ライフサイエンスコーパス: MKP

1 MKP-1 also provided neuroprotection in vivo in a lentivi

2 MKP-1 coordinates both myoblast proliferation and differ

3 MKP-1 deficiency in monocytes and macrophages promotes a

4 MKP-1 is a potential target for modulating regional effe

5 MKP-1 overexpression is also observed with unpredictable

6 MKP-1 serves as a master-regulator of macrophage phenoty

7 MKP-1 was regulated by innate recognition signals and it

8 MKP-1(-/-) mice experienced amplified injury.

9 MKP-1(-/-) or wild-type mice were ventilated with very h

10 MKP-5 controlled JNK to coordinate muscle stem cell prol

11 d to induction of MAP-kinase phosphatase -1 (MKP-1) and dephosphorylation of ERK1/2 in the mammospher

12 ological contribution of MAPK phosphatase 1 (MKP-1) as a nuclear antagonist of both p38 MAPK and JNK

13 ogen-activated protein kinase phosphatase 1 (MKP-1) in blood monocytes, and hematopoietic MKP-1-defic

14 ERK1/2, stabilization of MAPK phosphatase 1 (MKP-1), and induction of TNF-alpha with concomitant down

15 ogen-activated protein kinase phosphatase 1 (MKP-1)-dependent dephosphorylation of p38 MAPK.

16 ogen-activated protein kinase phosphatase 1 (MKP-1).

17 e considered the role of MAPK phosphatase 1 (MKP-1/DUSP1), which catalyzes dephosphorylation and inac

18 otein kinase/dual-specificity phosphatase 1 (MKP-1/DUSP1).

19 ogen-activated protein kinase phosphatase-1 (MKP-1) and enhanced GC inhibition of LPS-induced IL-6.

20 eased phosphorylation of MAPK phosphatase-1 (MKP-1) concomitant with inhibited phosphorylation of p38

21 tivated protein kinase (MAPK) phosphatase-1 (MKP-1) have increased fatty acid oxidation and are prote

22 ogen-activated protein kinase phosphatase-1 (MKP-1) in cisplatin resistance.

23 ogen-activated protein kinase phosphatase-1 (MKP-1) is a key deactivator of MAP kinases, known effect

24 ogen-activated protein kinase phosphatase-1 (MKP-1) mRNA expression, which inhibits p-p38, was analyz

25 We also found that MAPK phosphatase-1 (MKP-1) negatively regulates S. pneumoniae-induced ERK-de

26 tment, the expression of MAPK phosphatase-1 (MKP-1) was significantly upregulated in human monocytes

27 hanced the expression of MAPK phosphatase-1 (MKP-1), a critical negative regulator of MAPKs that driv

28 ogen-activated protein kinase phosphatase-1 (MKP-1), a negative regulator of ERK1/2, through a protea

29 ogen-activated protein kinase phosphatase-1 (MKP-1), also known as dual specificity phosphatase-1 (DU

30 ogen-activated protein kinase phosphatase-1 (MKP-1), an inducible nuclear phosphatase, by regulating

31 ogen-activated protein kinase phosphatase-1 (MKP-1).

32 longed downregulation of MAPK phosphatase-1 (MKP-1).

33 ogen-activated protein kinase phosphatase-1 (MKP-1).

34 the epitope sequence recognized by the M-18 MKP-1 antibody revealed extensive phosphorylation of two

35 els, but hindered their detection by an M-18 MKP-1 antibody.

36 These data point to ACC MKP-1 as a key factor in the pathophysiology of depressi

37 oD bound to the MKP-1 promoter and activated MKP-1 expression in proliferating myoblasts.

38 In addition, MKP-1-deficient muscles exhibit exacerbated myopathy acc

39 In addition, MKP-2(-/-) CD11c(+) dendritic cells (DCs) had reduced ex

40 53 protein, while the activation of PI3K/Akt/MKP-1 pathway results in the inhibition of mitogen-activ

41 pathways, the PI3K/Akt/MDM2 and the PI3K/Akt/MKP-1 pathways.

42 Injurious ventilation induces MAPK in an MKP-1-dependent fashion.

43 ion by inhibiting the MAPK ERK pathway in an MKP-1-dependent manner.

44 e found that upon LPS stimulation, MKP-1 and MKP-2 accumulated with different kinetics: MKP-1 level p

45 Deletion of the C terminus from MKP-1 and MKP-2 also considerably increased their stabilities.

46 residues in the C terminus of both MKP-1 and MKP-2 by the ERK pathway.

47 odification in the accumulation of MKP-1 and MKP-2 in macrophages following LPS stimulation.

48 ingly, enhanced stabilities of the MKP-1 and MKP-2 mutants were not associated with decreased ubiquit

49 S stimulation had little effect on MKP-1 and MKP-2 protein levels, but hindered their detection by an

50 Our studies suggest that MKP-1 and MKP-2 stability is regulated by ERK-mediated phosphoryla

51 two C-terminal serine residues in MKP-1 and MKP-2 to alanine decreased their half-lives, while mutat

52 Degradation of both MKP-1 and MKP-2 was attenuated by proteasomal inhibitors.

53 Remarkably, the stability of both MKP-1 and MKP-2 was markedly decreased in macrophages in the prese

54 Accumulation of both MKP-1 and MKP-2 were attenuated by inhibition of the ERK cascade.

55 We found that Prdx1 bound to both MKP-1 and MKP-5, but dissociated from MKP-1 when the Prdx1 peroxid

56 lipid profiles; however, both MKP-1(+/-) and MKP-1(-/-) mice had significantly less aortic root ather

57 had cytotoxic effects, induced autophagy and MKP-1 expression, and enhanced Dox-induced apoptosis in

58 a (alpha) and beta (beta) isoforms of GR and MKP-1 in peripheral blood mononuclear cells (PBMC) after

59 orer cytoplasmic export of nuclear IRAK3 and MKP-1 stabilization, resulting in increased p38MAPK acti

60 lot study, the expression of GR isoforms and MKP-1 corresponded with patients' clinical response to s

61 arian tumor-derived cell lines MKP-Liver and MKP-Lung cells reproduce in vivo EMT and represent the f

62 ty compared with free ARN and Dusp1 mRNA and MKP-1 activity was significantly increased by ARN-NPs in

63 for the p53(DBD).(DP)JNK (274 +/- 14 nm) and MKP-5.(DP)JNK (55 +/- 8 nm) complexes were established;

64 f 3A-KO VSMCs with p53 siRNA reduced p21 and MKP-1 levels and completely restored growth without affe

65 We used wild-type and MKP-3 knock-out (KO) mice, a paw incision model of acute

66 he expression of negative regulators such as MKP-1 may have significant therapeutic potential for tre

67 ory effects, at least in part, by augmenting MKP-1 expression.

68 Blocking MKP-1 expression by triptolide also abolished the accele

69 ight and serum lipid profiles; however, both MKP-1(+/-) and MKP-1(-/-) mice had significantly less ao

70 wo serine residues in the C terminus of both MKP-1 and MKP-2 by the ERK pathway.

71 Degradation of both MKP-1 and MKP-2 was attenuated by proteasomal inhibitors

72 Remarkably, the stability of both MKP-1 and MKP-2 was markedly decreased in macrophages in

73 Accumulation of both MKP-1 and MKP-2 were attenuated by inhibition of the ERK

74 We found that Prdx1 bound to both MKP-1 and MKP-5, but dissociated from MKP-1 when the Prd

75 ads to a 50% reduction in the number of both MKPs and MKs and is associated with a 3-fold increase in

76 cates that suppression of JNK1/2 activity by MKP-1 maintains PARP-1 levels and suggests that MKP-1-me

77 -ribose) polymerase-1 (PARP-1) expression by MKP-1.

78 ve effects of p38 and JNK MAPK inhibition by MKP-1 without consequence to ERK activation in this stri

79 by preventing its rapid dephosphorylation by MKPs and that the simultaneous activation of p53 and JNK

80 USP9/MKP-4 is unique among these cytoplasmic MKPs in containing a conserved PKA consensus phosphoryla

81 +/+), heterozygous MKP-1(+/-), and deficient MKP-1(-/-) mice were exposed to sea level (SL), Denver a

82 Expression profiling demonstrated MKP-1 20-fold higher in rats ventilated prone rather tha

83 pneumoniae by inhibiting cAMP-PKA-dependent MKP-1 pathway.

84 PK, which was associated with time-dependent MKP-1 destabilization.

85 dual-specificity protein phosphatase DUSP10/MKP-5 negatively regulates muscle stem cell function in

86 Here, we investigated the function of Dusp16/MKP-7 in the innate immune system.

87 hich includes the ERK-specific enzymes DUSP6/MKP-3 and DUSP7/MKP-X.

88 However, unlike DUSP6/MKP-3, DUSP9/MKP-4 also inactivates the p38alpha MAP kin

89 e ERK-specific enzymes DUSP6/MKP-3 and DUSP7/MKP-X.

90 DUSP9/MKP-4 is phosphorylated on Ser-58 by PKA in vitro, and p

91 However, unlike DUSP6/MKP-3, DUSP9/MKP-4 also inactivates the p38alpha MAP kinase both in v

92 MAP kinase phosphatase 4 (DUSP9/MKP-4) plays an essential role during placental developm

93 ivation of both ERK1/2 and p38alpha by DUSP9/MKP-4 is mediated by a conserved arginine-rich kinase in

94 antibody demonstrates that endogenous DUSP9/MKP-4 is phosphorylated on Ser-58 in response to the PKA

95 Furthermore, DUSP9/MKP-4 is unique among these cytoplasmic MKPs in containi

96 PKA signaling and that attenuation of DUSP9/MKP-4 function can mediate cross-talk between the PKA pa

97 osphorylation abrogates the binding of DUSP9/MKP-4 to both ERK2 and p38alpha MAP kinases.

98 ution inhibits both the interaction of DUSP9/MKP-4 with ERK2 and p38alpha in vivo and its ability to

99 ct the intrinsic catalytic activity of DUSP9/MKP-4, phospho-mimetic (Ser-58 to Glu) substitution inhi

100 dy, we identified the MAPK phosphatase Dusp9/MKP-4 by transcriptome analysis as selectively expressed

101 We conclude that DUSP9/MKP-4 is a bona fide target of PKA signaling and that at

102 bone marrow megakaryocytes (MKs), embryonic MKPs were CD45(-) and represent an abundant population i

103 ransgenic mice where the Dusp4 gene encoding MKP-2 has been knocked out (MKP-2(-/-) mice), we show th

104 Here we show that enhancing MKP-1 expression is sufficient to achieve neuroprotectio

105 negative ERK2 mutant or a vector expressing MKP-3 inhibited the arginase II promoter activity.

106 After 12 weeks of HFD feeding, MKP-1LeuKO mice showed increased lesion size in both the

107 Immunoblotting for MKP-1, and IkappaBalpha and cytokine ELISAs were perform

108 e controls, indicating an important role for MKP-2 in EAE development.

109 ed IL-6 and TNF-alpha production by BMM from MKP-1(-/-) mice was significantly reduced as compared wi

110 o both MKP-1 and MKP-5, but dissociated from MKP-1 when the Prdx1 peroxidatic cysteine Cys52 was over

111 Hepatocytes from MKP-1-deficient mice exhibited reduced PPARgamma-induced

112 d primary hippocampal cultures prepared from MKP-2(-/-) mice with no effect on EPSC amplitude observe

113 Deletion of the C terminus from MKP-1 and MKP-2 also considerably increased their stabil

114 h these alterations in hippocampal function, MKP-2(-/-) mice show deficits in spatial reference and w

115 vitro assays were used to measure functional MKP-1 induction and preclinical models using Aggregatiba

116 ndings strongly suggest that CD49f(H)CD41(H) MKPs are fundamental to promote FL development, as propo

117 Moreover, after removing CD49f(H)CD41(H) MKPs from purified E11.5 FL hepatoepithelial-enriched ce

118 medium conditioned by E11.5 CD49f(H)CD41(H) MKPs produced a partial effect on CD49f(D) cells, induci

119 The CD49f(H)CD41(H) MKPs purified by cytometry differentiated in vitro to pr

120 Hematopoietic MKP-1 deficiency in atherosclerosis-prone mice mimicked

121 MKP-1) in blood monocytes, and hematopoietic MKP-1-deficiency in atherosclerosis-prone mice accelerat

122 Hence, MKP-1 plays an important role in MAPK-mediated control o

123 Further, hepatic MKP-1 regulates both interleukin-6 (IL-6) and fibroblast

124 Hence, hepatic MKP-1 serves as a selective regulator of MAPK-dependent

125 Mice lacking hepatic MKP-1 exhibit reduced circulating IL-6 and FGF21 levels

126 Here we show that hepatic MKP-1 becomes overexpressed following high-fat feeding.

127 These results also demonstrate that hepatic MKP-1 overexpression in obesity is causally linked to th

128 Wild-type MKP-1(+/+), heterozygous MKP-1(+/-), and deficient MKP-1(-/-) mice were exposed t

129 n D response element of the murine and human MKP-1 promoters were demonstrated.

130 tor and MED14, 4.7 kbp upstream of the human MKP-1 gene transcription start site, enhanced binding of

131 ssel wall thickness was increased in hypoxic MKP-1(-/-) lung.

132 In conclusion, we identified MKP-1 as a central redox-sensitive regulator of monocyte

133 These results identify MKP-5 as an essential negative regulator of the promyoge

134 esult of MKK3/6 activation and a decrease in MKP-1 expression, thereby leading to an increase in the

135 w that long-term potentiation is impaired in MKP-2(-/-) mice compared with MKP-2(+/+) controls wherea

136 d ERK pathways with a subsequent increase in MKP-1 expression.

137 cytes was already significantly increased in MKP-1LeuKO mice.

138 Although hypoxia up-regulated VEGF levels in MKP-1(+/+) MEFs eightfold, only a 70% increase in VEGF e

139 l p-p38 was expressed mostly in microglia in MKP-3 KO mice, and their selective pharmacological inhib

140 increase in VEGF expression was observed in MKP-1-deficient cells.

141 horylation of p38 MAP kinase was observed in MKP-1-null MEFs in response to hypoxia exposure.

142 The importance of PR in MKP-1 expression was supported by findings that MKP-1 an

143 from diabetic mice showed a 55% reduction in MKP-1 activity compared with nondiabetic mice.

144 ion of the two C-terminal serine residues in MKP-1 and MKP-2 to alanine decreased their half-lives, w

145 to sulfonic acid, which in turn resulted in MKP-1 oxidation-induced oligomerization and inactivity t

146 P activity restored cisplatin sensitivity in MKP-1 overexpressing cells.

147 of the transcription start site to increase MKP-1 expression.

148 induced ERK1/2 phosphorylation by increasing MKP-1 expression via a cAMP-PKA-dependent signaling path

149 Indeed, MKP-2(-/-) mice developed reduced EAE severity, associat

150 PG490-88 induced MKP-1 and was protective against high Vt in a nuclear fa

151 cell counts and cytokine levels, and induced MKP-1 and IkappaBalpha.

152 VitD/DEX-induced MKP-1 mRNA levels remained significantly lower in monocy

153 wn to mediate VitD enhancement of GC-induced MKP-1 production in monocytes via increased production o

154 shed VitD-mediated enhancement of GC-induced MKP-1 production.

155 MKP-1 or NAC treatment blocked 4-HNE-induced MKP-1 degradation, thereby protecting cell from apoptosi

156 stin treatment of T47D cells rapidly induced MKP-1 expression in a PR-dependent manner.

157 pressant treatment normalizes stress-induced MKP-1 expression and behavior, and mice lacking MKP-1 ar

158 VitD induced MKP-1 expression and enhanced DEX induction of MKP-1 in

159 Prone positioning is protective and induces MKP-1.

160 increased accumulation of p53, which induces MKP-1, p21, and WIP1, leading to inhibition of G(1) to S

161 PDE4B inhibits MKP-1 expression in a cAMP-PKA-dependent manner.

162 l mechanism that implicates PKCepsilon-IRAK3-MKP-1 signaling in the regulation of MAPK activity and i

163 tion and cognition, such as the MAP kinases, MKPs, CaMKII, CREB, Fyn, and Tau.

164 d MKP-2 accumulated with different kinetics: MKP-1 level peaked at approximately 1 h, while MKP-2 lev

165 ptin receptor-deficient (db/db) mice lacking MKP-1 are also resistant to the development of hepatic s

166 -1 expression and behavior, and mice lacking MKP-1 are resilient to stress.

167 y analyses of livers from db/db mice lacking MKP-1 showed suppression of peroxisome proliferator-acti

168 oth db/db and high fat diet-fed mice lacking MKP-1.

169 sistent mechanical allodynia in mice lacking MKP-3 (postoperative day 21), concurrently with persiste

170 Ovarian tumor-derived cell lines MKP-Liver and MKP-Lung cells reproduce in vivo EMT and r

171 ndings identify a regulatory circuit linking MKP-1 signaling in DCs, production of polarizing cytokin

172 he AKT pathway attenuated rapamycin-mediated MKP-1 induction.

173 vated the ERK pathway, leading to a moderate MKP-1 induction.

174 with immune-suppressive properties modulate MKP-1 expression as part of their mechanism of action.

175 n of the critical anti-inflammatory molecule MKP-1 in response to beta2 -agonists, as well as impaire

176 Moreover, MKP-1 inhibited induction of regulatory T cells by downr

177 ents revealed that CD4(+) T cells from naive MKP-2(-/-) mice had decreased cell proliferation and IL-

178 in hypoxia-induced vascular abnormalities of MKP-1(-/-) lung.

179 lational modification in the accumulation of MKP-1 and MKP-2 in macrophages following LPS stimulation

180 al cells revealed the specific activation of MKP-5, resulting in decreased p38MAPKalpha activity.

181 plexes were established; however, binding of MKP-5 and p53 to JNK was not mutually exclusive.

182 ments showed that bone marrow derived DCs of MKP-2(-/-) mice had impaired capability in antigen prese

183 d subsequent inactivation and degradation of MKP-1.

184 gulating proteasome-dependent degradation of MKP-1.

185 Liver-specific deletion of MKP-1 enhances gluconeogenesis and causes hepatic insuli

186 dings strongly suggest that dysregulation of MKP-3 prevents spontaneous resolution of acute postopera

187 This neuroprotective effect of MKP-1 was demonstrated to be dependent on its enzymatic

188 pal cultures, suggesting that the effects of MKP-2 deletion were MAPK independent.

189 sion, it markedly enhanced the expression of MKP-1 in cells stimulated by LPS, in a similar manner an

190 pathway, including altered the expression of MKP-1.

191 Here, we have shown that expression of MKP-3 is markedly increased in the liver of diet-induced

192 c stress promoted the S-glutathionylation of MKP-1, targeting MKP-1 for proteasomal degradation.

193 -induced oligomerization and inactivation of MKP-5 so that activation toward p38MAPK was maintained.

194 P-1 expression and enhanced DEX induction of MKP-1 in both patients with SS asthma and patients with

195 Importantly, P(4) induction of MKP-1 was associated with reduced levels of phosphorylat

196 horylated ERK1/2, whereas siRNA knockdown of MKP-1 blocked progestin-mediated ERK1/2 dephosphorylatio

197 Knockdown of MKP-1 mimicked the priming effects of metabolic stress,

198 Lack of MKP-1 compromised myoblast proliferation and induced pre

199 crophage content was increased in lesions of MKP-1LeuKO mice compared to mice that received wildtype

200 varian cancer cells expressed high levels of MKP-1 and PARP-1 proteins, and that silencing MKP-1 or P

201 on and migration and showed that the loss of MKP-1 activity is a critical step in monocyte priming an

202 Mechanistically, loss of MKP-1 inhibited PPARgamma function by increasing MAPK-de

203 diabetic conditions resulted in the loss of MKP-1 protein levels, the hyperactivation of ERK and p38

204 Moreover, mutants of MKP-1 that selectively prevented p38 or JNK binding conf

205 Importantly, either overexpression of MKP-1 or NAC treatment blocked 4-HNE-induced MKP-1 degra

206 Overexpression of MKP-1 prevented the polyglutamine-expanded huntingtin-in

207 induced cell death whereas overexpression of MKP-1 protects macrophages against metabolic stress-indu

208 lucocorticoid receptor, a known regulator of MKP-1 in other cell types.

209 ovide new insights into a functional role of MKP-1 in oxidative stress-induced cell death by regulati

210 2 deactivation, further supporting a role of MKP-1 in the anti-inflammatory mechanism of mapracorat.

211 However, the regulatory role of MKP-1 in the interplay between MAPK and NFkappaB pathway

212 kout, an antagonist, or a local silencing of MKP-1 attenuates depressive-like behaviors, pointing to

213 Gene silencing of MKP-1 increased STAT1 phosphorylation and prevented 5-am

214 horylation of p38 MAP kinase, a substrate of MKP-1, as well as alpha smooth muscle actin (alphaSMA) e

215 Transplantation of MKP-1-deficient bone marrow into LDL-R(-/-) (MKP-1LeuKO)

216 ed a significant Dex-induced upregulation of MKP-1 (P = .005).

217 n, this study identified the upregulation of MKP-1 by vitamin D as a novel pathway by which vitamin D

218 lar inflammation through the upregulation of MKP-1.

219 t studies have identified novel functions of MKPs in development, the immune system, and cancer.

220 mycin and a dual mTOR inhibitor (AZD2014) on MKP-1 expression.

221 rior to LPS stimulation had little effect on MKP-1 and MKP-2 protein levels, but hindered their detec

222 MAPK phosphatases (MKP-1 and/or MKP-5), which are known to dephosphorylate and deactivat

223 ered by either polyglutamine-expanded Htt or MKP-1.

224 p4 gene encoding MKP-2 has been knocked out (MKP-2(-/-) mice), we show that long-term potentiation is

225 to inhibiting hepatic fatty acid oxidation, MKP-1 promotes hepatic lipogenic gene expression through

226 97 and its cofactor, UBXD8, destabilize p21, MKP-1, and SIRT1, three established mRNA targets of the

227 at dendritic cell (DC)-expressed phosphatase MKP-1, a negative regulator of the MAP kinases, programm

228 ear dual-specificity MAP kinase phosphatase (MKP) DUSP2, a known regulator of the ERK and p38 MAPKs,

229 itogen-activated protein kinase phosphatase (MKP)-1 expression in vitro and in vivo.

230 kinase (MAPKs) regulator, MAPK phosphatase (MKP)-3, in the resolution of postoperative pain.

231 vented its inactivation by MAPK phosphatase (MKP)-5; however, JNK was still able to phosphorylate c-J

232 pression of the MAPK inhibitory phosphatase, MKP-1.

233 MAP phosphatases (MKP)-1 acts as an important regulator of innate immune r

234 nalyzed by microarray and MAPK phosphatases (MKP)-1 quantitative polymerase chain reaction.

235 MAPK phosphatases (MKP-1 and/or MKP-5), which are known to dephosphorylate

236 MAP kinase phosphatases (MKPs) are important regulators of the activation levels

237 togen-activated protein kinase phosphatases (MKPs) play key roles in inflammation and immune mediated

238 togen-activated protein kinase phosphatases (MKPs), directly inactivate MAPKs through dephosphorylati

239 MAP kinase phosphatases (MKPs), such as Arabidopsis (Arabidopsis thaliana) MKP1,

240 of dual-specificity MAP kinase phosphatases (MKPs/DUSPs).

241 MAPK phosphatases (MKPs) are critical modulators of the innate immune respo

242 which are inactivated by MAPK phosphatases (MKPs), represent a central signaling node in the regulat

243 rolled by redox-sensitive MAPK phosphatases (MKPs).

244 ctivated protein kinase (MAPK) phosphatases (MKPs) have been considered "undruggable," but their posi

245 lpha activation induced by S. aureus via PKA-MKP-1 pathway.

246 the post-translational regulation of a plant MKP in vivo, adding an additional regulatory layer to MA

247 t the post-translational regulation of plant MKPs in vivo.

248 on of Prdx1-Cys52 was enhancing in the Prdx1:MKP-5 complex with increasing amounts of H(2)O(2) concen

249 Preventing MKP-1 S-glutathionylation in metabolically stressed mono

250 The embryonic megakaryocyte progenitors (MKPs) in the E11.5 FL were identified as CD49f(H) CD41(H

251 ances the expansion of human MK progenitors (MKPs) and, to some extent, MKs.

252 s by overexpressing glutaredoxin 1 protected MKP-1 from degradation and normalized monocyte adhesion

253 MKP-1-deficient bone marrow into LDL-R(-/-) (MKP-1LeuKO) mice accelerated high-fat diet (HFD)-induced

254 KP-1 transcription start site to up-regulate MKP-1 promoter activity.

255 iting the expression of a negative regulator MKP-1, which in turn leads to enhanced MAPK ERK activati

256 p38 MAPK via induction of negative regulator MKP-1.

257 Introduction of a degradation-resistant MKP-1 mutant effectively attenuated luteolin-induced JNK

258 Silencing MKP-1 promoted PARP-1 ubiquitination, which decreased PA

259 KP-1 and PARP-1 proteins, and that silencing MKP-1 or PARP-1 increased cisplatin sensitivity in resis

260 While mapracorat alone did not stimulate MKP-1 expression, it markedly enhanced the expression of

261 We found that upon LPS stimulation, MKP-1 and MKP-2 accumulated with different kinetics: MKP

262 a soil isolate Pseudomonas monteilii strain MKP 213.

263 il a novel pathway consisting of superoxide, MKP-1, and JNK for luteolin's cytotoxicity in lung cance

264 esting that inhibition of the JNK suppressor MKP-1 plays a major role in luteolin-induced lung cancer

265 the S-glutathionylation of MKP-1, targeting MKP-1 for proteasomal degradation.

266 c root atherosclerotic lesion formation than MKP-1(+/+) mice.

267 appaBalpha with MKP-1, and demonstrated that MKP-1 was a pivotal feedback control for both MAP kinase

268 -1 expression was supported by findings that MKP-1 and PR mRNA levels were significantly correlated i

269 We found that MKP-1 overexpression stimulates PARP-1 and poly(ADP-ribo

270 We therefore hypothesized that MKP-1 is a crucial modulator of hypoxia-stimulated vesse

271 Our results show that MKP-2 mRNA levels in the spinal cord and lymphoid organs

272 These data show that MKP-2 plays a role in regulating hippocampal function an

273 Our studies suggest that MKP-1 and MKP-2 stability is regulated by ERK-mediated p

274 Collectively, these findings suggest that MKP-1 is a critical mediator of anti-proliferative and a

275 Therefore, our data strongly suggest that MKP-1 might be the key regulator of vascular densities t

276 ogenic actions of the MAPKs and suggest that MKP-5 may serve as a target to promote muscle stem cell

277 -1 maintains PARP-1 levels and suggests that MKP-1-mediated cisplatin resistance can be bypassed by P

278 crophage activation, our study suggests that MKP-2 is essential to the pathogenic response of EAE, an

279 The MKP-1 regulator PG490-88 (MRx-108; 0.75 mg/kg) or phosph

280 Here we show that, although the MKP DUSP5 both inactivates and anchors ERK in the nucleu

281 the ERK and p38 MAPKs, is unique amongst the MKP family in being able to bind to both ERK3 and ERK4.

282 Surprisingly, enhanced stabilities of the MKP-1 and MKP-2 mutants were not associated with decreas

283 oid response element 4.6 kbp upstream of the MKP-1 gene were significantly lower in monocytes from pa

284 n the glucocorticoid response element of the MKP-1 promoter in monocytes were analyzed by means of ch

285 6-kbp glucocorticoid response element of the MKP-1 promoter in the presence of GM-CSF in U937 cells.

286 esterone response elements downstream of the MKP-1 transcription start site to up-regulate MKP-1 prom

287 Mechanistically, MyoD bound to the MKP-1 promoter and activated MKP-1 expression in prolife

288 In line with this, MKP-1-null atheroma exhibited less macrophage content.

289 l contributions of p38 and JNK regulation to MKP-1-mediated neuroprotection.

290 Wild-type MKP-1 overexpression inhibited apoptosis in primary stri

291 Wild-type MKP-1(+/+), heterozygous MKP-1(+/-), and deficient MKP-1

292 priming effects of metabolic stress, whereas MKP-1 overexpression blunted both MAPK activation and mo

293 the underlying molecular mechanism by which MKP-1 expression is negatively regulated during S. pneum

294 Here we investigated the mechanisms by which MKP-2 modulates central nervous system (CNS) inflammatio

295 as to determine the mechanisms through which MKP-1 deficiency in monocytes and macrophages promotes a

296 While MKP-2 also modulates macrophage activation, our study su

297 P-1 level peaked at approximately 1 h, while MKP-2 levels continued to rise for at least 6 h.

298 is impaired in MKP-2(-/-) mice compared with MKP-2(+/+) controls whereas neuronal excitability, evoke

299 expression of MHC-II and CD40 compared with MKP-2(+/+) mice.

300 nteractions of p38, ERK or IkappaBalpha with MKP-1, and demonstrated that MKP-1 was a pivotal feedbac