ライフサイエンスコーパス: CYP1A2

1 tested (CYP2C19, CYP2C9, CYP2B6, CYP3A5, and CYP1A2).

2 metabolism (i.e. cytochrome P450 [CYP] 3A4, CYP1A2).

3 ect on levels of hepatic cytochrome P4501A2 (CYP1A2).

4 cytochrome P450 (CYP) isoenzymes, including CYP1A2.

5 dentify a novel TCDD-responsive enhancer for CYP1A2.

6 ot significantly affected by the addition of CYP1A2.

7 epatic 5-aminolevulinate synthase (ALAS) and CYP1A2.

8 ice have about twice the wild-type levels of CYP1A2.

9 bon receptor and its target genes CYP1A1 and CYP1A2.

10 60-fold genetic differences in hepatic basal CYP1A2.

11 ciated with the enzyme activities of NAT2 or CYP1A2.

12 y baculovirus-expressed human CYP1A1 but not CYP1A2.

13 of cytochrome P450, particularly CYP1A1 and CYP1A2.

14 CYP1A1 followed by remaining amino acids of CYP1A2.

15 nd mediator 1 (MED1), two transactivators of Cyp1a2.

16 e metabolism by the simple system containing CYP1A2.

17 YO5A, TYRP1, AIM, DCT, and TYR genes and the CYP1A2-15q22-ter, CYP1B1-2p21, CYP2C8-10q23, CYP2C9-10q2

18 50 1 wild-type, Cyp1a2(-/-), Cyp1b1(-/-), or Cyp1a2/1b1(-/-) knockouts, and mice with Cyp1a1 expressi

19 /*1: 8.97; CI: 3.34-24.10; P<0.0001) and the CYP1A2*1C allele (adjusted HR for *1/*1C versus *1/*1: 1

20 common among black carriers of CYP2C19*17 or CYP1A2*1C.

21 from the single nucleotide variant rs762551 (CYP1A2*1F).

22 reconstituted systems were prepared: 1) CPR.CYP1A2, 2) CPR.CYP2B4, 3) a mixture of CPR.CYP1A2 vesicl

23 CYP2C19, and CYP3A5 were also detected while CYP1A2, 2A6, and 2C8 were below limits of detection.

24 containing a phenolic group, five isoforms (CYP1A2, 2B6, 2D6, 2E1, and 3A4) supported ortho hydroxyl

25 of chicory root decreased the expression of CYP1A2, 2C33, 2D25 and 3A29 at high concentrations.

26 monstrates that two AhR binding sites in the CYP1A2 3' region are occupied in TCDD-treated cells.

27 AhR also binds to the CYP1A2 3' region in TCDD-treated LS180 cells but not in

28 In the latter cell lines, the CYP1A2 3' region is extensively methylated.

29 Wild type (WT), Cyp1a1-/- and Cyp1a2-/- (8-10 wk, C57BL/6J background) mice were expos

30 Decreased genotype-predicted CYP2C19 and CYP1A2 activities were associated with higher pneumonia

31 On days 5 and 12, hepatic CYP3A4 and CYP1A2 activities were measured and colon biopsies were

32 metabolism was significantly inhibited, and CYP1A2 activities were stimulated by the presence of the

33 NA adducts measured on day 11 and both liver CYP1A2 activity (P = 0.027) and enterocyte CYP1A1 protei

34 Because CYP1A2 activity has been shown to vary up to 60-fold amo

35 irst evidence supporting a critical role for CYP1A2 activity in the disposition of the drug in vivo.

36 disposition are more strongly influenced by CYP1A2 activity than are those of PhIP.

37 dence interval: 1.07, 1.37), suggesting that CYP1A2 activity, and not the absolute levels of paraxant

38 ts, we proposed that a convenient measure of CYP1A2 activity, the [(13)C 3-methyl] caffeine breath te

39 bolites) in urine was associated with higher CYP1A2 activity, whereas total PhIP (unmetabolized plus

40 nterval (CI) 0.28-3.04) compared with higher CYP1A2 activity.

41 onjugated) in urine showed no association to CYP1A2 activity.

42 Our data suggest that CYP1a2 affects OR activation by converting acetophenone

43 gh ionic strength, consistent with a loss in CYP1A2 affinity for CYP2B4.

44 lar dialysis with the P450 antibody anti-rat CYP1A2 also significantly reduced cardiac ICa.

45 P-450 isoforms in the liver (i.e., CYP1A2 and 4A1) were determined using reverse transcript

46 Approximately 73% of CYP1A2 and 68% of CPR resided in DRM fractions, compared

47 associations between SNPs in AHR and CYP1A1-CYP1A2 and caffeine and coffee consumption from GWASs in

48 These findings suggest that CYP1A2 and CPR reside in ER-DRMs and that the unique lip

49 onal similarities and differences with human CYP1A2 and CYP1B1 enzymes, but the structural basis for

50 re used to examine the expression of CYP1A1, CYP1A2 and CYP1B1 in mouse liver.

51 In contrast, both CYP1A2 and CYP1B1 mRNA, constitutively expressed at low

52 Tetrapod cytochrome P4501 family (CYP1A1, CYP1A2 and CYP1B1) enzymes are most active in hydroxylat

53 t pathway(s) can be involved in induction of CYP1A2 and CYP1B1.

54 2B6, 2C8, 2C9, 2D6, and 2E1) examined, only CYP1A2 and CYP2B6 could catalyze ortho hydroxylation of

55 In rats, the mixed inhibition of CYP1A2 and CYP2D1, and competitive inhibition for CYP2B1

56 vated IRE1alpha suppressed the expression of Cyp1a2 and Cyp2e1 in WT, but not IRE1alpha-deficient mou

57 activation in the liver, leading to RIDD of Cyp1a2 and Cyp2e1 mRNAs, reduced JNK activation, and pro

58 e expression of two cytochrome P450 enzymes, CYP1A2 and CYP2E1, was almost completely abolished in li

59 f phase I detoxification genes revealed that CYP1A2 and CYP3A11 were up-regulated in wild-type mice b

60 Additionally iPSC-derived HE supported both CYP1A2 and CYP3A4 metabolism, which is essential for dru

61 ound that NAFLD-mSI had higher expression of CYP1A2 and CYP3A4, which alleviate hepatic steatosis thr

62 raction between miR-122 and the 3'UTR of the CYP1A2 and CYP3A4.

63 on-treated Cyp1a2(-/-) knockout mouse has no CYP1A2 and exhibits no detectable uroporphyrin accumulat

64 development of uroporphyria as a function of CYP1A2 and iron levels in the liver of mice having a com

65 closely related cytochrome P450s CYP1A1 and CYP1A2 and is structurally and functionally similar to t

66 Cigarette smoking induces CYP1A2 and may, therefore, enhance the conversion of clo

67 lications for disease-association studies in CYP1A2 and other genes.

68 uced teratogenesis, we compared Cyp1a1(-/-), Cyp1a2(-/-), and Cyp1b1(-/-) knock-out mice with Cyp1(+/

69 several SNPs at 7p21 (near AHR), 15q24 (near CYP1A2) and 19q13.2 (near CYP2A6) met GW-significance (P

70 imarily bioactivated by cytochrome P450 1A2 (CYP1A2) and 3A4 to a genotoxic epoxide that forms N7-gua

71 The enzymes cytochrome P4501A2 (CYP1A2) and N-acetyltransferase (NAT2) are principally i

72 for a physical interaction between P450 1A2 (CYP1A2) and P450 2B4 (CYP2B4), by determining if the int

73 ved in pharmacokinetics (ABCG2, AHR, POR and CYP1A2) and pharmacodynamics (BDNF and SLC6A4) of caffei

74 ffeine is detoxified by cytochrome P450 1A2 (CYP1A2), and genetic variation in CYP1A2 impacts the rat

75 ,3',4,4',5-pentachlorbiphenyl, an inducer of CYP1A2, and 5-aminolevulinic acid.

76 olism-associated genes (eg, SEC14L6, ELOVL3, CYP1A2, and AKR1D1).

77 activation induces the expression of CYP2E1, CYP1A2, and aryl hydrocarbon receptor, but not of CYP3A4

78 human microsomes, by recombinant CYP1A1 and CYP1A2, and by sensitive human tumor cell lines to speci

79 The mammalian CYP1A1, CYP1A2, and CYP1B1 genes (encoding cytochromes P450 1A1,

80 The Cyp1a1, Cyp1a2, and Cyp1b1 genes are up-regulated by the aryl hy

81 Finally, deletion of the Cyp1a1, Cyp1a2, and Cyp1b1 in triple knockout mice resulted in r

82 d messenger RNA (mRNA) expression of CYP1A1, CYP1A2, and CYP1B1.

83 idence for a physical interaction among CPR, CYP1A2, and CYP2B4 was provided by cross-linking with bi

84 rved as a lack of glutamine synthetase (GS), Cyp1a2, and Cyp2e1.

85 cytochromes P450, including CYP1A1, CYP1B1, CYP1A2, and CYP3A4, were also able to epoxidize BaP-7,8-

86 carbinols are the only metabolites formed by CYP1A2, and substantial (70-80%) incorporation of oxygen

87 udy showed that the expression of CYP1A1 and CYP1A2 are cell specific and CYP2E1 and GSTM1 may not pl

88 The human CYP1A genes CYP1A1 and CYP1A2 are in a head-to-head orientation on chromosome 1

89 CYP3A4, CYP2D6, CYP2C9, CYP2C19, CYP2E1, and CYP1A2 are responsible for the oxidative metabolism of m

90 ous for the targeted Cyp1a2 gene, designated Cyp1a2(-/-), are completely viable and fertile; histolog

91 man orthologues of dCYP1A2, we confirm human CYP1A2 as a PCB 28 metabolizing enzyme.

92 H-bonding and/or geometric fit of ArNH(2) to CYP1A2 as well as feasibility of both proton abstraction

93 among those with the AC and CC genotypes of CYP1A2 at rs762551 associated with slow caffeine metabol

94 stribution of positively charged residues in CYP1A2 (AVR) and negatively charged phospholipids was hi

95 rocal substitution of three amino acids from CYP1A2 (AVR) into CYP1A1 resulted in a partial redistrib

96 metabolism through greater efficiency in CPR-CYP1A2 binding.

97 yl-8-methylxanthines are good substrates for CYP1A2 but are not themselves inactivating agents.

98 se data indicate that maternal mouse hepatic CYP1A2, by sequestering dioxin and thus altering the pha

99 e rate of the putative rate-limiting step of CYP1A2 catalysis, abstraction of a hydrogen radical from

100 a single liver enzyme, cytochrome P450 1A2 (CYP1A2), catalyzes the major route of metabolism and eli

101 Previously, a CYP1A2 chimera containing the first 109 amino acids of C

102 of CYP1A2 was higher than that of the CYP1A1-CYP1A2 chimera containing the N-terminal end of CYP1A1 w

103 Thus, CYP1A2 chimeras containing substitutions from homologous

104 The POR*CYP1A2 complex was readily disrupted by the addition of

105 th, consistent with disruption of the CYP2B4-CYP1A2 complex.

106 ionic strength was measured as a function of CYP1A2 concentration, a shift to the right in the inflec

107 In addition, intact CYP1A2 containing a 206-302-residue peptide segment of C

108 CYP1A2, containing the N-terminal regions from CYP1A1, n

109 2(+/-) mice contain about 60% of the hepatic CYP1A2 content of Cyp1a2(+/+) mice, and the PCB126-pretr

110 both the variants with selection signals at CYP1A2-CSK (p = 1.10 x 10(-19)) and the variants with an

111 R, AGR3-AHR, ADH1B, ALDH1B1, ALDH1A1, ALDH2, CYP1A2-CSK and ADORA2A-AS1) for 13 dietary traits (P < 3

112 of recent selection at two additional loci: CYP1A2-CSK and F12.

113 (BRET), HO-1 formed HO-1*P450 complexes with CYP1A2, CYP1A1, and CYP2D6, but not all P450s.

114 Cytochrome P450 1 wild-type, Cyp1a2(-/-), Cyp1b1(-/-), or Cyp1a2/1b1(-/-) knockouts,

115 drocarbon hydroxylase (Ah) receptor (Cyp1a1, Cyp1a2, Cyp1b1, and Nqo1).

116 in genes involved in HCA metabolism (CYP1A1, CYP1A2, CYP1B1, GSTA1, GSTM1, GSTM3, GSTP1, NAT1, NAT2,

117 ription of multiple genes, including CYP1A1, CYP1A2, CYP1B1, UGT1A1, UGT1A6, IL6, and SAA1.

118 or and MetaDrug software suggested a role of CYP1A2, CYP2A6, CYP2B6, CYP2E1, and CYP3A4 in the metabo

119 In contrast, levels of CYP1A1, CYP1A2, CYP2B1, CYP2J3, CYP4A1, and CYP4A3 were unchange

120 s to investigate the effects of plumbagin on CYP1A2, CYP2B1/6, CYP2C9/11, CYP2D1/6, CYP2E1 and CYP3A2

121 nslocation of CAR as well as inducibility of CYP1A2, CYP2B10, CYP3A11, and CYP7A1 expression.

122 emonstrating that the characteristics of the CYP1A2-CYP2B4 complex are influenced by the substrates p

123 nteraction by examining the potential of the CYP1A2-CYP2B4 complex to be formed by charge-pair intera

124 his study was to characterize the effects of CYP1A2.CYP2B4 complex formation on the rates and efficie

125 , results consistent with the formation of a CYP1A2.CYP2B4 complex in which the CYP1A2 moiety has a h

126 esicles with CPR.CYP2B4 vesicles, and 4) CPR.CYP1A2.CYP2B4 in the same vesicles (ternary system).

127 yme inactivation of additional P450 enzymes (CYP1A2, CYP2C8, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP

128 ed for drug induction studies, where CYP3A4, CYP1A2, CYP2C9, and CYP2C19 inductions were achieved fol

129 Human CYP450 proteins CYP1A2, CYP2C9, CYP2C19, CYP2D6 and CYP3A4 are the major

130 of a panel of hepatic CYP enzymes including CYP1A2, CYP2C9, CYP2C19, CYP2D6, and CYP3A4 and the cruc

131 The oxidation of alpha-thujone by human CYP1A2, CYP2C9, CYP2C19, CYP2D6, CYP2E1, and CYP3A4 occu

132 or nine compounds and their metabolites from CYP1A2, CYP2D6, and CYP3A4 and a mixture of the three P4

133 nzyme genes (such as CYP3A4, CYP2D6, CYP2C9, CYP1A2, CYP2E1 and UGT1A4) in THLE-2 cell microarrays.

134 This process was specific for P-450s CYP1A2, CYP2E1, CYP3A, and CYP4A and was not demonstrate

135 the United States and is primarily caused by CYP1A2-, CYP2E1-, and CYP3A4-driven conversion of APAP i

136 CYP1A2, CYP3A4 and CYP2E1 mRNA levels were decreased, wh

137 ty represent a regulatory response to modify CYP1A2, CYP3A4 and CYP2E1 translation due to cellular st

138 5p in cells suppressed protein expression of CYP1A2, CYP3A4 and CYP2E1.

139 The enzyme CYP1A2 (cytochrome 1A2) is involved in the metabolism of

140 The rapid loss of human CYP1A2 (cytochrome P450 1A2) activity caused by the 8-me

141 Fetuses from Cyp1a2(-/-) dams exhibited a approximately 6-fold increa

142 More dioxin reached the embryos from Cyp1a2(-/-) dams, compared with that from Cyp1(+/+) dams

143 To fetuses carried by Cyp1a2(-/-) dams, however, this dose of dioxin was letha

144 isrupt geometric and/or electrostatic fit to CYP1A2, decrease the acidity of the NH(2) group, destabi

145 lic functions of this enzyme, we developed a CYP1A2-deficient mouse line by homologous recombination

146 Availability of a viable and fertile CYP1A2-deficient mouse line will provide a valuable tool

147 ycles were employed to improve upon potency, CYP1A2-dependent challenges, and in vivo clearance.

148 mice, these results indicate that Cyp1a1 and Cyp1a2 do not play a dominant role in AHR-mediated vascu

149 up-regulation by dioxin, whereas Cyp1a1 and Cyp1a2 do not.

150 and CYP1B1 are well characterized, a similar CYP1A2 enhancer has not been identified.

151 abortions, the unadjusted odds ratio for low CYP1A2 enzyme activity (below the median) was 0.92 (95%

152 ost human P450 enzymes, including CYP1A1 and CYP1A2, exhibit a high preference for estradiol 2-hydrox

153 hyl salicylate was observed in the medium of CYP1a2-expressing cells.

154 alteration of key functional markers such as CYP1A2 expression.

155 , or Ctcf in Mir122(-/-) hepatocytes reduced Cyp1a2 expression.

156 rrelated with upregulation of AHR, MED1, and CYP1A2 expression.

157 These results indicate that HO-1 and CYP1A2 form a stable complex and have mutual effects on

158 CYP1A2 formed a physical complex with HO-1 that was stab

159 As expected, both HO-1 and CYP1A2 formed BRET-detectable complexes with POR.

160 CYP1A2 function was studied in three purified lipid vesi

161 inting with a -211 to +81 probe from the rat CYP1A2 gene and nuclear extracts from rat liver and olfa

162 ssential for transcriptional activity of the CYP1A2 gene in an in vitro transcription assay using nuc

163 le in the tissue-selective expression of the CYP1A2 gene in the liver and olfactory mucosa.

164 Therefore, analysis of the native CYP1A2 gene in these cells can provide insight into its

165 1A1 and CYP1A2 genes in the absence of mouse Cyp1a2 gene), the teratogenic effects of dioxin reverted

166 Mice homozygous for the targeted Cyp1a2 gene, designated Cyp1a2(-/-), are completely viab

167 subfamily, appear unaffected by loss of the Cyp1a2 gene.

168 Mammalian CYP1A1 and CYP1A2 genes appear to have diverged after the evolution

169 genic mouse (expressing the human CYP1A1 and CYP1A2 genes in the absence of mouse Cyp1a2 gene), the t

170 he adaptive up-regulation of both Cyp1a1 and Cyp1a2 genes in vivo.

171 oter region of rat, mouse, rabbit, and human CYP1A2 genes through data base analysis.

172 -kb intergenic region between the Cyp1a1 and Cyp1a2 genes.

173 AHR) and cytochrome P450 1A1 and 1A2 (CYP1A1-CYP1A2) genes that are associated with habitual caffeine

174 CYP1A2 genotype and caffeine-GS were not associated with

175 ect was absolutely dependent on the maternal Cyp1a2 genotype and independent of the embryonic Cyp1a2

176 The aim of this study was to examine if the CYP1A2 genotype or a genetic score for caffeine metaboli

177 s no evidence for an interaction between the CYP1A2 genotype or caffeine-GS and coffee intake with re

178 isk, and whether the association varies with CYP1A2 genotype or caffeine-GS.

179 Coffee intake and CYP1A2 genotype rs762551 were exposures analyzed over a

180 a2 genotype and independent of the embryonic Cyp1a2 genotype.

181 a known substrate for CYP1A2, we studied the Cyp1a2(-/-) genotype by using the zoxazolamine paralysis

182 n the arrays was found in the order CYP1B1 > CYP1A2 > CYP1A1 > CYP2E1 > myoglobin, the same as the or

183 ALA- and iron-treated Cyp1a2(+/-) heterozygote mice accumulated no uroporphyri

184 o the Cyp1a2(+/+) wild-type animals, and the Cyp1a2(+/-) heterozygotes showed an intermediate effect.

185 We compared Cyp1a2(-/-) knockout mice, Cyp1a2(+/-) heterozygotes, Cyp1a2(+/+) wild type, and Cy

186 rat CL(p) = 3.1 mL/min/kg, t(1/2) = 445 min, CYP1A2 IC(50) > 30 muM).

187 P450 1A2 (CYP1A2), and genetic variation in CYP1A2 impacts the rate of caffeine clearance.

188 CYP1A2, we sequenced a 3.7-kb region 5' from CYP1A2 in a diverse collection of 113 individuals from t

189 her protein abundance and enzyme activity of CYP1A2 in male-derived liver microsomes, which leads to

190 activating enzymes cytochrome P-450 (CYP)1A1/CYP1A2 in microsomes and intact HepG2 cells.

191 rchers wishing to define the precise role of CYP1A2 in numerous metabolic and pharmacokinetic process

192 lgus monkey and up to 45-fold for CYP1A1 and CYP1A2 in vitro in rat and human hepatocytes were observ

193 the cytochrome P450 superfamily, CYP1A1 and CYP1A2, in the number of exons (3 versus 7) and chromoso

194 C57BL/6 Hfe(-/-) mice treated with ALA and a CYP1A2 inducer.

195 CYP1A2 inhibition and induction can most likely be attri

196 Studies then focused on the HO-1-CYP1A2 interaction.

197 by cytochrome P450 monooxygenases, primarily CYP1A2, into reactive N-arylhydroxylamines that can lead

198 CYP1A2 is a cytochrome P450 gene that is involved in hum

199 CYP1A2 is a major cytochrome P-450 isoform in the liver

200 The major hepatic P-450 isoform CYP1A2 is down-regulated and inhibition of P-450 enzyme

201 e mechanism of N-hydroxylation of ArNH(2) by CYP1A2 is investigated by density functional theory (DFT

202 Cytochrome P450 1A2 (CYP1A2) is a predominantly hepatic enzyme known to be im

203 the major P-450 isoform in rat liver (i.e., CYP1A2) is down-regulated during the progression of seps

204 The liver enzyme cytochrome P450 1A2 (CYP1A2) is responsible for 90% of caffeine metabolism, w

205 We compared Cyp1a2(-/-) knockout mice, Cyp1a2(+/-) heterozygotes, Cy

206 eviously reported, the ALA- and iron-treated Cyp1a2(-/-) knockout mouse has no CYP1A2 and exhibits no

207 We conclude that small changes in hepatic CYP1A2 levels can dramatically affect uroporphyria in C5

208 that the positive charges of the CYP1A1 and CYP1A2 linker regions between the N termini and catalyti

209 Rabbit CYP1A1 and CYP1A2 localize into disordered and ordered microdomains

210 The Cyp1a1 and Cyp1a2 loci represent linked genes thought to play impor

211 eral genes and inhibition of both CYP3A4 and CYP1A2, matching effects observed with whole clementine

212 However, inhibitor/inducers of CYP3A4 and CYP1A2 may also cause DDI with warfarin.

213 Cytochrome P4501A2 (CYP1A2)-mediated N-hydroxylation followed by phase II O-

214 RET data suggested substantial inhibition of CYP1A2-mediated 7-ethoxyresorufin de-ethylation in the p

215 The results indicate that CYP1A2 messenger RNA expression decreased significantly

216 findings suggest that cytochrome P-450 1A2 (CYP1A2) metabolic activity may be associated with IUGR,

217 ALA- and iron-treated Cyp1a2(+/+) mice are known to accumulate hepatic uroporp

218 Cyp1a2(+/+) mice, and the PCB126-pretreated Cyp1a2(+/+) mice have about twice the wild-type levels o

219 -) heterozygotes, Cyp1a2(+/+) wild type, and Cyp1a2(+/+) mice pretreated with a low dose of 3,3',4,4'

220 e-response curves in ALA- and PCB126-treated Cyp1a2(+/+) mice showed that hepatic iron levels greater

221 n about 60% of the hepatic CYP1A2 content of Cyp1a2(+/+) mice, and the PCB126-pretreated Cyp1a2(+/+)

222 Cyp1a2(+/-) mice contain about 60% of the hepatic CYP1A2

223 y using the zoxazolamine paralysis test: the Cyp1a2(-/-) mice exhibited dramatically lengthened paral

224 fferences in susceptibility of Cyp1a1-/- and Cyp1a2-/- mice to HLI and suggest novel pathways that ne

225 entially regulated between WT, Cyp1a1-/- and Cyp1a2-/- mice.

226 genes unique to Cyp1a1-/- and 119 unique to Cyp1a2-/- mice.

227 e found to be cholesterol-dependent: CPR and CYP1A2 migrated to the more dense regions of the sucrose

228 tion of a CYP1A2.CYP2B4 complex in which the CYP1A2 moiety has a higher affinity for CPR binding.

229 sue, mammary gland, and circulating blood of Cyp1a2(-/-) mothers, compared with that in the Cyp1(+/+)

230 achieved against data on hepatic zonation of CYP1A2 mRNA expression caused by three different doses o

231 In the human prostate cell line RWPE-1, CYP1A2 mRNA expression is dramatically induced by TCDD.

232 me P450 (CYP) enzyme activity and CYP1A1 and CYP1A2 mRNA expression.

233 No CYP1A2 mRNA was detected by Northern blot analysis.

234 Lung CYP2A13, CYP2A6, and CYP2A7 (and CYP1A2) mRNA levels in smokers and nonsmokers were asses

235 lung CYP2A13, CYP2A6, and CYP2A7 (and higher CYP1A2) mRNA.

236 439 administration, the levels of CYP1A1 and CYP1A2 mRNAs peaked at 8 hr and 16 hr, respectively, bef

237 A CYP1A2 mutant with the three amino acids from CYP1A1 (VA

238 ects were phenotyped for cytochrome P4501A2 (CYP1A2), N-acetyltransferase 2, and sulfotransferase 1A1

239 were detected in gel-shift assays using the CYP1A2 NF-1-like element and nuclear extracts from liver

240 icologic studies using individual Cyp1a1 and Cyp1a2 null mice support the observation that up-regulat

241 tract, bile duct, and gall bladder of B6,129 CYP1A2-null and wild-type mice as well as in both sexes

242 ndular stomach were found in 95.7% of female CYP1A2-null mice as well as in 45.7% of female 129S4/SvJ

243 metabolites were present in incubations with CYP1A2 or CYP3A4.

244 No increases in CYP1A2 or other cytochrome P450s were detected in the Hf

245 indicate that biotransformation of MeIQx via CYP1A2 oxidation to form the N-hydroxylamine followed by

246 regions near the CYP17A1 (P = 7 x 10(-24)), CYP1A2 (P = 1 x 10(-23)), FGF5 (P = 1 x 10(-21)), SH2B3

247 ytochrome P450, subfamily 1A, polypeptide 2 (CYP1A2; P = 0.002) and RM compared with TA at AXL recept

248 n ordered domains, whereas the N terminus of CYP1A2 partially directed CYP1A1 into ordered regions.

249 he data showed that individuals with a rapid CYP1A2 phenotype and high levels of urinary N-hydroxy-Ph

250 the N-terminal end and an internal region of CYP1A2 play roles in targeting CYP1A2 to ordered domains

251 Upregulation of Cyp1a2 primary transcript and mRNA in LKO mice correlate

252 ld provides improved metabolic clearance and CYP1A2 profiles compared to previously discovered mGlu(4

253 lline, but not their N7-methyl analogues, by CYP1A2 promotes a major fraction of the inactivating xan

254 these xanthines are bound in a 1:1 ratio to CYP1A2 protein.

255 suggest that a variant occurring within the CYP1A2 region may be conferring an increased risk of lun

256 d to localize to disordered regions, whereas CYP1A2 resided in ordered domains.

257 e SNPs (AHR: rs6968865 and rs4410790; CYP1A1-CYP1A2: rs2472297 and rs2470893) and 6 additional tag SN

258 etic polymorphisms and another restricted to CYP1A2 rs762551 alone, did not reveal any evidence of ef

259 976T > C (ADORA2A; rs5751876) and -163C > A (CYP1A2; rs762551) influence the effect of caffeine on th

260 The objective was to study the effect of CYP1A2, sex, age, and smoking on coffee intake.

261 Among the CYPs tested, co-expression of CYP1a2 significantly affected the responses of various O

262 and p-cresol were inhibited, whereas that of CYP1A2-specific o-cresol was increased, results consiste

263 The commensurate increase in the rate of CYP1A2-specific product formation suggested the P450.P45

264 ional start site and 12.6 kb upstream of the Cyp1a2 start site.

265 ue lipid components of these domains enhance CYP1A2 substrate metabolism through greater efficiency i

266 CYP1A2 substrates include aflatoxin B1, acetaminophen, a

267 Human liver microsomes and CYP1A2 supersomes showed the highest bioactivation rate

268 s noteworthy that we identify a region 3' of CYP1A2 that also binds AhR in response to TCDD.

269 r role by causing a conformational change in CYP1A2 that makes its metabolism more efficient.

270 egulation of cytochrome P4502E1 (CYP2E1) and CYP1A2 that produced the toxic metabolite, N-acetyl-p-be

271 SNP alleles near GCKR, MLXIPL, BDNF and CYP1A2 that were associated with higher coffee consumpti

272 tochrome P450 family 1 subfamily A member 2 (CYP1A2) that convert acetaminophen to highly reactive N-

273 ycle checkpoints were transformed with human CYP1A2 to investigate how these DNA adducts are repaired

274 nal region of CYP1A2 play roles in targeting CYP1A2 to ordered domains, and domain localization may i

275 r a probe drug cocktail (caffeine [probe for CYP1A2], tolbutamide [CYP2C9], dextromethorphan [CYP2D6]

276 and birth defects; substitution of the human CYP1A2 trans-gene provides the same protection.

277 ce in constitutive or ligand-induced CYP1A1; CYP1A2; UDP glucuronosyltransferase 1A2; NAD(P)H dehydro

278 R.CYP1A2, 2) CPR.CYP2B4, 3) a mixture of CPR.CYP1A2 vesicles with CPR.CYP2B4 vesicles, and 4) CPR.CYP

279 tal smoking and birth weight (on MDS2, PBX1, CYP1A2, VPRBP, WBP1L, CD28, and CDK6 genes), and prenata

280 showed that after cross-linking, antibody to CYP1A2 was able to co-immunoprecipitate CYP2B4 but only

281 s from CYP1A1 (VAG) at positions 27 to 29 of CYP1A2 was generated that showed a distribution pattern

282 After expression, the catalytic activity of CYP1A2 was higher than that of the CYP1A1-CYP1A2 chimera

283 owever, when the association between CPR and CYP1A2 was measured, V-ER and V-DRM liposomes produced l

284 The level of hepatic CYP1A2 was unaffected by either AA intake.

285 al selection in shaping genetic diversity in CYP1A2, we sequenced a 3.7-kb region 5' from CYP1A2 in a

286 laxant zoxazolamine is a known substrate for CYP1A2, we studied the Cyp1a2(-/-) genotype by using the

287 Thus, chimeric constructs of CYP1A1 and CYP1A2 were created, and their localization was tested i

288 ealed that the transcriptional activities of CYP1A2 were increased by PBO and ACN treatments.

289 NADPH-cytochrome P450 reductase, CYP2B4, and CYP1A2, where a dramatic inhibition of 7-pentoxyresorufi

290 a functional variant at cytochrome P450 1A2 (CYP1A2), which makes them less effective at metabolizing

291 putational analysis in this region suggested CYP1A2, which metabolizes tobacco-derived carcinogen, as

292 -) knockout mice, Cyp1a2(+/-) heterozygotes, Cyp1a2(+/+) wild type, and Cyp1a2(+/+) mice pretreated w

293 y lengthened paralysis times relative to the Cyp1a2(+/+) wild-type animals, and the Cyp1a2(+/-) heter

294 Metabolic studies employing expressed CYP1A2 with radiolabeled furafylline and a close analogu

295 3A4, but also a non-competitive inhibitor of CYP1A2, with Ki values no more than 2.16 muM.

296 e-metabolizing enzymes--cytochrome P-4501A2 (CYP1A2), xanthine oxidase, and N-acetyltransferase 2--by