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Volumn 74, Issue 12, 2009, Pages 971-977

Non-steroidal anti-inflammatory drugs interact with testosterone glucuronidation

Author keywords

Epitestosterone; T E ratio; Testosterone; UGT2B17 deletion

Indexed keywords

DICLOFENAC; DIMETHYL SULFOXIDE; DISODIUM HYDROGEN PHOSPHATE; EPITESTOSTERONE; FORMIC ACID; GLUCURONOSYLTRANSFERASE; GLUCURONOSYLTRANSFERASE 1A3; GLUCURONOSYLTRANSFERASE 1A4; GLUCURONOSYLTRANSFERASE 1A9; GLUCURONOSYLTRANSFERASE 2B7; IBUPROFEN; MAGNESIUM CHLORIDE; POTASSIUM DIHYDROGEN PHOSPHATE; RECOMBINANT ENZYME; TESTOSTERONE; TESTOSTERONE GLUCURONIDE; UNCLASSIFIED DRUG;

EID: 69949175584     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2009.07.004     Document Type: Article
Times cited : (39)

References (29)
  • 1
    • 0035038561 scopus 로고    scopus 로고
    • Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of diclofenac
    • King C., Tang W., Ngui J., Tephly T., and Braun M. Characterization of rat and human UDP-glucuronosyltransferases responsible for the in vitro glucuronidation of diclofenac. Toxicol Sci 61 (2001) 49-53
    • (2001) Toxicol Sci , vol.61 , pp. 49-53
    • King, C.1    Tang, W.2    Ngui, J.3    Tephly, T.4    Braun, M.5
  • 2
    • 0034128936 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: metabolism, expression, and disease
    • Tukey R.H., and Strassburg C.P. Human UDP-glucuronosyltransferases: metabolism, expression, and disease. Annu Rev Pharmacol Toxicol 40 (2000) 581-616
    • (2000) Annu Rev Pharmacol Toxicol , vol.40 , pp. 581-616
    • Tukey, R.H.1    Strassburg, C.P.2
  • 5
    • 59649084478 scopus 로고    scopus 로고
    • UDP-glucuronosyltransferases (UGTs) 2B7 and UGT2B17 display converse specificity in testosterone and epitestosterone glucuronidation, whereas UGT2A1 conjugates both androgens similarly
    • Sten T., Bichlmaier I., Kuuranne T., Leinonen A., Yli-Kauhaluoma J., and Finel M. UDP-glucuronosyltransferases (UGTs) 2B7 and UGT2B17 display converse specificity in testosterone and epitestosterone glucuronidation, whereas UGT2A1 conjugates both androgens similarly. Drug Metab Dispos 37 (2009) 417-423
    • (2009) Drug Metab Dispos , vol.37 , pp. 417-423
    • Sten, T.1    Bichlmaier, I.2    Kuuranne, T.3    Leinonen, A.4    Yli-Kauhaluoma, J.5    Finel, M.6
  • 6
    • 32544455635 scopus 로고    scopus 로고
    • Large differences in testosterone excretion in Korean and Swedish men are strongly associated with a UDP-glucuronosyl transferase 2B17 polymorphism
    • Jakobsson J., Ekström L., Inotsume N., Garle M., Lorentzon M., Ohlsson C., et al. Large differences in testosterone excretion in Korean and Swedish men are strongly associated with a UDP-glucuronosyl transferase 2B17 polymorphism. J Clin Endocrinol Metab 91 (2006) 687-693
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 687-693
    • Jakobsson, J.1    Ekström, L.2    Inotsume, N.3    Garle, M.4    Lorentzon, M.5    Ohlsson, C.6
  • 7
    • 33847383675 scopus 로고    scopus 로고
    • The glucuronidation of Delta4-3-Keto C19- and C21-hydroxysteroids by human liver microsomal and recombinant UDP-glucuronosyltransferases (UGTs): 6alpha- and 21-hydroxyprogesterone are selective substrates for UGT2B7
    • Bowalgaha K., Elliot D.J., Mackenzie P.I., Knights K.M., and Miners J.O. The glucuronidation of Delta4-3-Keto C19- and C21-hydroxysteroids by human liver microsomal and recombinant UDP-glucuronosyltransferases (UGTs): 6alpha- and 21-hydroxyprogesterone are selective substrates for UGT2B7. Drug Metab Dispos 35 (2007) 363-370
    • (2007) Drug Metab Dispos , vol.35 , pp. 363-370
    • Bowalgaha, K.1    Elliot, D.J.2    Mackenzie, P.I.3    Knights, K.M.4    Miners, J.O.5
  • 8
    • 0031894377 scopus 로고    scopus 로고
    • The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268)
    • Coffman B.L., King C.D., Rios G.R., and Tephly T.R. The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268). Drug Metab Dispos 26 (1998) 73-77
    • (1998) Drug Metab Dispos , vol.26 , pp. 73-77
    • Coffman, B.L.1    King, C.D.2    Rios, G.R.3    Tephly, T.R.4
  • 9
    • 44449083711 scopus 로고    scopus 로고
    • Genetic aspects of epitestosterone formation and androgen disposition: influence of polymorphisms in CYP17 and UGT2B enzymes
    • Schulze J.J., Lorentzon M., Ohlsson C., Lundmark J., Roh H.K., Rane A., et al. Genetic aspects of epitestosterone formation and androgen disposition: influence of polymorphisms in CYP17 and UGT2B enzymes. Pharmacogenet Genomics 18 (2008) 477-485
    • (2008) Pharmacogenet Genomics , vol.18 , pp. 477-485
    • Schulze, J.J.1    Lorentzon, M.2    Ohlsson, C.3    Lundmark, J.4    Roh, H.K.5    Rane, A.6
  • 10
    • 0002565127 scopus 로고
    • Nachweis von exogenem testosteron
    • Heck H., Hollmann W., Leisen H., and Rost R. (Eds), Deutsche Ärtze-Verlag, Cologne
    • Donike M., Bärwald K.-R., Klostermann K., Schänzer W., and Zimmermann J. Nachweis von exogenem testosteron (The detection of exogenous testosterone). In: Heck H., Hollmann W., Leisen H., and Rost R. (Eds). Sport: Leistung und Gesundheit (1983), Deutsche Ärtze-Verlag, Cologne 292-300
    • (1983) Sport: Leistung und Gesundheit , pp. 292-300
    • Donike, M.1    Bärwald, K.-R.2    Klostermann, K.3    Schänzer, W.4    Zimmermann, J.5
  • 11
    • 69949184563 scopus 로고    scopus 로고
    • WADA. Reporting and evaluation guidance for testosterone, epitestosterone, T/E ratio and other endogenous steroids. Available at http://www.wada-ama.org/rtecontent/document/end_steroids_aug_04.pdf; 2004.
    • WADA. Reporting and evaluation guidance for testosterone, epitestosterone, T/E ratio and other endogenous steroids. Available at http://www.wada-ama.org/rtecontent/document/end_steroids_aug_04.pdf; 2004.
  • 12
    • 47549084086 scopus 로고    scopus 로고
    • Doping test results dependent on genotype of uridine diphospho-glucuronosyl transferase 2B17, the major enzyme for testosterone glucuronidation
    • Schulze J.J., Lundmark J., Garle M., Skilving I., Ekström L., and Rane A. Doping test results dependent on genotype of uridine diphospho-glucuronosyl transferase 2B17, the major enzyme for testosterone glucuronidation. J Clin Endocrinol Metab 93 (2008) 2500-2506
    • (2008) J Clin Endocrinol Metab , vol.93 , pp. 2500-2506
    • Schulze, J.J.1    Lundmark, J.2    Garle, M.3    Skilving, I.4    Ekström, L.5    Rane, A.6
  • 13
    • 34147185182 scopus 로고    scopus 로고
    • Bayesian detection of abnormal values in longitudinal biomarkers with an application to T/E ratio
    • Sottas P.E., Baume N., Saudan C., Schweizer C., Kamber M., and Saugy M. Bayesian detection of abnormal values in longitudinal biomarkers with an application to T/E ratio. Biostatistics 8 (2007) 285-296
    • (2007) Biostatistics , vol.8 , pp. 285-296
    • Sottas, P.E.1    Baume, N.2    Saudan, C.3    Schweizer, C.4    Kamber, M.5    Saugy, M.6
  • 14
    • 69949177242 scopus 로고    scopus 로고
    • Substantial advantage of a combined Bayesian and genotyping approach in testosterone doping tests
    • Schulze J.J., Lundmark J., Garle M., Ekström L., Sottas P.E., and Rane A. Substantial advantage of a combined Bayesian and genotyping approach in testosterone doping tests. Steroids (2008)
    • (2008) Steroids
    • Schulze, J.J.1    Lundmark, J.2    Garle, M.3    Ekström, L.4    Sottas, P.E.5    Rane, A.6
  • 15
    • 22344442057 scopus 로고    scopus 로고
    • Glucuronidation of nonsteroidal anti-inflammatory drugs: identifying the enzymes responsible in human liver microsomes
    • Kuehl G.E., Lampe J.W., Potter J.D., and Bigler J. Glucuronidation of nonsteroidal anti-inflammatory drugs: identifying the enzymes responsible in human liver microsomes. Drug Metab Dispos 33 (2005) 1027-1035
    • (2005) Drug Metab Dispos , vol.33 , pp. 1027-1035
    • Kuehl, G.E.1    Lampe, J.W.2    Potter, J.D.3    Bigler, J.4
  • 16
    • 43949113328 scopus 로고    scopus 로고
    • Use of prescription drugs in athletes
    • Alaranta A., Alaranta H., and Helenius I. Use of prescription drugs in athletes. Sports Med 38 (2008) 449-463
    • (2008) Sports Med , vol.38 , pp. 449-463
    • Alaranta, A.1    Alaranta, H.2    Helenius, I.3
  • 17
    • 0031886547 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of ibuprofen. The first 30 years
    • Davies N.M. Clinical pharmacokinetics of ibuprofen. The first 30 years. Clin Pharmacokinet 34 (1998) 101-154
    • (1998) Clin Pharmacokinet , vol.34 , pp. 101-154
    • Davies, N.M.1
  • 18
    • 0027433317 scopus 로고
    • Complementary deoxyribonucleic acid cloning and expression of a human liver uridine diphosphate-glucuronosyltransferase glucuronidating carboxylic acid-containing drugs
    • Jin C., Miners J.O., Lillywhite K.J., and Mackenzie P.I. Complementary deoxyribonucleic acid cloning and expression of a human liver uridine diphosphate-glucuronosyltransferase glucuronidating carboxylic acid-containing drugs. J Pharmacol Exp Ther 264 (1993) 475-479
    • (1993) J Pharmacol Exp Ther , vol.264 , pp. 475-479
    • Jin, C.1    Miners, J.O.2    Lillywhite, K.J.3    Mackenzie, P.I.4
  • 21
    • 0037423299 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs). UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme
    • Kurkela M., Garcia-Horsman J.A., Luukkanen L., Mörsky S., Taskinen J., Baumann M., et al. Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs). UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme. J Biol Chem 278 (2003) 3536-3544
    • (2003) J Biol Chem , vol.278 , pp. 3536-3544
    • Kurkela, M.1    Garcia-Horsman, J.A.2    Luukkanen, L.3    Mörsky, S.4    Taskinen, J.5    Baumann, M.6
  • 22
    • 33847043537 scopus 로고    scopus 로고
    • Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6
    • Kurkela M., Patana A.S., Mackenzie P.I., Court M.H., Tate C.G., Hirvonen J., et al. Interactions with other human UDP-glucuronosyltransferases attenuate the consequences of the Y485D mutation on the activity and substrate affinity of UGT1A6. Pharmacogenet Genomics 17 (2007) 115-126
    • (2007) Pharmacogenet Genomics , vol.17 , pp. 115-126
    • Kurkela, M.1    Patana, A.S.2    Mackenzie, P.I.3    Court, M.H.4    Tate, C.G.5    Hirvonen, J.6
  • 23
    • 0034094062 scopus 로고    scopus 로고
    • Determination of the kinetics of rat UDP-glucuronosyltransferases (UGTs) in liver and intestine using HPLC
    • Narayanan R., LeDuc B., and Williams D.A. Determination of the kinetics of rat UDP-glucuronosyltransferases (UGTs) in liver and intestine using HPLC. J Pharm Biomed Anal 22 (2000) 527-540
    • (2000) J Pharm Biomed Anal , vol.22 , pp. 527-540
    • Narayanan, R.1    LeDuc, B.2    Williams, D.A.3
  • 24
    • 0041856580 scopus 로고    scopus 로고
    • Glucuronidation of anabolic androgenic steroids by recombinant human UDP-glucuronosyltransferases
    • Kuuranne T., Kurkela M., Thevis M., Schänzer W., Finel M., and Kostiainen R. Glucuronidation of anabolic androgenic steroids by recombinant human UDP-glucuronosyltransferases. Drug Metab Dispos 31 (2003) 1117-1124
    • (2003) Drug Metab Dispos , vol.31 , pp. 1117-1124
    • Kuuranne, T.1    Kurkela, M.2    Thevis, M.3    Schänzer, W.4    Finel, M.5    Kostiainen, R.6
  • 25
    • 0035397393 scopus 로고    scopus 로고
    • Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data
    • Cortes A., Cascante M., Cardenas M.L., and Cornish-Bowden A. Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data. Biochem J 357 (2001) 263-268
    • (2001) Biochem J , vol.357 , pp. 263-268
    • Cortes, A.1    Cascante, M.2    Cardenas, M.L.3    Cornish-Bowden, A.4
  • 26
    • 33846430542 scopus 로고    scopus 로고
    • Inhibitory potential of nonsteroidal anti-inflammatory drugs on UDP-glucuronosyltransferase 2B7 in human liver microsomes
    • Mano Y., Usui T., and Kamimura H. Inhibitory potential of nonsteroidal anti-inflammatory drugs on UDP-glucuronosyltransferase 2B7 in human liver microsomes. Eur J Clin Pharmacol 63 (2007) 211-216
    • (2007) Eur J Clin Pharmacol , vol.63 , pp. 211-216
    • Mano, Y.1    Usui, T.2    Kamimura, H.3
  • 27
    • 1842536833 scopus 로고    scopus 로고
    • Human UDP-glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid
    • Uchaipichat V., Mackenzie P.I., Guo X.H., Gardner-Stephen D., Galetin A., Houston J.B., et al. Human UDP-glucuronosyltransferases: isoform selectivity and kinetics of 4-methylumbelliferone and 1-naphthol glucuronidation, effects of organic solvents, and inhibition by diclofenac and probenecid. Drug Metab Dispos 32 (2004) 413-423
    • (2004) Drug Metab Dispos , vol.32 , pp. 413-423
    • Uchaipichat, V.1    Mackenzie, P.I.2    Guo, X.H.3    Gardner-Stephen, D.4    Galetin, A.5    Houston, J.B.6
  • 28
    • 0037403749 scopus 로고    scopus 로고
    • Glucuronidation activity of the UGT2B17 enzyme toward xenobiotics
    • Turgeon D., Carrier J.S., Chouinard S., and Belanger A. Glucuronidation activity of the UGT2B17 enzyme toward xenobiotics. Drug Metab Dispos 31 (2003) 670-676
    • (2003) Drug Metab Dispos , vol.31 , pp. 670-676
    • Turgeon, D.1    Carrier, J.S.2    Chouinard, S.3    Belanger, A.4
  • 29
    • 54349124543 scopus 로고    scopus 로고
    • The configuration of the 17-hydroxy group variably influences the glucuronidation of beta-estradiol and epiestradiol by human UDP-glucuronosyltransferases
    • Itäaho K., Mackenzie P.I., Ikushiro S., Miners J.O., and Finel M. The configuration of the 17-hydroxy group variably influences the glucuronidation of beta-estradiol and epiestradiol by human UDP-glucuronosyltransferases. Drug Metab Dispos 36 (2008) 2307-2315
    • (2008) Drug Metab Dispos , vol.36 , pp. 2307-2315
    • Itäaho, K.1    Mackenzie, P.I.2    Ikushiro, S.3    Miners, J.O.4    Finel, M.5


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