ライフサイエンスコーパス: MKP-1

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 deficiency in T cells impaired the activation, pro

5 MKP-1 expression induced by BDNF signaling caused spatio

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

7 MKP-1 is a stress-responsive MKP that inactivates the MA

8 MKP-1 overexpression is also observed with unpredictable

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

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

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

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

13 MKP-1, also known as dual-specificity phosphatase-1 (DUS

14 MKP-1, also known as DUSP1, was previously shown to nega

15 Mice with homozygous deficiency in MKP-1 (MKP-1(-/-)) were bred with apolipoprotein (Apo)E-deficie

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

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

18 tion and inactivation of MAPK phosphatase 1 (MKP-1), a nuclear phosphatase.

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

20 ogen-activated protein kinase phosphatase 1 (MKP-1), is down-regulated by KLF5 ablation.

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

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

23 hosphorylation of p38 by MAPK phosphatase 1 (MKP-1).

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

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

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

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

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

29 We found that MAP kinase phosphatase-1 (MKP-1) controls axon branching.

30 ogen-activated protein kinase phosphatase-1 (MKP-1) exhibit exaggerated inflammatory responses and ra

31 ion also rapidly induced MAPK phosphatase-1 (MKP-1) expression; PI3K and TLR2 signaling were required

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

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

34 tivated protein kinase (MAPK) phosphatase-1 (MKP-1) is a critical negative regulator of the MAPKs.

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

36 MAPK phosphatase-1 (MKP-1) is encoded by mkp-1, a stress-responsive immediat

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

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

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

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

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

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

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

44 ogen-activated protein kinase phosphatase-1 (MKP-1), has been shown to be an important negative regul

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

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

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

48 tivated protein kinase (MAPK) phosphatase-1 (MKP-1, encoded by DUSP1, but hereafter called MKP-1) in

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

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

51 (Apo)E-deficient mice (ApoE(-/-)) and the 3 MKP-1 genotypes (MKP-1(+/+)/ApoE(-/-) ; MKP-1(+/-)/ApoE(

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

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

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

55 In addition, MKP-1-null mice had higher levels of plasma stromal cell

56 53 protein, while the activation of PI3K/Akt/MKP-1 pathway results in the inhibition of mitogen-activ

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

58 We tested the role of altered MKP-1 expression in rat and mouse models of depression a

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

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

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

62 -1(+/+)/ApoE(-/-) ; MKP-1(+/-)/ApoE(-/-) and MKP-1(-/-)/ApoE(-/-)) were maintained on a normal chow d

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

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

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

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

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

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

69 vented r-OPN-induced MKP-1 upregulation, and MKP-1 siRNA abolished both MAPK inactivation and anti-va

70 he 3 MKP-1 genotypes (MKP-1(+/+)/ApoE(-/-) ; MKP-1(+/-)/ApoE(-/-) and MKP-1(-/-)/ApoE(-/-)) were main

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

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

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

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

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

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

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

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

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

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

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

82 ng p38 dephosphorylation and inactivation by MKP-1.

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

84 KP-1, encoded by DUSP1, but hereafter called MKP-1) in the hippocampal subfields of subjects with MDD

85 Consistently, MKP-1(-/-) mice were defective in anti-influenza immunit

86 e chase assays, we found that KLF5 decreases MKP-1 protein degradation via activating the ERK signali

87 targets ERK deactivation, thereby decreasing MKP-1 and thus removing the negative inhibition of MKP-1

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

89 Consistently, the phosphorylation-deficient MKP-1 mutant cannot be stabilized by KLF5.

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

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

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

93 DUSP1/MKP-1 is implicated in cellular protection against a var

94 MAPK phosphatase-1 (DUSP1/MKP-1) is a mitogen and stress-inducible dual specificit

95 ators of UV-induced p38alpha-dependent DUSP1/MKP-1 transcription.

96 The induction of DUSP1/MKP-1 mRNA and protein in response to UV radiation is me

97 JNK pathways mediated by induction of DUSP1/MKP-1 regulates the cellular response to UV radiation.

98 interfering RNA-mediated knockdown of DUSP1/MKP-1 sensitizes wild-type MEFs to UV radiation, DUSP1/M

99 ld-type DUSP1/MKP-1 and by a mutant of DUSP1/MKP-1, which is unable to bind to either p38alpha or ERK

100 itizes wild-type MEFs to UV radiation, DUSP1/MKP-1 knockdown in MEFS lacking JNK1 and -2 does not res

101 and genetic tools to demonstrate that DUSP1/MKP-1 is an essential non-redundant regulator of UV-indu

102 ued by the reintroduction of wild-type DUSP1/MKP-1 and by a mutant of DUSP1/MKP-1, which is unable to

103 llel activation of PI3K, leading to enhanced MKP-1 expression, accelerated deactivation of MAPKs, and

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

105 tion increased in MKP-2(-/-) BMDMs following MKP-1 knockdown.

106 tor-kappaB ligand induced the expression for MKP-1, and osteoclasts derived from mkp-1(-/-) mice had

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

108 these data demonstrate an essential role for MKP-1 as a regulator of the myofiber composition of skel

109 etal muscle and suggest a potential role for MKP-1 in metabolic syndrome.

110 These results suggest a role for MKP-1 in osteoclasts, which originate from the fusion of

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

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

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

114 Furthermore, macrophages isolated from MKP-1-null mice showed dramatic defects in their spreadi

115 greater iNOS expression in macrophages from MKP-1(-/-) mice than in macrophages from wild-type mice.

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

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

118 mice (ApoE(-/-)) and the 3 MKP-1 genotypes (MKP-1(+/+)/ApoE(-/-) ; MKP-1(+/-)/ApoE(-/-) and MKP-1(-/

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

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

121 Hence, MKP-1 plays a critical role in muscle stem cells and in

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 ression and found that increased hippocampal MKP-1 expression, as a result of stress or viral-mediate

130 However, MKP-1 is not a KLF5 direct transcription target because

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

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

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

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

135 postmortem and preclinical studies identify MKP-1 as a key factor in MDD pathophysiology and as a ne

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

137 Mice with homozygous deficiency in MKP-1 (MKP-1(-/-)) were bred with apolipoprotein (Apo)E-

138 Previously we showed that mice deficient in MKP-1 have enhanced energy expenditure and are resistant

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

140 croRNA (miR)-155 expression was increased in MKP-1-deficient macrophages compared with wild-type macr

141 llenge elicited a stronger iNOS induction in MKP-1 knock-out mice than in wild-type mice.

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

143 gamma, was more potently activated by LPS in MKP-1(-/-) macrophages than in wild-type cells.

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

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

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

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

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

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

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

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

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

153 GSK-3-induced MKP-1 phosphorylation mediates negative feedback control

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

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

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

157 f Erk1/2 phosphorylation blocked EGF-induced MKP-1 phosphorylation.

158 show in mice that excess dietary fat induced MKP-1 overexpression in skeletal muscle, and that this r

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

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

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

162 bitor U0126 specifically blocks KLF5-induced MKP-1 phosphorylation and stabilization.

163 r-OPN induced MKP-1 in the spastic cerebral arteries via binding to L-

164 GRGDSP prevented r-OPN-induced MKP-1 upregulation, and MKP-1 siRNA abolished both MAPK

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

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

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

168 Prone positioning is protective and induces MKP-1.

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

170 r-OPN enhanced an endogenous MAPK inhibitor, MKP-1, and suppressed the phosphorylation of MAPKs, cald

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

172 splantation of MKP-1-intact bone marrow into MKP-1-null mice fully rescued the wild-type atherosclero

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

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

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

176 -1 expression and behavior, and mice lacking MKP-1 are resilient to stress.

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

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

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

180 In response to LPS, MKP-1(-/-) mice produce greater amounts of inflammatory

181 ell survival partially through pERK-mediated MKP-1 phosphorylation and stabilization.

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

183 In mdx mice, MKP-1 deficiency reduced body weight, muscle mass, and m

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

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

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

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

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

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

190 dings demonstrate that chronic deficiency of MKP-1 leads to decreased atherosclerosis via mechanisms

191 d subsequent inactivation and degradation of MKP-1.

192 gulating proteasome-dependent degradation of MKP-1.

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

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

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

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

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

198 ssion of GR phosphorylation and induction of MKP-1 and serum/glucocorticoid-regulated kinase.

199 n of JNK and p38, and increased induction of MKP-1 following LPS stimulation.

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

201 Therapeutic induction of MKP-1 may be a novel approach for the prevention and tre

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

203 ugh oxidative modification and inhibition of MKP-1 leading to a sustained activation of JNK and p38 M

204 and thus removing the negative inhibition of MKP-1 on cytokine production.

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

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

207 Furthermore, knockdown of MKP-1 using small interfering RNA enhances TGF-beta1-ind

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

209 iotoxin-induced muscle injury model, lack of MKP-1 impaired muscle regeneration.

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

211 Peak levels of MKP-1 correlated closely with the decline in p38 MAPK an

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

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

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

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

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

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

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

219 1 promoter leading to the down-regulation of MKP-1 and facilitation of promyogenic p38alpha/beta MAPK

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

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

222 ve for myogenesis, the physiological role of MKP-1 in skeletal muscle repair and regeneration has rem

223 2 deactivation, further supporting a role of MKP-1 in the anti-inflammatory mechanism of mapracorat.

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

225 ase in NO production, we studied the role of MKP-1 in the regulation of iNOS expression.

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

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

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

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

230 Finally, transplantation of MKP-1-intact bone marrow into MKP-1-null mice fully resc

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

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

233 lar inflammation through the upregulation of MKP-1.

234 s en face lesion was observed in 8-month-old MKP-1(-/-) mice.

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

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

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

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

239 97 and its cofactor, UBXD8, destabilize p21, MKP-1, and SIRT1, three established mRNA targets of the

240 The KLF5-FGF-BP-pERK-MKP-1 signaling axis may provide new therapeutic targets

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

242 we have identified nuclear MAPK phosphatase MKP-1 as a novel molecular target of ROS in TGF-beta sig

243 2) and the dual-specificity MAPK phosphatase MKP-1/DUSP1.

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

245 mitogen-activated kinase (MAP) phosphatases MKP-1 and MKP-3 were elevated in neurons.

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

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

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

249 Prolonging MKP-1 phosphorylation by LY294002 increased p27Kip1, whe

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

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

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

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

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

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

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

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

258 creases in iNOS expression in LPS-stimulated MKP-1(-/-) macrophages.

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

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

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

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

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

264 Our results thus demonstrate that MKP-1 is a critical positive regulator of T cell activat

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

266 -1 expression was supported by findings that MKP-1 and PR mRNA levels were significantly correlated i

267 We further found that MKP-1 is essential and sufficient for KLF5 to promote br

268 Here, we found that MKP-1 is necessary in T cell activation and function.

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 Immunohistochemical analysis revealed that MKP-1 expression was enriched in macrophage-rich areas v

272 Immunofluorescence revealed that MKP-1 was induced in the arterial smooth muscle layer.

273 Taken together, these results show that MKP-1 plays a role in the maintenance of bone mass and d

274 Here, we show that MKP-1 plays an essential role in adult regenerative myog

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

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

277 Our results suggest that MKP-1 may negatively regulate iNOS expression by control

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

279 -1 maintains PARP-1 levels and suggests that MKP-1-mediated cisplatin resistance can be bypassed by P

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

281 kines and NO than do wild-type mice, and the MKP-1(-/-) mice exhibit severe hypotension.

282 KLF5 direct transcription target because the MKP-1 mRNA level is not regulated by KLF5.

283 , during myogenesis, MyoD uncoupled from the MKP-1 promoter leading to the down-regulation of MKP-1 a

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

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

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

287 6-kbp glucocorticoid response element of the MKP-1 promoter in the presence of GM-CSF in U937 cells.

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

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

290 Consistent with this, MKP-1-deficient mice expressed higher levels of PGC-1alp

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

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

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

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

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

296 entral role in macrophages; however, whether MKP-1 plays a role in the maintenance of bone mass has y

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

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

299 4), is a phosphatase highly homologous with MKP-1 and is known to regulate MAP kinase signaling; how

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