ライフサイエンスコーパス: CYP1A2

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

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

3 dentify a novel TCDD-responsive enhancer for CYP1A2.

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

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

6 bon receptor and its target genes CYP1A1 and CYP1A2.

7 60-fold genetic differences in hepatic basal CYP1A2.

8 ciated with the enzyme activities of NAT2 or CYP1A2.

9 y baculovirus-expressed human CYP1A1 but not CYP1A2.

10 of cytochrome P450, particularly CYP1A1 and CYP1A2.

11 e metabolism by the simple system containing CYP1A2.

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

13 cytochrome P450 (CYP) isoenzymes, including CYP1A2.

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

15 50 1 wild-type, Cyp1a2(-/-), Cyp1b1(-/-), or Cyp1a2/1b1(-/-) knockouts, and mice with Cyp1a1 expressi

16 /*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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

49 2B6, 2C8, 2C9, 2D6, and 2E1) examined, only CYP1A2 and CYP2B6 could catalyze ortho hydroxylation of

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

68 ,3',4,4',5-pentachlorbiphenyl, an inducer of CYP1A2, and 5-aminolevulinic acid.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

83 metabolism through greater efficiency in CPR-CYP1A2 binding.

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

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

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

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

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

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

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

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

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

93 2(+/-) mice contain about 60% of the hepatic CYP1A2 content of Cyp1a2(+/+) mice, and the PCB126-pretr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

118 5p in cells suppressed protein expression of CYP1A2, CYP3A4 and CYP2E1.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

135 CYP1A2 function was studied in three purified lipid vesi

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

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

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

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

140 1A1 and CYP1A2 genes in the absence of mouse Cyp1a2 gene), the teratogenic effects of dioxin reverted

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

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

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

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

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

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

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

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

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

150 a2 genotype and independent of the embryonic Cyp1a2 genotype.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

172 The results indicate that CYP1A2 messenger RNA expression decreased significantly

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

190 No CYP1A2 mRNA was detected by Northern blot analysis.

191 439 administration, the levels of CYP1A1 and CYP1A2 mRNAs peaked at 8 hr and 16 hr, respectively, bef

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

216 CYP1A2 substrates include aflatoxin B1, acetaminophen, a

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

240 3A4, but also a non-competitive inhibitor of CYP1A2, with Ki values no more than 2.16 muM.

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