ライフサイエンスコーパス: glucose-6-phosphatase

1 ing phosphoenoylpyruvate carboxyl kinase and glucose-6-phosphatase.

2 f endoplasmic reticulum harboring the marker glucose-6-phosphatase.

3 c amino acids, and downregulation of hepatic glucose-6-phosphatase.

4 vity to an epitope derived from liver/kidney glucose-6-phosphatase.

5 nal glucose levels by increasing the K(m) of glucose-6-phosphatase.

6 luding phosphoenolpyruvate carboxykinase and glucose-6-phosphatase.

7 ted protein (IGRP) is indeed the major islet glucose-6-phosphatase.

8 hosphoenolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase.

9 inal step in gluconeogenesis is catalyzed by glucose-6-phosphatase.

10 y a deficiency in the activity of the enzyme glucose-6-phosphatase.

11 e expression of the key gluconeogenic enzyme glucose-6-phosphatase.

12 nesis, phosphoenolpyruvate carboxykinase and glucose-6-phosphatase.

13 oplasmic reticulum phosphatase homologous to glucose-6-phosphatase.

14 down regulation of the gluconeogenic enzyme, glucose-6-phosphatase.

15 ol can induce a rate-limiting enzyme of GNG, glucose-6-phosphatase.

16 -phosphate (1,5AG6P) caused neutropenia in a glucose-6-phosphatase 3 (G6PC3)-deficient mouse model an

17 Glucose-6-phosphatase, a key enzyme in the homeostatic r

18 orage disease type Ia (GSD-Ia), deficient in glucose-6-phosphatase-a (G6PC), is characterized by impa

19 zymes, phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, above the levels in control liver

20 , there was no change in glycogen content or glucose 6-phosphatase activity but increased Slc2a2 gluc

21 ose and [5-3H]glucose, (c) indicating little glucose- 6-phosphatase activity, (b) unchanged low pento

22 albumin expression, and become positive for glucose-6-phosphatase activity (a profile consistent wit

23 phosphate (G6P) transport, causing a loss of glucose-6-phosphatase activity and glucose homeostasis.

24 om ultracentrifugation of cell lysates), the glucose-6-phosphatase activity had a positive correlatio

25 f hepatic glucose output, have 2.4-fold more glucose-6-phosphatase activity in liver than lean contro

26 that hyperglycemia at basal insulin inhibits glucose-6-phosphatase activity in vivo.

27 volved in the export of glucose and in which glucose-6-phosphatase activity is relatively low.

28 Glucose-6-phosphatase activity was reduced, whereas basa

29 es from liver, which possess a high level of glucose-6-phosphatase activity, were compared with those

30 ude cytosol that affect microsome-associated glucose-6-phosphatase activity.

31 ountin(-) cells did not significantly change glucose-6-phosphatase activity.

32 enous glucose production despite the loss of glucose-6-phosphatase activity.

33 tion in HL1C cells, presumably by decreasing glucose-6-phosphatase activity.

34 duction, which was associated with increased glucose-6-phosphatase activity.

35 coplasmic reticulum for G-6-P independent of glucose-6-phosphatase activity.

36 rted in the literature suggest that G6PC2, a glucose-6-phosphatase almost exclusively expressed in pa

37 Glucose-6-phosphatase alpha (G6Pase) deficiency, also kn

38 (GSD Ia) is caused by autosomal mutations in glucose-6-phosphatase alpha catalytic subunit (G6PC) and

39 ease type-Ia (GSD-Ia) is caused by a lack of glucose-6-phosphatase-alpha (G6Pase-alpha or G6PC) activ

40 Glucose-6-phosphatase-alpha (G6Pase-alpha or G6PC) defic

41 in the endoplasmic reticulum (ER)-associated glucose-6-phosphatase-alpha (G6Pase-alpha or G6PC) that

42 ither by a liver/kidney/intestine-restricted glucose-6-phosphatase-alpha (G6Pase-alpha) or by a ubiqu

43 rks with a liver/kidney/intestine-restricted glucose-6-phosphatase-alpha (G6Pase-alpha) to maintain g

44 Glucose-6-phosphatase-alpha (G6Pase-alpha), which facili

45 iews held that there was a single ER enzyme, glucose-6-phosphatase-alpha (G6Pase-alpha), whose activi

46 ing a wide range (0.9-63%) of normal hepatic glucose-6-phosphatase-alpha activity maintain glucose ho

47 tients, deficient in the G6PC1 gene encoding glucose-6-phosphatase-alpha, lack blood glucose control,

48 p in hepatic gluconeogenesis is catalyzed by glucose-6-phosphatase, an enzyme activity residing in th

49 It is caused by the deficiency of glucose-6-phosphatase, an enzyme which catalyses the fin

50 on activates transcription of genes encoding glucose 6-phosphatase and enzymes for glycolysis and lip

51 an upregulation of the gluconeogenic enzymes glucose-6 phosphatase and phosphoenolpyruvate carboxykin

52 Similar regulation was demonstrated using glucose-6-phosphatase and alpha-fibrinogen promoters, in

53 related (50% overall identity) to the liver glucose-6-phosphatase and exhibited similar predicted tr

54 Hence, the surge of glucose-6-phosphatase and fructose-1,6-diphosphatase at

55 Glucose-6-phosphatase and fructose-1,6-diphosphatase, tw

56 n of the known FoxO transcriptional targets, glucose-6-phosphatase and growth arrest and DNA damage p

57 focus on the short- and long-term regulation glucose-6-phosphatase and its substrate cycle counter-pa

58 controls, transplanted cells showed greater glucose-6-phosphatase and lesser glycogen content in per

59 d by the decrease in gene expression of both glucose-6-phosphatase and PEPCK and by physiological hyp

60 xample, the expression of two hepatic genes, glucose-6-phosphatase and PEPCK, is normally inhibited b

61 and activities of the gluconeogenic enzymes glucose-6-phosphatase and phosphoenolpyruvate carboxykin

62 ss the expression of the gluconeogenic genes glucose-6-phosphatase and phosphoenolpyruvate carboxykin

63 1 and activation of key gluconeogenic genes, glucose-6-phosphatase and phosphoenolpyruvate carboxykin

64 ion of the key hepatic gluconeogenic enzymes glucose-6-phosphatase and phosphoenolpyruvate carboxykin

65 -regulation of the key gluconeogenic enzymes glucose-6-phosphatase and phosphoenolpyruvate carboxykin

66 d higher hepatic mRNA levels for the enzymes glucose-6-phosphatase and phosphoenolpyruvate carboxykin

67 r gene as well as FoxO1 target genes such as glucose-6-phosphatase and phosphoenolpyruvate carboxykin

68 ta cell function, including the induction of glucose-6-phosphatase and suppression of GLUT2, glucokin

69 he mRNA expression of gluconeogenic enzymes, glucose-6-phosphatase and the cytosolic form of phosphoe

70 oxOs (L-FoxO1,3,4) prevents the induction of glucose-6-phosphatase and the repression of glucokinase

71 CK (phosphoenolpyruvate carboxykinase), G6P (glucose-6-phosphatase), and certain mitochondrial genes

72 mice, hepatic expression of Spot 14, Bcl-3, glucose 6-phosphatase, and 5'-deiodinase mRNA was higher

73 luding phosphoenolpyruvate carboxykinase and glucose-6-phosphatase, and also activates the expression

74 ession of phosphoenolpyruvate carboxykinase, glucose-6-phosphatase, and fatty acid synthase in ob/ob

75 enzymes, phosphoenolpyruvate carboxykinase, glucose-6-phosphatase, and fructose 1,6-bisphosphatase,

76 glucose production (HGP) enzymes, PEPCK and glucose-6-phosphatase, and increased glycogen levels und

77 f phosphoenolpyruvate carboxykinase (PEPCK), glucose-6-phosphatase, and peroxisome proliferator-activ

78 , whereas phosphoenolpyruvate carboxykinase, glucose-6-phosphatase, and proliferator-activated recept

79 oxykinase (PEPCK), pyruvate carboxylase, and glucose-6-phosphatase, and the neonate's pools of glucon

80 tal glucose output (TGO), i.e., flux through glucose-6-phosphatase, and the rate of glucose cycling i

81 Inhibiting glucose-6-phosphatase, another fructose-responsive gene,

82 glucokinase and to inhibit the flux through glucose-6-phosphatase are impaired in DM2.

83 Glucose-6-phosphatase-beta (G6Pase-beta or G6PC3) defici

84 ies in the endoplasmic reticulum (ER) enzyme glucose-6-phosphatase-beta (G6Pase-beta or G6PC3) that c

85 ly, we showed G6PT interacts with the enzyme glucose-6-phosphatase-beta (G6Pase-beta) to regulate the

86 a ubiquitously expressed Glc-6-P hydrolase, glucose-6-phosphatase-beta (Glc-6-Pase-beta), that can c

87 In males, glucose-6-phosphatase-beta responses to hypoglycemia wer

88 G6PC3 (or glucose-6-phosphatase-beta) deficiency underlies a conge

89 nic NOD mice that overexpress islet-specific glucose 6 phosphatase catalytic subunit-related protein

90 t the pancreatic autoantigen, islet-specific glucose-6 phosphatase catalytic subunit-related protein

91 Because overexpression of the glucose-6-phosphatase catalytic subunit (G-6-Pase) in bo

92 HepG2 cells, the maximum repression of basal glucose-6-phosphatase catalytic subunit (G6Pase) gene tr

93 Mutations in the glucose-6-phosphatase catalytic subunit (G6Pase) give ri

94 Transcription of the gene encoding the glucose-6-phosphatase catalytic subunit (G6Pase) is stim

95 on expression of the gene encoding the mouse glucose-6-phosphatase catalytic subunit (G6Pase), the li

96 born error of metabolism caused by defective glucose-6-phosphatase catalytic subunit (G6PC) activity.

97 sion of two insulin signaling-related genes, glucose-6-phosphatase catalytic subunit (G6pc) and insul

98 regulate gluconeogenic genes, including the glucose-6-phosphatase catalytic subunit (G6Pc) and phosp

99 enolpyruvate carboxykinase 1 (PCK1), and the glucose-6-phosphatase catalytic subunit (G6PC).

100 Glucose-6-phosphatase catalytic subunit (G6PC)1 and G6PC

101 Glucose-6-phosphatase catalytic subunit 1 (G6PC1) plays

102 he rs563694 SNP is located between the genes glucose-6-phosphatase catalytic subunit 2 (G6PC2) and AT

103 Genetic variation at the glucose-6-phosphatase catalytic subunit 2 (G6PC2) locus,

104 Glucokinase (GCK) and glucose-6-phosphatase catalytic subunit 2 (G6PC2) regula

105 predominantly expressed in islets, encodes a glucose-6-phosphatase catalytic subunit that converts gl

106 ncreatic islet beta-cells where it encodes a glucose-6-phosphatase catalytic subunit that modulates t

107 IGRP is likely the authentic islet-specific glucose-6-phosphatase catalytic subunit, and selective i

108 G6PC2 gene, which encodes an islet-specific glucose-6-phosphatase catalytic subunit, is the most imp

109 n downregulation and subsequent increases in glucose-6-phosphatase catalytic subunit-2 (G6PC2) levels

110 parable with the frequency of islet-specific glucose-6-phosphatase catalytic subunit-related protein

111 Islet-specific glucose-6-phosphatase catalytic subunit-related protein

112 Islet-specific glucose-6-phosphatase catalytic subunit-related protein

113 Islet-specific glucose-6-phosphatase catalytic subunit-related protein

114 oid polypeptide (ppIAPP), and islet-specific glucose-6-phosphatase catalytic subunit-related protein

115 CD8+ T cells specific for an islet-specific glucose-6-phosphatase catalytic subunit-related protein

116 reported the discovery of an islet-specific glucose-6-phosphatase catalytic subunit-related protein

117 Islet-specific glucose-6-phosphatase catalytic subunit-related protein

118 in nonobese diabetic mice is islet-specific glucose-6-phosphatase catalytic subunit-related protein

119 , an inability to cross-prime islet-specific glucose-6-phosphatase catalytic subunit-related protein

120 eta-cell-specific autoantigen islet-specific glucose-6-phosphatase catalytic subunit-related protein

121 idated the natural history of islet-specific glucose-6-phosphatase catalytic subunit-related protein

122 monitored the recruitment of islet-specific glucose-6-phosphatase catalytic subunit-related protein

123 (d)-restricted T-cell epitope islet-specific glucose-6-phosphatase catalytic subunit-related protein

124 targeting residues 206-214 of islet-specific glucose-6-phosphatase catalytic subunit-related protein

125 Islet-specific glucose-6-phosphatase catalytic subunit-related protein

126 y linked peptide derived from islet-specific glucose-6-phosphatase catalytic subunit-related protein

127 A(2-10) and INS1 B(5-14)) and islet-specific glucose-6-phosphatase catalytic subunit-related protein

128 -coupled tetramers can delete islet-specific glucose-6-phosphatase catalytic subunit-related protein

129 y CD8(+) T cells specific for islet-specific glucose-6-phosphatase catalytic subunit-related protein(

130 nd all other autoreactive non-islet-specific glucose-6-phosphatase catalytic subunit-related protein(

131 ognizing autoantigens such as islet-specific glucose-6-phosphatase catalytic subunit-related protein,

132 3 are known to be insulin and islet-specific glucose-6-phosphatase catalytic subunit-related protein,

133 a production and expansion of islet-specific glucose-6-phosphatase catalytic subunit-related protein-

134 CD4(+) and CD8(+) T cells, and frequency of glucose-6-phosphatase catalytic subunit-related protein-

135 let-specific, endoplasmic reticulum-resident glucose-6-phosphatase catalytic subunit.

136 hosphoenolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase, catalytic (G6Pc).

137 In liver, glucose-6-phosphatase catalyzes the hydrolysis of glucos

138 Glucose-6-phosphatase catalyzes the hydrolysis of glucos

139 The substrate cycle enzyme glucose-6-phosphatase catalyzes the terminal step in bot

140 Glucose-6-phosphatase catalyzes the terminal step in the

141 Deficiency of G6PC3, a glucose-6-phosphatase, causes a rare multisystem syndrom

142 rocess of glucose output is catalyzed by the glucose-6-phosphatase complex.

143 tic conditions, such as sickle-cell disease, glucose-6-phosphatase deficiency, and some other erythro

144 enzymes (glucose dehydrogenase, EC 1.1.1.47; glucose 6-phosphatase, EC 3.1.3.9; glucose phosphate iso

145 Hepatic glucose-6-phosphatase enzymatic activity was increased b

146 phosphate pathway blocked the stimulation of glucose-6-phosphatase expression by glucose but not by x

147 ot exhibit significant differences in HK2 or glucose-6-phosphatase expression from (18)F-FDG-positive

148 Glucose-6-phosphatase expression was the same for Pten(+

149 ucose production rates and hepatic PEPCK and glucose-6-phosphatase expression, which were not suppres

150 osphoenolpyruvate carboxykinase (PEPCK), and glucose-6-phosphatase expression.

151 ance in a FoxO1-dependent manner and induces glucose-6-phosphatase expression.

152 /- 3 micromol x kg(-1) x min(-1)), increased glucose-6-phosphatase flux (150 +/- 11 vs. 58 +/- 8 micr

153 s was accompanied by reduction of the higher glucose-6-phosphatase flux (75 +/- 4 in ZDF-V, 41 +/- 4

154 tion of glycogenolysis, gluconeogenesis, and glucose-6-phosphatase flux.

155 -A), lactate (monocarboxylate) transporters, glucose-6-phosphatase, fructose-1,6-bisphosphatase, 12-l

156 a subset of TRbeta1 target genes, including glucose 6 phosphatase (G-6-Pc), and this is associated w

157 Glucose-6-phosphatase (G-6-Pase) catalyzes the dephospho

158 The activity of glucose-6-phosphatase (G-6-Pase) in isolated rat microso

159 in the gluconeogenic pathway is catalyzed by glucose-6-phosphatase (G-6-Pase).

160 Tissue glucose-6-phosphatase (G6P) and phosphoenolpyruvate carb

161 in the presence of dexamethasone, expressing glucose-6-phosphatase (G6P) and tyrosine amino transfera

162 e fruit fly, one of the gluconeogenic genes, glucose-6-phosphatase (G6P) is exclusively expressed in

163 polyprotein displayed an increased level of glucose-6-phosphatase (G6P) mRNA.

164 hosphoenolpyruvate carboxykinase (Pepck) and glucose-6-phosphatase (G6p).

165 sphoenolpyruvate carboxykinase 1 (Pck-1) and glucose 6-phosphatase (G6Pase) and this effect was absen

166 d metabolic disorder caused by deficiency of glucose 6-phosphatase (G6Pase-a).

167 se," is caused by a deficiency in microsomal glucose-6-phosphatase (G6Pase) activity.

168 ose disposal, arterial glucagon, and hepatic glucose-6-phosphatase (G6Pase) activity/expression in G4

169 transcript levels of key gluconeogenic genes glucose-6-phosphatase (G6Pase) and phosphoenolpyruvate c

170 sed transcription of the gluconeogenic genes glucose-6-phosphatase (G6pase) and phosphoenolpyruvate c

171 ling to decreased transcription of PEPCK and glucose-6-phosphatase (G6Pase) and provides a possible t

172 phosphoenolpyruvate carboxykinase 2 (PEPCK), glucose-6-phosphatase (G6Pase) and suppressed hepatic gl

173 Recent studies have suggested that increased glucose-6-phosphatase (G6Pase) and/or decreased glucokin

174 G6PC2 encodes a glucose-6-phosphatase (G6Pase) catalytic subunit that mo

175 Islet-specific glucose-6-phosphatase (G6Pase) catalytic subunit-related

176 Glucose-6-phosphatase (G6Pase) catalyzes the final step

177 sphate (G6P) is hydrolyzed to glucose by the glucose-6-phosphatase (G6Pase) complex.

178 d expression of the gene encoding the enzyme glucose-6-phosphatase (G6Pase) contributes to the increa

179 Similarly, glucose flux through glucose-6-phosphatase (G6Pase) decreased with Acrp30, wh

180 For example, glucose-6-phosphatase (G6Pase) deficiency in GSD type Ia

181 ling (GC) were responsible for 46 and 51% of glucose-6-phosphatase (G6Pase) flux, respectively.

182 hosphoenolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase (G6Pase) gene expression, however

183 ), fructose-1,6-bisphosphatase (FBPase), and glucose-6-phosphatase (G6Pase) gene transcription, we hy

184 phoenolpyruvate carboxykinase 1 (PEPCK1) and glucose-6-phosphatase (G6Pase) genes, thereby increasing

185 phosphoenolpyruvate carboxylase (PEPCK) and glucose-6-phosphatase (G6Pase) genes.

186 nce of phosphoenolpyruvate carboxykinase and glucose-6-phosphatase (G6Pase) in KO mice further suppor

187 Glucose-6-phosphatase (G6Pase) is a multicomponent syste

188 Glucose-6-phosphatase (G6Pase) is an essential, rate-lim

189 (GFP) by the transthyretin (TTR) promoter or glucose-6-phosphatase (G6Pase) promoter.

190 disease (GSD-1) in patients deficient in the glucose-6-phosphatase (G6Pase) system (e.g. growth retar

191 culum and consisting of a catalytic subunit (glucose-6-phosphatase (G6Pase)) and putative accessory t

192 Glucose-6-phosphatase (G6Pase), a key enzyme in glucose

193 Deficiency of glucose-6-phosphatase (G6Pase), a key enzyme in glucose

194 hyperuricemia, is caused by a deficiency in glucose-6-phosphatase (G6Pase), a key enzyme in glucose

195 The activation of glucose-6-phosphatase (G6Pase), a key enzyme of endogeno

196 disease type 1a is caused by a deficiency in glucose-6-phosphatase (G6Pase), a nine-helical endoplasm

197 growth factor-binding protein 1 (IGFBP1) and glucose-6-phosphatase (G6Pase), activating their express

198 Deficiency of glucose-6-phosphatase (G6Pase), an endoplasmic reticulum

199 sion of many hepatic genes, including PEPCK, glucose-6-phosphatase (G6Pase), and glucose-6-phosphate

200 osphoenolpyruvate carboxykinase (PEPCK), and glucose-6-phosphatase (G6Pase), and NAD(+) levels, and i

201 f the gene encoding the catalytic subunit of glucose-6-phosphatase (G6Pase), G6Pase-chloramphenicol a

202 Deficiency of microsomal glucose-6-phosphatase (G6Pase), the key enzyme in glucos

203 The gene for glucose-6-phosphatase (G6Pase), the key enzyme in glucos

204 -1a) is caused by a deficiency in microsomal glucose-6-phosphatase (G6Pase), the key enzyme in glucos

205 t expression of the key gluconeogenic enzyme glucose-6-phosphatase (G6pase).

206 se (GGT, a marker of fetal hepatoblasts) and glucose-6-phosphatase (G6Pase, a marker of mature hepato

207 pression of the hepatic gluconeogenic genes (glucose-6-phosphatase [G6Pase] and PEPCK) contributes to

208 osphoenolpyruvate carboxykinase 1 (PCK1) and glucose-6 phosphatase (G6PC) as well as glucose producti

209 Notch activation positively correlates with glucose-6-phosphatase (G6PC) and phosphoenolpyruvate car

210 IT repressed the liver expression of glucose-6-phosphatase (G6PC) and phosphoenolpyruvate car

211 ncreased expression of gluconeogenic enzymes glucose-6-phosphatase (G6PC) and phosphoenolpyruvate car

212 (Insr(P1195L/+)/HFD mice) revealed increased glucose-6-phosphatase (G6pc) expression in liver and inc

213 of glycolytic and lipogenic genes as well as glucose-6-phosphatase (G6pc) that was associated with th

214 phosphoenolpyruvate carboxykinase (PCK1) and glucose-6-phosphatase (G6PC), key regulatory enzymes of

215 n of alpha-fetoprotein (AFP), Albumin (Alb), Glucose-6-phosphatase (G6Pc), SRY (sex determining regio

216 phosphoenolpyruvate carboxykinase (PCK1) and glucose-6-phosphatase (G6PC).

217 sed by mutations in the catalytic subunit of glucose-6 phosphatase (G6PC1).

218 egr-1, C/EBPalpha), liver-specific enzymes (glucose-6-phosphatase [G6Phase], and secreted factors (i

219 l found in primary hepatocytes and increases glucose-6-phosphatase gene expression by 21-fold.

220 ersely, phlorizin failed to decrease hepatic glucose-6-phosphatase gene expression in diabetic rats w

221 nic and glycolytic pathways, also stimulated glucose-6-phosphatase gene expression in Fao cells.

222 sly reported inhibitory effect of insulin on glucose-6-phosphatase gene expression in these cells.

223 to 2.2 +/- 0.33 arbitrary units of mRNA) in glucose-6-phosphatase gene expression with a concomitant

224 The rate of transcription of the glucose-6-phosphatase gene increased about 3-fold in hep

225 how glucose regulates the expression of the glucose-6-phosphatase gene, the effect of glucose was st

226 orticoid-induced expression of the PEPCK and glucose-6-phosphatase genes in H4IIE hepatoma cells.

227 the promoter activity and expression of both glucose-6-phosphatase (Glc-6-P) and phosphoenolpyruvate

228 This property is attributed to elevated glucose-6-phosphatase (Glc-6-Pase) activity.

229 on and marked decreases in the expression of glucose-6-phosphatase (Glc-6-Pase) and phosphoenolpyruva

230 atic expression of the gluconeogenic enzymes glucose-6-phosphatase (Glc-6-Pase) and phosphoenolpyruva

231 rocess of glucose output is catalyzed by the glucose-6-phosphatase (Glc-6-Pase) complex.

232 nesis and glycogenolysis is catalyzed by the glucose-6-phosphatase (Glc-6-Pase) enzyme complex, locat

233 The glucose-6-phosphatase (Glc-6-Pase) family comprises two

234 ms underlying dietary nutrient regulation of glucose-6-phosphatase (Glc-6-Pase) gene expression are n

235 of P-enolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase (Glc-6-Pase) is regulated in respo

236 ticulum where it is hydrolyzed to glucose by glucose-6-phosphatase (Glc-6-Pase).

237 nd S 5627, Ca2+ aggregation had no effect on glucose-6-phosphatase (Glc-6-Pase).

238 Glucose-6-phosphatase (Glu-6-Pase) catalyzes the termina

239 level of the catalytic subunit of rat liver glucose-6-phosphatase (Glu-6-Pase) was regulated by horm

240 1), respectively, while other liver enzymes (glucose-6-phosphatase, glucokinase, and 11beta-hydroxyst

241 nd transcription factors as well as albumin, glucose-6-phosphatase, glycogen synthesis, cytochrome P4

242 NA for PEPCK-C but had no effect on mRNA for glucose-6-phosphatase in AML12 mouse hepatocytes.

243 We find that the activity of glucose-6-phosphatase in crude microsomes from cells wit

244 that repression of the gluconeogenic enzyme glucose-6-phosphatase in HepG2 cells by T0901317 is ROR-

245 ata indicate that in vivo gene expression of glucose-6-phosphatase in the diabetic liver is regulated

246 of neuropeptide Y in the hypothalamus and of glucose-6-phosphatase in the liver following short term

247 he protein level of the catalytic subunit of glucose-6-phosphatase in the liver.

248 ity) significantly increased the activity of glucose-6-phosphatase in wild-type microsomes by decreas

249 ype cells strongly repressed the activity of glucose-6-phosphatase in wild-type microsomes, whereas S

250 We investigated glucose-6-phosphatase-independent endogenous glucose pro

251 mic reticulum lumen where the active site of glucose 6-phosphatase is situated.

252 D-Glucose-6-phosphatase is a key regulator of endogenous g

253 Glucose-6-phosphatase is a multicomponent system that ca

254 Glucose-6-phosphatase is associated with microsomes in b

255 urprisingly found that endoplasmic reticulum glucose-6-phosphatase is present in human embryonic and

256 te G6P in the liver, that is, liver-specific glucose-6-phosphatase knockout (L-G6pc(-/-) ) mice, and

257 hosphoenolpyruvate carboxykinase (PEPCK) and glucose-6-phosphatase, leading to increased glucose outp

258 A homolog of liver glucose-6-phosphatase (LG-6-Pase) specifically expressed

259 ed suppression of the mRNA expression of the glucose 6-phosphatase, manganese superoxide dismutase, a

260 suric agent phlorizin normalized the hepatic glucose-6-phosphatase messenger RNA and protein within a

261 ne-independent fructose-induced increases in glucose-6-phosphatase mRNA abundance, suggesting that it

262 here was a concomitant reduced expression of glucose-6-phosphatase mRNA and glucose production from p

263 Glucose specifically increases glucose-6-phosphatase mRNA and L-type pyruvate kinase mR

264 esults in a metabolic pattern that increases glucose-6-phosphatase mRNA and results in a selective de

265 overexpression of the c-Myc protein induced glucose-6-phosphatase mRNA in the absence of glucose sti

266 Glucose-6-phosphatase mRNA levels increased about 10-fol

267 ated induction of L-type pyruvate kinase and glucose-6-phosphatase mRNA levels was diminished by mane

268 PEPCK and glucose-6-phosphatase mRNA levels were increased at leas

269 erived cell line, Fao, glucose increases the glucose-6-phosphatase mRNA only modestly (3-fold).

270 roduction nor does it change the response of glucose-6-phosphatase mRNA to glucose.

271 eaction, dramatically increases the level of glucose-6-phosphatase mRNA transcripts in primary hepato

272 The half-life of glucose-6-phosphatase mRNA was estimated to be 90 min in

273 downregulation of glucose transporter-1 and glucose-6-phosphatase mRNA, and hepatocyte proliferation

274 The steady-state levels of PEPCK and glucose-6-phosphatase mRNAs were elevated in livers of T

275 uction of the mRNA for the catalytic unit of glucose-6-phosphatase occurs by transcriptional and post

276 is mild, indicating that G6Pase is the major glucose-6-phosphatase of physiological importance for gl

277 in for 16 h did not affect the activities of glucose-6-phosphatase or glucokinase or the activation s

278 y HNF-1beta of the key gluconeogenic enzymes glucose-6-phosphatase or PEPCK.

279 sphate into glycogen rather than through the glucose-6-phosphatase pathway.

280 Fbp1 encoding the key gluconeogenic enzymes glucose-6-phosphatase, phosphoenolpyruvate carboxykinase

281 Analysis of the glucose-6-phosphatase promoter indicates a key role for

282 Glucose, the product of the glucose-6-phosphatase reaction, dramatically increases t

283 hat the previously identified islet-specific glucose-6-phosphatase-related protein (IGRP) is indeed t

284 A pancreatic islet-specific glucose-6-phosphatase-related protein (IGRP) was cloned

285 pertoire for reactivity to the islet antigen glucose-6-phosphatase-related protein (IGRP).

286 hase, phosphoenolpyruvate carboxykinase, and glucose-6-phosphatase remained at normal levels.

287 e disease (GSD) is caused by a deficiency of glucose-6-phosphatase resulting in severe fasting hypogl

288 Whereas the liver glucose-6-phosphatase showed activity in these transfect

289 A-specific CD4(+) T cells and islet specific glucose-6-phosphatase-specific CD8(+) T cells were signi

290 ch as lactate dehydrogenase-A, hexokinase I, glucose-6-phosphatase, stress genes (heme oxygenase-1, A

291 sors contain other protein components of the glucose-6-phosphatase system, ie, the phosphate and gluc

292 sphorylation and increased the expression of glucose-6-phosphatase, the enzyme regulating glucose out

293 sma glucose by 50% and reduced PEPCK, GLUT2, glucose-6-phosphatase, tyrosine aminotransferase, CRP, a

294 nd 10 were expressed in MCF-7 cells, whereas glucose-6-phosphatase was absent.

295 expression of glucose transporters, HKs, and glucose-6-phosphatase was determined using microarray te

296 basal mRNA levels for L-pyruvate kinase and glucose-6-phosphatase were not altered to any significan

297 orm of phosphoenolpyruvate carboxykinase and glucose-6-phosphatase were reduced, transcription of the

298 uch as phosphoenolpyruvate carboxykinase and glucose-6-phosphatase when HNF4alpha is absent.

299 tical mRNA expression and enzyme activity of glucose-6-phosphatase, which catalyzes the final step of

300 and for evaluating "candidate" genes such as glucose-6-phosphatase, which may contribute to developme