◀ Back to EPHB2
EPHB2 — NFKBIA
Text-mined interactions from Literome
Savkovic et al., Am J Physiol Gastrointest Liver Physiol 2001
(Inflammation...) :
ERK1/2 inhibitors
attenuated IkappaBalpha degradation and IL-8 expression
Jiang et al., J Biol Chem 2004
:
Inhibition of
ERK did not
affect interleukin-1beta induced
I-kappaBalpha phosphorylation and degradation but attenuated I-kappaBbeta degradation
Yeh et al., J Biol Chem 2004
:
However, results of immunoblotting analysis showed that neither cisplatin nor
MEK/ERK inhibitors
induced marked
IkappaBalpha degradation, suggesting that suppression of the MEK/ERK signaling pathway may enhance cisplatin induced NF-kappaB activation via mechanisms other than the conventional pathway
Matsubara et al., Biochem Pharmacol 2005
(MAP Kinase Signaling System) :
PD98059, a MEK inhibitor, and BAY 11-8702, an
I kappa B-alpha inhibitor,
reduced ERK and NF-kappa B cascade activation, respectively, with little effect on PKC phosphorylation
Lubin et al., Neuroscience 2005
:
Interestingly, inhibition of
ERK but not PI3K
blocked the kainate mediated increase in
phospho-IkappaBalpha
Maeng et al., Cell Signal 2006
:
Consistently, inhibition of
ERK significantly
increased IkappaB kinase (IKK) activity,
IkappaBalpha phosphorylation, and nuclear translocation of NF-kappaB induced by VEGF, whereas overexpression of ERK resulted in the loss of these responses to VEGF
Singleton et al., Shock 2005
(MAP Kinase Signaling System...) :
GLN given 1 h postsepsis led to inhibition of lung tissue NF-kappaB activation ( P < 0.001 vs. SP ), attenuated degradation of
IKBalpha , and
inhibited phosphorylation of p38 MAPK, and
ERK , pathways critical for cytokine release
Ha et al., J Immunol 2007
:
Moreover, IkappaB kinase (IKK) alpha and IKKbeta are distinctly involved in MUC5AC induction via an
ERK1 dependent , but
IkappaBalpha-p65- and p100-p52 independent, mechanism, thereby revealing novel roles for IKKs in mediating up-regulation of MUC5AC mucin by S. pneumoniae
Kanayama et al., J Endotoxin Res 2007
:
Here, we show that bikunin : ( i ) blocks LPS induced secretion of pro-inflammatory cytokines, including TNF-alpha and IL-1beta, in a dose dependent manner ; ( ii ) has an inhibitory effect on cytokine production at a concentration of 0.2 microM, reaching 65 % inhibition at the highest doses of bikunin tested ( 5 microM ) ; ( iii ) has the suppressive capacity of
ERK1/2 and p38 signaling pathways ; and ( iv )
inhibited sequentially the LPS induced phosphorylation of
IkappaB-alpha , degradation of IkappaB-alpha, and nuclear translocation of NF-kappaB
Adhikary et al., J Leukoc Biol 2008
(Corneal Diseases...) :
We found that S. aureus and Pam3Cys stimulate phosphorylation of JNK, p38 MAPK, and ERK within 4 h and that blockade of JNK, but not p38 or
ERK phosphorylation,
had an inhibitory effect on
IkBalpha degradation and CXC chemokine production
Thanislass et al., Vet Res Commun 2009
:
Activation of
ERK resulted in phosphorylation of
IkappaB-alpha which lead to its degradation which in turn followed by nuclear translocation of NF-kappaB, which is also supported by the western blot analysis
Min et al., Int Immunopharmacol 2009
:
5-Hydroxyzerumbone, however, did not affect the degradation of
IkappaB-alpha and the
activation of p38 and
ERK in LPS treated cells
Siggs et al., Proc Natl Acad Sci U S A 2010
(Immunologic Deficiency Syndromes) :
Degradation of
IkappaB alpha , which is considered a primary requirement for NEMO mediated immune signaling, occurred normally in response to Toll-like receptor stimulation, yet
ERK phosphorylation and NF-kappaB p65 nuclear translocation were severely
impaired
Chen et al., TheScientificWorldJournal 2010
:
Blocking phosphorylation of
ERK1/2 by MAPK inhibitors U0126 and PD98059, and
inhibiting activation of NF-?B by
IkappaB ( I?B ) kinase inhibitors wedelolactone or IMD-0354, abolished the DSP effects
Sonoda et al., J Biol Chem 1997
:
Since OA-activated Erk1 phosphorylated recombinant IkappaB-alpha in vitro, we assumed that
Erk1 is
involved in the phosphorylation and subsequent degradation of
IkappaB-alpha , thus leading to the activation of IL-8 gene transcription
Lee et al., Proc Natl Acad Sci U S A 1998
:
We have previously shown that mitogen activated protein
kinase/ERK kinase kinase 1 ( MEKK1 ) can
induce both this site-specific phosphorylation of IkappaB alpha at Ser-32 and Ser-36 in vivo and the activity of a high molecular weight
IkappaB kinase complex in vitro