdin is rescued by imidazole titration
H245A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H245Q
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R166A
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site-directed mutagenesis, the mutation completely abolished the HO activity of HugZ
C127A
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site-directed mutagenesis of the truncated HO-2 variant lacking the membrane spanning domain, spectral properties in comparison to the wild-type HO-2, overview
C127A/C282A
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site-directed mutagenesis of the truncated HO-2 variant lacking the membrane spanning domain, spectral properties in comparison to the wild-type HO-2, overview
D140A
G143H
the replacement of Gly143 with His leads to the formation of a bis-histidine complex
H25A
R183E
R254K
F157A
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mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
F157I
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mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
F157A
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
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mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
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F157I
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
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mutant is unable to carry out the complete degradation of heme to biliverdin, the reaction is arrested at the verdoheme stage. The protein displays bands at 357, 525 and 678 nm, reminiscent of the absorption spectrum reported for the HO-verdoheme complex. Overexpression of the HO F157 variants causes the Escherichia coli cells to turn dark green color
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H26A/K34A/K132A
mutant does not interact with holo-PhuS and shows no enzymatic activity
N19K/K34A/F117Y/K132A
change in regioselectivity, product is biliverdin IXalpha
H25A
site-directed mutagenesis, the mutant is translocated to the nucleus losing its C-terminus
L213I
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increases the distance between the phenyl ring of inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride and the residue from 3.6 to 4.4 A
M34V
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increases the distance to the phenyl group in the northeastern region of inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride
R183a
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same alpha-regioselectivity as wild-type, only alpha-biliverdin is produced
R183D
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in contrast to wild-type heme oxygenase-1 which converts heme exclusively to alpha-biliverdin, the R183D mutant converts heme to 20% delta-biliverdin in addition to alpha-biliverdin
R183E
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in contrast to wild-type heme oxygenase-1 which converts heme exclusively to alpha-biliverdin, the R183E mutant converts heme to 35% delta-biliverdin and small amounts of beta and gamma-biliverdin in addition to alpha-biliverdin
R183N
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same alpha-regioselectivity as wild-type, only alpha-biliverdin is produced
R183Q
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same alpha-regioselectivity as wild-type, only alpha-biliverdin is produced
S53A
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distance from the Ser53 of HO-1 to inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride will be similar if substituted with Ala (4.5 A), the hydroxyl group of Ser53 in the HO-1 model will be close enough to be within van der Waals contact of the inhibitor if it is rotated toward the hydrophobic pocket
V50A
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increases the distance between residue and inhibitor (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[(phenylsulfanyl)methyl]-1,3-dioxolane hydrochloride by ca. 0.8 A
H17F
very poor or no activity in live-cell assay, presence of heme, no binding of biliverdin observed
H17K
mutant retains activity in live-cell assay, and binds biliverdin
H17R
mutant retains activity in live-cell assay, and binds biliverdin. No activity in vitro
additional information
D140A
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abolished activity, retains the unusual wild-type azide complex spin/orbital ground state
D140A
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exhibits resolved and relaxed 2,4-dimethyldeuterohemin resonances at low pH and at high pH
H25A
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about 10% of wild-type activity, binding activity to heme similar to wild-type
H25A
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mutation leads to an empty pocket underneath the ferric ion in the heme, leading to loss of binding iron ligand. Enzymatic activity is reduced by 90.5%. By supplementing imidazole, the HO-1 activity is restored approximately 87.5% to its normal level
R183E
in addition to product biliverdin IXalpha, mutant yields biliverdin IXdelta and traces of biliverdin IXbeta. Crystal structure reveals altered active site hydrogen bonding network
R254K
site-directed mutagenesis, the exchange eliminates a thrombin cleavage site in the full-length enzyme, the mutant enzyme shows similar activity compared to the wild-type enzyme
R254K
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enhances protein stability during the glutathione S-transferase-tag removal procedure involving the protease thrombin
additional information
de novo synthesis of the heme proteins on a membrane-coupled template, and screening for heme proteins with heme oxygenase activity, overview
additional information
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de novo synthesis of the heme proteins on a membrane-coupled template, and screening for heme proteins with heme oxygenase activity, overview
additional information
a clinically relevant polymorphism within the HO-1 promoter critically influences its transcriptional activation by both PPAR isoforms, overview
additional information
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a clinically relevant polymorphism within the HO-1 promoter critically influences its transcriptional activation by both PPAR isoforms, overview
additional information
construction of apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region
additional information
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construction of apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
enzyme downregulation by expression of HO-1 siRNA in WM451Lu cells, reverses the upregulating effect of 5-aminolevulinic acid, oerview
additional information
enzyme suppression with siRNA abolishes the cytoprotective effect of HO-1
additional information
high-loading nanosized micelles of copoly(styrene-maleic acid)-zinc protoporphyrin with an average molecular size of 144 kDa for targeted delivery of a potent heme oxygenase inhibitor, method development, overview
additional information
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high-loading nanosized micelles of copoly(styrene-maleic acid)-zinc protoporphyrin with an average molecular size of 144 kDa for targeted delivery of a potent heme oxygenase inhibitor, method development, overview
additional information
HO-1 expression is enhanced in BI-1 transfected cells compared to untransfected cells, phenotype, overview
additional information
protective effect by iron chelation in HO1-deficient fibroblasts
additional information
a variant of ascorbate peroxidase, W41A, which reacts slowly with tert-butyl hydroperoxide does not form the usual peroxidase compound I intermediate, but instead forms a product in which the heme is cleaved at the alpha-meso position, analogous to the heme oxygenase mechanism
additional information
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adenovirus-mediated HO-1 transduction of Rattus norvegicus primary cardiomyocytes and H9C2 myocytes results in significant induction of VEGF expression, overview
additional information
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construction of a truncated HO-2 variant lacking the membrane spanning domain, spectral properties in comparison to the wild-type HO-2, overview
additional information
a variant of Hmox1 lacking the C-terminal heme regulatory domain exhibits the same specific activity as one containing both the catalytic core and heme regulatory domain. A truncated variant containing only the heme regulatory region binds but cannot oxidize heme
additional information
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a variant of Hmox1 lacking the C-terminal heme regulatory domain exhibits the same specific activity as one containing both the catalytic core and heme regulatory domain. A truncated variant containing only the heme regulatory region binds but cannot oxidize heme
additional information
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a C26S variant lacking the last 20 C-terminal residues incorporates the prosthetic group efficiently and is active
additional information
Leptospira interrogans serovar Icterohaemorrhagiae serovar Lai 56601
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a C26S variant lacking the last 20 C-terminal residues incorporates the prosthetic group efficiently and is active
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additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-1, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
construction of deletion and/or disruption mutants of HO-2, phenotypes, overview
additional information
HO-1 expression is reduced in toll-like receptor 2 TLR2-knockout mice after stab-wound injury, overview
additional information
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HO-1 expression is reduced in toll-like receptor 2 TLR2-knockout mice after stab-wound injury, overview
additional information
inhibition of HO-1 expression by small interfering RNA decreases cellular survival and apoptosis in the mouse hepatoma cell lines Hepa129 and Hepa1-6, and orthotopic tumor growth in immune-competent C3H/HeN mice, mechanism. But application of siHO1 does not induce liver or kidney damage in mice, overview
additional information
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inhibition of HO-1 expression by small interfering RNA decreases cellular survival and apoptosis in the mouse hepatoma cell lines Hepa129 and Hepa1-6, and orthotopic tumor growth in immune-competent C3H/HeN mice, mechanism. But application of siHO1 does not induce liver or kidney damage in mice, overview
additional information
knock-down of HO-1 expression by siRNA expression, overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
additional information
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knock-down of HO-1 expression by siRNA expression, overexpression of HO-1 in B16F10 cells confers resistance to cisplatin treatment, overview
additional information
RNA interference with HO-1 siRNA reduces the expression of HO-1 transcripts and protein as well as oxygen radical production
additional information
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inhibition of HO-1 expression by small interfering RNA decreases cellular survival and apoptosis in the mouse hepatoma cell lines Hepa129 and Hepa1-6, and orthotopic tumor growth in immune-competent C3H/HeN mice, mechanism. But application of siHO1 does not induce liver or kidney damage in mice, overview
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additional information
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HO-1 expression is reduced in toll-like receptor 2 TLR2-knockout mice after stab-wound injury, overview
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additional information
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C-terminal truncation of the enzyme, e.g. by sequential deletion of three residues, His207, Arg208, His209. Deleting His209 minimally perturbs the interaction of the C-terminus, but deletion of Arg208 completely abolishes it
additional information
HO-1 overexpression activates an oxidant-responsive HO-1 promoter
additional information
HO-1-specific siRNA significantly reduces hemin and cadmium chloride-mediated HO-1 induction, cobstruction of HO-1 deletion mutants showing decreased enzyme activity
additional information
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rat HO-1 cDNA transfected RBL-2H3 cells show altered cytokine production in response to stimulation with anti-ovalbumin OA serum/OA compared to Mock transfected RBL-2H3 cells. HO-1 inhibits anti-OA serum/OA-induced IL-3 and TNF-alpha production. Inhibition of HO-1 activity by Zn (II) protoporphyrin IX, a specific HO-1 inhibitor, prevents the suppression of TNF-alpha production. The cytokine inhibition by HO-1 is associated with selective suppression of the DNA-binding activity of AP-1 transcription factors, phenotype, overview
additional information
rat HO-1 cDNA transfected RBL-2H3 cells show altered cytokine production in response to stimulation with anti-ovalbumin OA serum/OA compared to Mock transfected RBL-2H3 cells. HO-1 inhibits anti-OA serum/OA-induced IL-3 and TNF-alpha production. Inhibition of HO-1 activity by Zn (II) protoporphyrin IX, a specific HO-1 inhibitor, prevents the suppression of TNF-alpha production. The cytokine inhibition by HO-1 is associated with selective suppression of the DNA-binding activity of AP-1 transcription factors, phenotype, overview
additional information
RNA interference with HO-1 siRNA reduces the expression of HO-1 transcripts and protein as well as oxygen radical production
