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

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

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

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

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

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

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

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

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

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

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

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

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

24 (8-12 microg (kg body wt)-1 day-1), G6P and PEPCK activities in the liver and kidney were greater th

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

26 Increments in hepatic and renal G6P and PEPCK activities seen between 127-130 and 140-145 days o

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

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

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

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

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

32 increases in phosphorylation of p38 MAPK and PEPCK mRNA.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

50 reducing phosphoenolpyruvate carboxykinase (PEPCK) expression in hepatocytes and activating Akt kina

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

52 ident for phosphoenolpyruvate carboxykinase (PEPCK) expression, pyruvate kinase expression was decrea

53 imilar to phosphoenolpyruvate carboxykinase (PEPCK) from Escherichia coli as recently described in ot

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 ssing the phosphoenolpyruvate carboxykinase (PEPCK) gene under control of its own promoter.

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

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 an enzyme phosphoenolpyruvate carboxykinase (PEPCK) with and without bound substrates.

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

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

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

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

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

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

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

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

76 -1alpha), phosphoenolpyruvate carboxykinase (PEPCK), pyruvate carboxylase, and glucose-6-phosphatase,

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

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

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

80 Pase) and 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 ic enzyme phosphoenolpyruvate carboxykinase (PEPCK).

87 , such as phosphoenolpyruvate carboxykinase (PEPCK).

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

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

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

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

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

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

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

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

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

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

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

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

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

101 GTP-binding site unique to the GTP-dependent PEPCK family.

102 e first to be determined for a GTP-dependent PEPCK, and provide the first view of a novel GTP-binding

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

136 However, PEPCK and G6Pc expression remained unchanged.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

168 4 (TR4) as a key PEPCK regulator modulating PEPCK gene via a transcriptional mechanism.

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

170 GR to the same percent as was the nonmutated PEPCK-C gene promoter.

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

172 (PGC1alpha), a transcriptional activator of PEPCK.

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

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

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

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

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

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

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

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

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

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

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

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

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

186 Higher expression of PEPCK in the liver of B6 mice, under both standard-diet

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

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

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

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

191 tes glucose metabolism and the expression of PEPCK.

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

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

194 I) site are participants in the induction of PEPCK gene expression by thyroid hormone and cAMP.

195 primarily responsible for the inhibition of PEPCK by the LXR agonist.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

212 andidate to participate in the regulation of PEPCK.

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

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

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

216 ion of STAT3, a transcriptional repressor of PEPCK.

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

218 but had no effect on insulin suppression of PEPCK.

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

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

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

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

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

224 uconeogenic enzymes glucose-6-phosphatase or PEPCK.

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

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

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

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

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

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

235 7-130 days, hepatic and renal G6P, and renal PEPCK, activities were similar in intact and TX fetuses;

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

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

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

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

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

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

242 5A in Huh7 or primary hepatocytes stimulated PEPCK gene expression and glucose output in HepG2 cells,

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

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

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

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

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

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

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

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

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

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

253 4alpha stimulation of transcription from the PEPCK-C gene promoter.

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

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

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

257 entrations are dramatically increased in the PEPCK null livers.

258 ed a thyroid hormone response element in the PEPCK promoter and demonstrated that C/EBP proteins boun

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

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

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

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

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

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

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

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

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

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

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

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

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

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

273 in glucocorticoid-mediated expression 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 mone ligand, inhibited the activation of the PEPCK-C gene promoter by C/EBP alpha or C/EBP beta but n

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

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

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

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

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

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

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

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

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

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

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

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