Title : Equine catechol estrogen 4-hydroxyequilenin is a more potent inhibitor of the variant form of catechol-O-methyltransferase.

Pub. Date : 2004 Apr

PMID : 15089093






25 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Equine catechol estrogen 4-hydroxyequilenin is a more potent inhibitor of the variant form of catechol-O-methyltransferase. catechol catechol O-methyltransferase Equus caballus
2 Equine catechol estrogen 4-hydroxyequilenin is a more potent inhibitor of the variant form of catechol-O-methyltransferase. 4-hydroxy-equilenin catechol O-methyltransferase Equus caballus
3 Catechol-O-methyltransferase (COMT) plays an important role in the inactivation of biologically active and toxic catechols. Catechols catechol O-methyltransferase Equus caballus
4 Catechol-O-methyltransferase (COMT) plays an important role in the inactivation of biologically active and toxic catechols. Catechols catechol O-methyltransferase Equus caballus
5 It has been shown that COMT is genetically polymorphic with a wild-type and variant form where a valine has been substituted with a methionine. Valine catechol O-methyltransferase Equus caballus
6 It has been shown that COMT is genetically polymorphic with a wild-type and variant form where a valine has been substituted with a methionine. Methionine catechol O-methyltransferase Equus caballus
7 Previously, we showed that 4-hydroxyequilenin (4-OHEN), a cytotoxic/genotoxic equine catechol estrogen metabolite, is both a substrate of COMT and an irreversible inhibitor of the methylation activity of COMT in vitro. 4-hydroxy-equilenin catechol O-methyltransferase Equus caballus
8 Previously, we showed that 4-hydroxyequilenin (4-OHEN), a cytotoxic/genotoxic equine catechol estrogen metabolite, is both a substrate of COMT and an irreversible inhibitor of the methylation activity of COMT in vitro. 4-hydroxy-equilenin catechol O-methyltransferase Equus caballus
9 Previously, we showed that 4-hydroxyequilenin (4-OHEN), a cytotoxic/genotoxic equine catechol estrogen metabolite, is both a substrate of COMT and an irreversible inhibitor of the methylation activity of COMT in vitro. 4-ohen catechol O-methyltransferase Equus caballus
10 Previously, we showed that 4-hydroxyequilenin (4-OHEN), a cytotoxic/genotoxic equine catechol estrogen metabolite, is both a substrate of COMT and an irreversible inhibitor of the methylation activity of COMT in vitro. 4-ohen catechol O-methyltransferase Equus caballus
11 To further understand the mechanism(s) of the association between the breast cancer risk and the COMT polymorphism, it was of interest to study the effect of the Val/Met polymorphism on COMT-catalyzed catechol estrogen methylation and 4-OHEN-mediated inhibition. Valine catechol O-methyltransferase Equus caballus
12 To further understand the mechanism(s) of the association between the breast cancer risk and the COMT polymorphism, it was of interest to study the effect of the Val/Met polymorphism on COMT-catalyzed catechol estrogen methylation and 4-OHEN-mediated inhibition. Methionine catechol O-methyltransferase Equus caballus
13 To further understand the mechanism(s) of the association between the breast cancer risk and the COMT polymorphism, it was of interest to study the effect of the Val/Met polymorphism on COMT-catalyzed catechol estrogen methylation and 4-OHEN-mediated inhibition. catechol catechol O-methyltransferase Equus caballus
14 To further understand the mechanism(s) of the association between the breast cancer risk and the COMT polymorphism, it was of interest to study the effect of the Val/Met polymorphism on COMT-catalyzed catechol estrogen methylation and 4-OHEN-mediated inhibition. catechol catechol O-methyltransferase Equus caballus
15 To further understand the mechanism(s) of the association between the breast cancer risk and the COMT polymorphism, it was of interest to study the effect of the Val/Met polymorphism on COMT-catalyzed catechol estrogen methylation and 4-OHEN-mediated inhibition. 4-ohen catechol O-methyltransferase Equus caballus
16 However, we found that the COMT variant form was more susceptible to 4-OHEN-mediated irreversible inactivation. 4-ohen catechol O-methyltransferase Equus caballus
17 Electrospray ionization mass spectrometry and SDS-gel analysis of COMT modified by 4-OHEN revealed that inhibition mechanisms include alkylation and/or oxidation of certain amino acids. Sodium Dodecyl Sulfate catechol O-methyltransferase Equus caballus
18 Electrospray ionization mass spectrometry and SDS-gel analysis of COMT modified by 4-OHEN revealed that inhibition mechanisms include alkylation and/or oxidation of certain amino acids. 4-ohen catechol O-methyltransferase Equus caballus
19 Furthermore, thermotropic studies indicated that the variant form was more thermolabile, which suggested that the valine to methionine substitution may have changed the secondary/tertiary structure of the variant form of COMT, making it more susceptible to 4-OHEN and heat inactivation. Valine catechol O-methyltransferase Equus caballus
20 Furthermore, thermotropic studies indicated that the variant form was more thermolabile, which suggested that the valine to methionine substitution may have changed the secondary/tertiary structure of the variant form of COMT, making it more susceptible to 4-OHEN and heat inactivation. Methionine catechol O-methyltransferase Equus caballus
21 Furthermore, thermotropic studies indicated that the variant form was more thermolabile, which suggested that the valine to methionine substitution may have changed the secondary/tertiary structure of the variant form of COMT, making it more susceptible to 4-OHEN and heat inactivation. 4-ohen catechol O-methyltransferase Equus caballus
22 These data suggest that 4-OHEN-mediated inhibition of the variant form of COMT in vivo might affect the detoxification efficiency of endogenous and/or exogenous catechol estrogens and play a role in the association between breast cancer risk and COMT polymorphism. 4-ohen catechol O-methyltransferase Equus caballus
23 These data suggest that 4-OHEN-mediated inhibition of the variant form of COMT in vivo might affect the detoxification efficiency of endogenous and/or exogenous catechol estrogens and play a role in the association between breast cancer risk and COMT polymorphism. 4-ohen catechol O-methyltransferase Equus caballus
24 These data suggest that 4-OHEN-mediated inhibition of the variant form of COMT in vivo might affect the detoxification efficiency of endogenous and/or exogenous catechol estrogens and play a role in the association between breast cancer risk and COMT polymorphism. catechol catechol O-methyltransferase Equus caballus
25 These data suggest that 4-OHEN-mediated inhibition of the variant form of COMT in vivo might affect the detoxification efficiency of endogenous and/or exogenous catechol estrogens and play a role in the association between breast cancer risk and COMT polymorphism. catechol catechol O-methyltransferase Equus caballus