ライフサイエンスコーパス: PEPCK

1 PEPCK activity was elevated threefold in lung cancer sam

2 PEPCK and G6Pase transcript levels are downregulated in

3 PEPCK and glucose-6-phosphatase mRNA levels were increas

4 PEPCK depletion also attenuated Mtb in IFNgamma-deficien

5 PEPCK enzymatic activity is half that of primary hepatoc

6 PEPCK-C(mus) mice had an enhanced exercise capacity, wit

7 PEPCK-C(mus) mice had an extended life span relative to

8 PEPCK-M was acutely silenced in gluconeogenic tissues of

9 sion of phosphoenolpyruvate carboxykinase 2 (PEPCK), glucose-6-phosphatase (G6Pase) and suppressed he

10 1.0+/-0.8), pyruvate cycling (154.4+/-43.4), PEPCK flux (221.7+/-47.6), and TCA cycle flux (49.1+/-16

11 ffect of 3-mercaptopicolinic acid (3-MPA), a PEPCK inhibitor, on C2C12 muscle cells.

12 Only caMKK6 activated transcription of a PEPCK-luciferase reporter construct.

13 ctural and kinetic characterization of A467G-PEPCK supports our model of the role of the active site

14 lthough cytosolic PEPCK (PEPCK-C) is absent, PEPCK-M message and protein were detected in INS-1 832/1

15 In addition, MKP-3 can activate PEPCK promoter in synergy with dexamethasone in hepatoma

16 f glycerol in promastigotes and amastigotes; PEPCK participates in the entry of aspartate in promasti

17 gulate other FoxO1 target genes (IGFBP-1 and PEPCK) but not serpinB1 expression in mouse primary hepa

18 te is diagnostic of pyruvate carboxylase and PEPCK flux in the liver.

19 YC), whereas ME abundance did not change and PEPCK abundance declined.

20 ated FOXO1/phospho-FOXO1 protein content and PEPCK/G6Pase messenger RNA (mRNA) expression did not rev

21 oduction (P < 0.02 vs. genotype control) and PEPCK gene expression.

22 vator-1alpha co-activation of the CYP7A1 and PEPCK genes.

23 sulted in significant increase of CYP7A1 and PEPCK mRNA expression and the rate of bile acid synthesi

24 e PPDK gene in the wild-type (Deltappdk) and PEPCK null (Deltappdk/Deltapepck) backgrounds.

25 important for the prepartum rises in G6P and PEPCK activities in the liver and kidney and may mediate

26 (8-12 microg (kg body wt)-1 day-1), G6P and PEPCK activities in the liver and kidney were greater th

27 At 140-145 days, tissue G6P and PEPCK activities in TX fetuses were lower than in intact

28 line-infused fetuses, but only renal G6P and PEPCK increased to the level seen close to term.

29 ic genes (glucose-6-phosphatase [G6Pase] and PEPCK) contributes to hyperglycemia.

30 of glucocorticoid receptor, 11beta-HSD1, and PEPCK, and these effects were abolished by RU486.

31 emia, glycemia after pyruvate injection, and PEPCK protein expression in the liver of HFD-fed and db/

32 of DBC1 knockdown on Rev-erbalpha levels and PEPCK expression, suggesting that the mechanism of PEPCK

33 increases in phosphorylation of p38 MAPK and PEPCK mRNA.

34 gluconeogenesis by decreasing Glc-6-Pase and PEPCK gene expression through NR1D1.

35 genesis and the expression of Glc-6-Pase and PEPCK.

36 f leptin on gluconeogenesis, Glc-6-Pase, and PEPCK were abolished, and a marked suppression of glycog

37 profound increase in expression of PHGDH and PEPCK-M in skeletal muscle, implicating a role for biosy

38 ydrate response element-binding protein, and PEPCK mRNAs were unaffected in SMLPL(-/-) mice, but pero

39 mouse lungs but also failed to survive, and PEPCK depletion during the chronic phase of infection re

40 TR4 transactivates the 490-bp PEPCK promoter-containing luciferase reporter gene activ

41 (G6P) and phosphoenolpyruvate carboxykinase (PEPCK) activities were investigated in sheep fetuses aft

42 inhibited phosphoenolpyruvate carboxykinase (PEPCK) and accelerated fibroblast cell migration up to 3

43 ession of phosphoenolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase, catalytic (G6Pc).

44 ic enzyme phosphoenolpyruvate carboxykinase (PEPCK) and impairs insulin signalling in muscle.

45 n enzymes phosphoenolpyruvate carboxykinase (PEPCK) and malic enzyme (ME) did not change.

46 c enzymes phosphoenolpyruvate carboxykinase (PEPCK) and phosphoenolpyruvate carboxykinase 2 (PCK2) to

47 cytosolic phosphoenolpyruvate carboxykinase (PEPCK) and plastidic NADP-dependent malic enzyme (ME) on

48 -Pase and phosphoenolpyruvate carboxykinase (PEPCK) by apoA-IV was determined by luciferase activity

49 lycosomal phosphoenolpyruvate carboxykinase (PEPCK) by EP and again found that the intradermal route

50 Phosphoenolpyruvate carboxykinase (PEPCK) catalyzes the first committed step of gluconeogen

51 ic enzyme phosphoenolpyruvate carboxykinase (PEPCK) demonstrate that PEPCK contains a 10-residue Omeg

52 discrete phosphoenolpyruvate carboxykinase (PEPCK) enzymes in the parasite, one of which resides in

53 Phosphoenolpyruvate carboxykinase (PEPCK) expression plays a critical role in the modulatio

54 hesis and phosphoenolpyruvate carboxykinase (PEPCK) gene in gluconeogenesis.

55 The phosphoenolpyruvate carboxykinase (PEPCK) gene is a case in point.

56 vation of phosphoenolpyruvate carboxykinase (PEPCK) gene transcription in response to all-trans-retin

57 lation of phosphoenolpyruvate carboxykinase (PEPCK) in wild-type (WT) mouse liver.

58 Phosphoenolpyruvate carboxykinase (PEPCK) is a gluconeogenic enzyme with a cytosolic (Pck1/

59 Phosphoenolpyruvate carboxykinase (PEPCK) is an essential metabolic enzyme operating in the

60 Phosphoenolpyruvate carboxykinase (PEPCK) is regulated solely by alterations in gene expres

61 Phosphoenolpyruvate carboxykinase (PEPCK) is well known for its role in gluconeogenesis.

62 -specific phosphoenolpyruvate carboxykinase (PEPCK) null mice, when fasted, maintain normal whole bod

63 used the phosphoenolpyruvate carboxykinase (PEPCK) promoter to generate transgenic mice in which Cre

64 alyzed by phosphoenolpyruvate carboxykinase (PEPCK) provides significant insight into the chemical me

65 soform of phosphoenolpyruvate carboxykinase (PEPCK) reported in the PEPCK-Mn2+, -Mn2+-oxaloacetic aci

66 ic enzyme phosphoenolpyruvate carboxykinase (PEPCK) transcription and associated transcription factor

67 iption of phosphoenolpyruvate carboxykinase (PEPCK), a key regulator of gluconeogenesis, by consuming

68 ence that phosphoenolpyruvate carboxykinase (PEPCK), an enzyme involved in malate metabolism and gluc

69 ic genes, phosphoenolpyruvate carboxykinase (PEPCK), and glucose-6-phosphatase (G6Pase), and NAD(+) l

70 (PGC-1), phosphoenolpyruvate carboxykinase (PEPCK), and glucose-6-phosphatase expression.

71 ase (GK), phosphoenolpyruvate carboxykinase (PEPCK), and pyruvate phosphate dikinase (PPDK) in glucon

72 etate via phosphoenolpyruvate carboxykinase (PEPCK), forward TCA cycle flux of [4-(13)C]oxaloacetate

73 levels of phosphoenolpyruvate carboxykinase (PEPCK), glucose-6-phosphatase, and peroxisome proliferat

74 c enzyme, phosphoenolpyruvate carboxykinase (PEPCK), has been shown to provide metabolites for cell g

75 -1alpha), phosphoenolpyruvate carboxykinase (PEPCK), pyruvate carboxylase, and glucose-6-phosphatase,

76 lation of phosphoenolpyruvate carboxykinase (PEPCK), the key gene in gluconeogenesis, is critical for

77 In phosphoenolpyruvate carboxykinase (PEPCK)-GFP mice, serial MPM found PEC-to-podocyte migrat

78 D-ME) and phosphoenolpyruvate carboxykinase (PEPCK).

79 Pase) and phosphoenolpyruvate carboxykinase (PEPCK).

80 ic enzyme phosphoenolpyruvate carboxykinase (PEPCK).

81 enic gene phosphoenolpyruvate carboxykinase (PEPCK).

82 Pase) and phosphoenolpyruvate carboxykinase (PEPCK).

83 lpha) and phosphoenolpyruvate carboxykinase (PEPCK).

84 ession of phosphoenolpyruvate carboxykinase (PEPCK).

85 Pase) and phosphoenolpyruvate carboxykinase (PEPCK).

86 , such as phosphoenolpyruvate carboxykinase (PEPCK).

87 cytosolic phosphoenolpyruvate carboxykinase (PEPCK-C) and associated pathways.

88 rm of the phosphoenolpyruvate carboxykinase (PEPCK-C) gene is selectively expressed in several tissue

89 soform of phosphoenolpyruvate carboxykinase (PEPCK-M) is the GTPase linking hydrolysis of mtGTP made

90 chondrial phosphoenolpyruvate carboxykinase (PEPCK-M), encoded by the nuclear PCK2 gene, links TCA cy

91 d genes (phosphoenolpyruvate carboxykinase - PEPCK, glucocorticoid receptor - GR, and Vtg) in liver a

92 ressor of phosphoenolpyruvate carboxykinase, PEPCK) is a methanol- and biotin starvation-inducible zi

93 riptions of phosphoenolpyruvate carboxylase (PEPCK) and glucose-6-phosphatase (G6Pase) genes.

94 f other key regulatory proteins that control PEPCK-C gene transcription also likely contributed to th

95 Although cytosolic PEPCK (PEPCK-C) is absent, PEPCK-M message and protein w

96 s lacking in plastidic NADP-ME and cytosolic PEPCK activities revealed differential changes in overal

97 c fluxes in livers lacking hepatic cytosolic PEPCK by NMR using 2H and 13C tracers.

98 Inactivation of cytosolic PEPCK affected the respiration rate, which suggests that

99 The present study demonstrates PEPCK-M overexpression in tumorigenic cells as well as t

100 ex/RA has a synergistic effect on endogenous PEPCK gene expression in rat hepatocytes and H4IIE hepat

101 cells, pterosin A inhibited inducer-enhanced PEPCK expression, triggered the phosphorylations of AMPK

102 s SREBP1c, transmembrane protein FAS, enzyme PEPCK, and protein HSL).

103 e up-regulation of the rate-limiting enzymes PEPCK and G6Pc.

104 ey hepatic glucose production (HGP) enzymes, PEPCK and glucose-6-phosphatase, and increased glycogen

105 alpha-skeletal actin gene promoter, express PEPCK-C in skeletal muscle (1-3 units/g).

106 Finally, PEPCK-M knockdown using either siRNA or shRNA were suffi

107 ulin represses transcription of the gene for PEPCK-C by inducing SREBP-1c production in the liver, wh

108 tion inhibited transcription of the gene for PEPCK-C in part by deacetylation of HNF4alpha.

109 as a new posttranslational modification for PEPCK, 2) describes a pathway by which transcriptional i

110 IsoNAM decreased the level of mRNA for PEPCK-C but had no effect on mRNA for glucose-6-phosphat

111 We show here an unexpected role for PEPCK in promoting cancer cell proliferation in vitro an

112 together, these data demonstrate a role for PEPCK that links metabolic flux and anabolic pathways to

113 cells and 41% of PEP in rat islets came from PEPCK-M.

114 f PEPCK-C knock-out livers, hepatocytes from PEPCK-M-deficient livers maintained normal oxidative fun

115 nate was completely abolished in livers from PEPCK KO mice, indicating that the major pathway for ent

116 patic gluconeogenic genes, including G6Pase, PEPCK, and FOXO1.

117 expression of the glucagon receptor (GCGR), PEPCK, and genes involved in amino acid metabolism and u

118 decreased expression of gluconeogenic genes PEPCK and G-6-Pase, enhanced insulin-induced suppression

119 eduction of the expression of two key genes: PEPCK (phosphoenolpyruvate carboxykinase) and SREBP-1c (

120 When linked to GFP or to GFP-PEPCK-C each of the novel NLS motifs was sufficient to d

121 Our results demonstrated that indeed GK, PEPCK, and PPDK are key players in the gluconeogenesis p

122 he half-life of various chimeric beta-globin-PEPCK (betaG-PCK) mRNAs in LLC-PK -F(+) cells.

123 icator of TCA flux that is crucial for GSIS, PEPCK-M is a strong candidate to link mtGTP synthesis wi

124 the identification of a new pathway, TR4 --> PEPCK --> gluconeogenesis --> blood glucose, which may a

125 for phosphoenolpyruvate carboxykinase (GTP) (PEPCK-C) (EC 4.1.1.32) was linked to the alpha-skeletal

126 of phosphoenolpyruvate carboxykinase (GTP) (PEPCK-C).

127 of phosphoenolpyruvate carboxykinase (GTP) (PEPCK-C).

128 phosphoenolpyruvate (PEP) carboxykinase (GTP-PEPCK) were investigated.

129 d basal glucose production rates and hepatic PEPCK and glucose-6-phosphatase expression, which were n

130 r in intact and TX fetuses; however, hepatic PEPCK was increased by TX.

131 roscopy to show that in mice lacking hepatic PEPCK, 1) whole-body glucose turnover is only slightly d

132 an increase in the expression of the hepatic PEPCK depending on previous metabolic status.

133 Thus, although mice without hepatic PEPCK have markedly impaired hepatic gluconeogenesis, th

134 However, PEPCK and G6Pc expression remained unchanged.

135 However, PEPCK is also a key regulator of TCA cycle flux.

136 However, PEPCK-M is present in a variety of non-gluconeogenic tis

137 The human PEPCK crystal structure suggests that Asp(78) influences

138 Changes in PEPCK appear to have little or no acute effect on glucon

139 h of the study, despite a marked decrease in PEPCK content, suggesting poor control strength for this

140 rexpression of DBC1 results in a decrease in PEPCK mRNA and protein levels.

141 rease in SREBP-1c mRNA and a 95% decrease in PEPCK mRNA.

142 y investigate the roles of the lid domain in PEPCK function, we introduced three mutations that repla

143 DBC1 absence leads to an increase in PEPCK mRNA and protein expression.

144 suggested that the pH-responsive increase in PEPCK mRNA in LLC-PK1-FBPase+ cells is mediated by a p38

145 Thus, the pH-responsive increase in PEPCK mRNA in the kidney is mediated by the p38 MAPK sig

146 ) and 7 (p < 0.01), and a 2-fold increase in PEPCK-M protein expression at day 7 (p < 0.01).

147 l by 4 h, despite a substantial reduction in PEPCK protein, as gluconeogenically-derived carbon was r

148 se in insulin, despite eventual reduction in PEPCK protein, supporting the concept that PEPCK has poo

149 ound that conditional inactivation of VHL in PEPCK-Cre mutants resulted in renal cyst development tha

150 aling pathways are responsible for increased PEPCK-M levels.

151 ontrast, ectopic expression of TR4 increased PEPCK gene expression and hepatic glucose production in

152 in high plasma glucose content by increasing PEPCK and G6P mRNA level.

153 nthrin, and 3-PBA decreased cortisol-induced PEPCK gene expression, while o,p'-DDT and methoxychlor i

154 with exogenous LPA blunted glucagon-induced PEPCK expression and glucose production.

155 on; in cells lacking NR1D1, fails to inhibit PEPCK and Glc-6-Pase gene expression; and stimulates hig

156 were unable to confirm that 3-MPA inhibited PEPCK-M enzyme activity as 3-MPA interfered with the PEP

157 ins its profusely studied cytosolic isoform (PEPCK-C) potentiating gluconeogenesis and TCA flux.

158 although loss of the mitochondrial isoform (PEPCK-M) has never been assessed.

159 lar orphan nuclear receptor 4 (TR4) as a key PEPCK regulator modulating PEPCK gene via a transcriptio

160 d liver phosphoenolpyruvate carboxyl kinase (PEPCK) expression in diabetic mice.

161 n of phosphoenolpyruvate carboxylase kinase (PEPCK), fructose-1,6-bisphosphatase (FBPase), and glucos

162 Upon an extended 24-h fast, livers that lack PEPCK exhibit both 2-fold lower glucose production and o

163 uconeogenesis rates from hepatocytes lacking PEPCK-M are severely reduced for lactate, alanine, and g

164 Importantly, Mtb lacking PEPCK not only failed to replicate in mouse lungs but al

165 In the liver PEPCK-M adjoins its profusely studied cytosolic isoform

166 expected and important role of mitochondrial PEPCK in cancer metabolism.

167 4 (TR4) as a key PEPCK regulator modulating PEPCK gene via a transcriptional mechanism.

168 activity of PEPCK-C of 9 units/g of muscle (PEPCK-C(mus) mice).

169 ta-shRNA significantly reduced or normalized PEPCK expression, with no change in PGC-1alpha or FOXO1

170 (PGC1alpha), a transcriptional activator of PEPCK.

171 s together produced mice with an activity of PEPCK-C of 9 units/g of muscle (PEPCK-C(mus) mice).

172 e mitochondrial deficiency characteristic of PEPCK-C knock-out livers, hepatocytes from PEPCK-M-defic

173 ivator 1 alpha (PGC1alpha), a coactivator of PEPCK and G6Pase transcription.

174 s transactivation activity in the context of PEPCK gene transcription.

175 The contribution of PEPCK-M to overall PEP synthesis more than tripled with

176 islets measured substantial contribution of PEPCK-M to the synthesis of PEP.

177 Finally, we show that the effects of PEPCK on glucose metabolism and cell proliferation are i

178 ator holocomplex and regulates expression of PEPCK (phosphoenolpyruvate carboxykinase), G6P (glucose-

179 oviral infection increased the expression of PEPCK and G6Pase genes and led to elevated glucose produ

180 sts, accompanied with enhanced expression of PEPCK and G6Pase genes.

181 nd that apoA-IV suppresses the expression of PEPCK and Glc-6-Pase in hepatocytes; decreases hepatic g

182 The FFA-induced expression of PEPCK and PGC-1alpha genes and gluconeogenesis in isolat

183 vels of Foxo1 protein and mRNA expression of PEPCK by 48 +/- 4% and G6Pase by 64 +/- 3%.

184 er and insulin sensitivity and expression of PEPCK mRNA in db/db mice and db/+ controls.

185 in patients with T2DM, hepatic expression of PEPCK or G6Pc was not increased.

186 Surprisingly, the expression of PEPCK or G6Pc was not increased.

187 sphorylation of FOXO1, reduced expression of PEPCK, and increased glucokinase expression resulting in

188 urn be attributed to decreased expression of PEPCK, FBPase, and G6Pase due to increased acetylation o

189 tes glucose metabolism and the expression of PEPCK.

190 Both cytosolic and mitochondrial forms of PEPCK were found to undergo ADP-ribosylation.

191 erence (RNAi) vector blocks the induction of PEPCK and G6P, and blunts hepatic glucose output.

192 ic differentiation through the inhibition of PEPCK-M.

193 re we show that the mitochondrial isoform of PEPCK (PCK2) is expressed and active in three lung cance

194 been attributed to the cytosolic isoform of PEPCK (PEPCK-C), although loss of the mitochondrial isof

195 e structures of the mitochondrial isoform of PEPCK reported are complexed with Mn2+, Mn2+-PEP, or Mn2

196 of p38 MAPK and an increase in the level of PEPCK mRNA that closely mimicked the effect of treatment

197 omato plants with strongly reduced levels of PEPCK and plastidic NADP-ME were generated by RNA interf

198 ption of hepatic cataplerosis due to loss of PEPCK leads to the accumulation of TCA cycle intermediat

199 iously proposed a model for the mechanism of PEPCK catalysis in which the conformation of this mobile

200 expression, suggesting that the mechanism of PEPCK regulation is, at least in part, dependent on the

201 nt of triglyceride in the skeletal muscle of PEPCK-C(mus) mice were greatly increased as compared wit

202 g AMPK down-regulation and overexpression of PEPCK and G6Pc.

203 We conclude that overexpression of PEPCK-C repatterns energy metabolism and leads to greate

204 expression that involve changes in rates of PEPCK mRNA transcription and degradation.

205 Mice lacking TR4 also display reduction of PEPCK expression with impaired gluconeogenesis.

206 i-1/2, and this blocks insulin regulation of PEPCK and G6Pase expression.

207 or PKB activity in the insulin regulation of PEPCK, G6Pase, and a third insulin-regulated gene, IGF-b

208 ral pathways contribute to the regulation of PEPCK, including the nuclear receptor Rev-erbalpha and t

209 andidate to participate in the regulation of PEPCK.

210 protein that acts as a negative regulator of PEPCK in P. pastoris cultured in biotin-deficient, gluco

211 s that reverse insulin-induced repression of PEPCK transcription.

212 is, rescues the DUSP4-mediated repression of PEPCK.

213 ion of STAT3, a transcriptional repressor of PEPCK.

214 ntrasts a previously determined structure of PEPCK in complex with a triphosphate nucleotide analogue

215 but had no effect on insulin suppression of PEPCK.

216 ulin signaling to decreased transcription of PEPCK and glucose-6-phosphatase (G6Pase) and provides a

217 er is necessary for hepatic transcription of PEPCK-C.

218 ity or levels prevents the effect of DBC1 on PEPCK.

219 gene that antagonized insulin suppression on PEPCK gene transcription from this screen.

220 Upon formation of the PEPCK-Mn2+-PEP or PEPCK-Mn2+-malonate-Mn2+ GDP complexes, C307 coordinatio

221 uconeogenic enzymes glucose-6-phosphatase or PEPCK.

222 nt glucagon-stimulated glucose production or PEPCK expression in hepatocytes lacking STAT3.

223 Experimental data on other PEPCKs indicate that Arg(81) binds PEP, and the phosphat

224 gluconeogenic enzyme with a cytosolic (Pck1/PEPCK-C) and mitochondrial (Pck2/PEPCK-M) isoform.

225 To conclude, as Pck2/PEPCK-M is the predominant isoform in C2C12 cells, we po

226 e, phosphoenolpyruvate carboxykinase-M (Pck2/PEPCK-M), increased during treatment with BA, and to a l

227 solic (Pck1/PEPCK-C) and mitochondrial (Pck2/PEPCK-M) isoform.

228 atocytes reduced the T(3) induction of PDK4, PEPCK, and CPT-1a genes.

229 Although cytosolic PEPCK (PEPCK-C) is absent, PEPCK-M message and protein were det

230 ttributed to the cytosolic isoform of PEPCK (PEPCK-C), although loss of the mitochondrial isoform (PE

231 mall interfering RNA and the pharmacological PEPCK inhibitor 3-mercaptopicolinate significantly enhan

232 ogenesis, indicating Pck2 is the predominant PEPCK isoform.

233 anslational change in a TCDD target protein (PEPCK), and 3) reveals that the AHR exerts complex, prev

234 d increase in endogenous LPA levels, reduced PEPCK levels during fasting, and decreased hepatic gluco

235 G2 cells, whereas a deletion in NS5A reduced PEPCK expression and lowered cellular lipids but was wit

236 7-130 days, hepatic and renal G6P, and renal PEPCK, activities were similar in intact and TX fetuses;

237 lin-induced PKB is required to fully repress PEPCK and G6Pase expression.

238 erestingly, however, hGRbeta did not repress PEPCK in GR liver knockout (GRLKO) mice.

239 to glucagon receptor activation and requires PEPCK-C, thus providing new insights into liver metaboli

240 amuscular route for generating skin-resident PEPCK-specific T cells.

241 Silencing PEPCK-M lowers plasma glucose, insulin, and triglyceride

242 Liver-specific PEPCK knockout mice, which are viable despite markedly a

243 ptor- null mice and mice with liver-specific PEPCK-C deletion.

244 5A in Huh7 or primary hepatocytes stimulated PEPCK gene expression and glucose output in HepG2 cells,

245 cate that C/EBPalpha mediates p38-stimulated PEPCK transcription in liver cells.

246 ucose production (i.e., it fails to suppress PEPCK and other genes of gluconeogenesis), yet it retain

247 ss promoters of enzymes of glucose synthesis PEPCK and G6Pase.

248 t here that TCDD-induced TiPARP also targets PEPCK for ADP-ribosylation.

249 uring dark-induced stomatal closure and that PEPCK is involved in this process.

250 n PEPCK protein, supporting the concept that PEPCK has poor control strength over the gluconeogenic p

251 ses and (13)C carbon tracing to confirm that PEPCK is essential for growth of Mtb on fatty acids and

252 uvate carboxykinase (PEPCK) demonstrate that PEPCK contains a 10-residue Omega-loop domain that acts

253 We further show that PEPCK is required for growth of Mtb in isolated bone mar

254 The PEPCK-C(mus) mice ate 60% more than controls but had hal

255 4alpha stimulation of transcription from the PEPCK-C gene promoter.

256 rol failed to repress transcription from the PEPCK-C gene promoter; overexpression of HNF4alpha in Ch

257 timulated transcription (8-27-fold) from the PEPCK-C gene promoter; this was lost when both SREs were

258 s provides a further illustration of how the PEPCK gene promoter integrates different hormone respons

259 entrations are dramatically increased in the PEPCK null livers.

260 tivation of the cAMP response element in the PEPCK promoter.

261 he glucocorticoid response unit (GRU) in the PEPCK-C gene promoter (-2000 to +73) restrained C/EBP al

262 two SREBP regulatory elements (SREs) in the PEPCK-C gene promoter (-322 to -313 and -590 to -581).

263 ty lipoprotein (LDL) receptor gene (T in the PEPCK-C gene promoter at -582, compared with an A in the

264 ory regions corresponding to the SREs in the PEPCK-C gene promoter.

265 n inhibition as observed with the SRE in the PEPCK-C gene promoter.

266 the binding to nuclear receptor sites in the PEPCK-C gene promoter.

267 ruvate carboxykinase (PEPCK) reported in the PEPCK-Mn2+, -Mn2+-oxaloacetic acid (OAA), -Mn2+-OAA-Mn2+

268 In the PEPCK-Mn2+-GTP structure, the same water molecule displa

269 ird conformation of the mobile P-loop in the PEPCK-Mn2+-malonate-Mn2+ GDP complex demonstrates the pa

270 rdering of the mobile active site lid in the PEPCK-Mn2+-malonate-Mn2+ GDP complex yields the first ob

271 In the PEPCK-Mn2+-OAA complex, an alternate bound conformation

272 ntroduction of the LDL receptor SRE into the PEPCK-C gene promoter increased SREBP-1c binding and cau

273 ion, in contrast to their stimulation of the PEPCK gene.

274 RNA, which contains the entire 3'-UTR of the PEPCK mRNA, was degraded with a half-life of 1.2 h.

275 hat participate in the rapid turnover of the PEPCK mRNA.

276 hat may contribute to the rapid decay of the PEPCK mRNA.

277 ice using a reporter system comprised of the PEPCK promoter placed upstream of the alkaline phosphata

278 ifically, a reporter system comprised of the PEPCK promoter upstream of alkaline phosphatase was used

279 d SDF-1beta both inhibited activation of the PEPCK promoter.

280 CREB prevented FFA-induced activation of the PEPCK promoter.

281 necessary for FFA-induced activation of the PEPCK promoter.

282 quired for transcriptional repression of the PEPCK-C gene promoter caused by these compounds.

283 pha was the strongest trans-activator of the PEPCK-C gene promoter in the NIH3T3 cell line.

284 the stimulatory effect of Sp1 at -590 of the PEPCK-C gene promoter.

285 Upon formation of the PEPCK-Mn2+-PEP or PEPCK-Mn2+-malonate-Mn2+ GDP complexes

286 pattern of nucleosomal repositioning on the PEPCK promoter in vitro and in vivo, correlating with NF

287 Ai) in hepatocytes significantly reduced the PEPCK gene expression and glucose production in response

288 Silencing the PEPCK-M gene completely inhibited GSIS underscoring its

289 uitment of p300 and RNA polymerase II to the PEPCK promoter is increased by the combined Dex/RA treat

290 which decreased its binding affinity to the PEPCK-C gene promoter.

291 During light-dark transients the PEPCK mutant plants show both increased overall stomatal

292 Using the PEPCK promoter, we validated the integrity of these temp

293 enzyme activity as 3-MPA interfered with the PEPCK enzyme assay, particularly at 0.5 and 1 mM.

294 opsis PCK1 gene promoter indicated that this PEPCK isoform is specifically expressed in guard cells a

295 boxylase, and that cataplerotic flux through PEPCK is the primary source of [(13)C]bicarbonate.

296 Thus, PEPCK-M has a direct role in fasted and fed glucose home

297 On a mouse treadmill, PEPCK-C(mus) mice ran up to 6 km at a speed of 20 m/min,

298 Unexpectedly, PEPCK also increased the synthesis of ribose from non-ca

299 The interaction of Mg-IDP with PEPCK is dependent upon a single acidic ionization attri

300 the interaction of phosphoenolpyruvate with PEPCK and a single basic ionization with a pK(a) value o