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CYBA — NOX3
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
STRING interaction:
NOX3
—
CYBA
(interaction, mapped from reactome kegg_pathways)
-
STRING interaction:
CYBA
—
NOX3
(interaction, mapped from reactome kegg_pathways)
Text-mined interactions from Literome
Huang et al., J Biol Chem 1999
:
Activation of phagocyte
NADPH oxidase requires interaction between p47(phox) and
p22(phox)
Xiao et al., Am J Physiol Cell Physiol 2002
(Cardiomegaly...) :
We found that ARVM express gp91(phox),
p22(phox) , p67(phox), and p47(phox), four major components of NAD ( P ) H oxidase, and that alpha ( 1 ) -AR stimulated ERK1/2 activation was
blocked by four structurally unrelated inhibitors of
NAD ( P ) H oxidase [ diphenyleneiodonium, phenylarsine oxide, 4- ( 2-aminoethyl ) benzenesulfonyl fluoride, and cadmium ]
San José et al., Hypertension 2004
(Hypertension) :
We thus investigated the relationships between the -930A/G polymorphism and
p22phox expression and
NADPH oxidase mediated superoxide production in phagocytic cells from 70 patients with essential hypertension and 70 normotensive controls
Kawahara et al., J Biol Chem 2005
:
Similarly,
p22phox ( P156Q ), a mutation that disrupts Src homology 3 binding by the PRR, potently
inhibited reactive oxygen production from Nox1 and
Nox2 but not from Nox4 and Nox5 ... Expression of
p22phox ( P156Q )
inhibited NOXO1 stimulated
Nox3 activity, but co-expression of NOXA1 overcame the inhibitory effect
Modlinger et al., Hypertension 2006
(Hypertension) :
An increase in
p22phox is
required for increased renal NADPH oxidase activity, expression of
Nox proteins and oxidative stress, and contributes < or =50 % to hypertension during an Ang II slow-pressor response
Nobuhisa et al., Biochem J 2006
:
Activation of the superoxide producing phagocyte
NADPH oxidase , crucial for host defence,
requires an SH3 ( Src homology 3 ) -domain mediated interaction of the regulatory protein p47phox with
p22phox , a subunit of the oxidase catalytic core flavocytochrome b558
Kawahara et al., BMC evolutionary biology 2007
:
NOXO1 and
p22phox also
regulate Nox3 , whereas Nox4 requires only p22phox
Haurani et al., Hypertension 2008
:
Cotransfection with human Nox4 and human
p22-phox plasmids combined with Ang II
reduced endogenous Nox4 mRNA levels ( 37+/-5 % of control ; P < 0.05 ), whereas it had no significant effect on Nox1 or
Nox2
Tian et al., Am J Physiol Regul Integr Comp Physiol 2008
(Disease Models, Animal...) :
By day 35 in the high-Na S rats, mRNA expression of renal cortical gp91phox,
p22phox , p47phox, and p67phox NADPH subunits in S rats increased markedly, and treatment of high-Na S rats with the NADPH oxidase inhibitor apocynin
resulted in significant decreases in mRNA expression of these
NADPH oxidase subunits
Lewis et al., J Biol Chem 2010
:
Phosphorylation of
p22phox on threonine 147
enhances NADPH oxidase activity by promoting p47phox binding ... We also explored the mechanism by which
p22(phox) phosphorylation
affects NADPH oxidase activity
Sardina et al., Cell Death Differ 2010
:
p22phox dependent
NADPH oxidase activity is required for megakaryocytic differentiation ... RNA interference experiments have shown that a
p22(phox) dependent
NADPH oxidase activity is responsible for ROS production
Edderkaoui et al., J Biol Chem 2011
(Pancreatic Neoplasms) :
Up-regulation of
p22(phox) by the growth factors
results in increased Nox4-p22(phox) complex formation and activation of
NADPH oxidase
Zhao et al., Chin Med J (Engl) 2013
:
AcorA significantly
inhibited high glucose induced activation of
NADPH oxidase , a ROS generating enzyme, by increasing phosphorylation of p47(phox) and enhancing interaction between
p22(phox) and p47(phox)
Sumimoto et al., J Biol Chem 1996
:
Specific interaction of the N-terminal Src homology 3 domain of p47phox with
p22phox is
required for activation of the
NADPH oxidase
Marshall et al., Am J Respir Cell Mol Biol 1996
(Anoxia) :
Together these observations demonstrate that the unique
cytochrome b-245 containing NADPH-oxidase is present in pulmonary artery smooth muscle and that an
NADPH-oxidase or NADH-oxidoreductase complex is
activated to release superoxide by hypoxic conditions