메뉴 건너뛰기




Volumn 46, Issue 10, 2016, Pages 862-867

Esterase phenotyping in human liver in vitro: specificity of carboxylesterase inhibitors

Author keywords

Butyrylcholinesterase; Eserine; Ethylenediaminetetraacetic acid; Fraction hydrolyzed; Relative activity factor; Tacrine

Indexed keywords

CARBOXYLESTERASE 1 INHIBITOR; CARBOXYLESTERASE 2 INHIBITOR; CLOPIDOGREL; EDETIC ACID; ESTERASE INHIBITOR; IRINOTECAN; PHYSOSTIGMINE; TACRINE; UNCLASSIFIED DRUG; CARBOXYLESTERASE; ENZYME INHIBITOR; ESTERASE;

EID: 84958765332     PISSN: 00498254     EISSN: 13665928     Source Type: Journal    
DOI: 10.3109/00498254.2015.1133867     Document Type: Article
Times cited : (17)

References (26)
  • 1
    • 77953785085 scopus 로고    scopus 로고
    • Identification of the human enzymes responsible for the enzymatic hydrolysis of aclidinium bromide
    • J.Albertí, A.Martinet, S.Sentellas, M.Salvà (2010). Identification of the human enzymes responsible for the enzymatic hydrolysis of aclidinium bromide. Drug Metab Dispos 38:1202–10.
    • (2010) Drug Metab Dispos , vol.38 , pp. 1202-1210
    • Albertí, J.1    Martinet, A.2    Sentellas, S.3    Salvà, M.4
  • 2
    • 0024500536 scopus 로고
    • Comparative inhibitory effects of various physostigmine analogs against acetyl- and butyrylcholinesterases
    • J.R.Atack, Q.S.Yu, T.T.Soncrant,. (1989). Comparative inhibitory effects of various physostigmine analogs against acetyl- and butyrylcholinesterases. J Pharmacol Exp Ther 249:194–202.
    • (1989) J Pharmacol Exp Ther , vol.249 , pp. 194-202
    • Atack, J.R.1    Yu, Q.S.2    Soncrant, T.T.3
  • 3
    • 0345373886 scopus 로고    scopus 로고
    • Crystal structure of human carboxylesterase 1 complexed with the Alzheimer’s drug tacrine: From Binding promiscuity to selective inhibition
    • S.Bencharit, C.L.Morton, J.L.Hyatt,. (2003). Crystal structure of human carboxylesterase 1 complexed with the Alzheimer’s drug tacrine: from binding promiscuity to selective inhibition. Chem Biol 10:341–9.
    • (2003) Chem Biol , vol.10 , pp. 341-349
    • Bencharit, S.1    Morton, C.L.2    Hyatt, J.L.3
  • 4
    • 69949103013 scopus 로고    scopus 로고
    • Esterase activities in the blood, liver and intestine of several preclinical species and humans
    • L.M.Berry, L.Wollenberg, Z.Zhao (2009). Esterase activities in the blood, liver and intestine of several preclinical species and humans. Drug Metab Lett 3:70–7.
    • (2009) Drug Metab Lett , vol.3 , pp. 70-77
    • Berry, L.M.1    Wollenberg, L.2    Zhao, Z.3
  • 5
    • 10744232330 scopus 로고    scopus 로고
    • The conduct of in vitro and in vivo drug-drug interaction studies: A Pharmaceutical Research and Manufacturers of America (PhRMA) perspective
    • T.D.Bjornsson, J.T.Callaghan, H.J.Einolf,. (2003). The conduct of in vitro and in vivo drug-drug interaction studies: a Pharmaceutical Research and Manufacturers of America (PhRMA) perspective. Drug Metab Dispos 31:815–32.
    • (2003) Drug Metab Dispos , vol.31 , pp. 815-832
    • Bjornsson, T.D.1    Callaghan, J.T.2    Einolf, H.J.3
  • 6
    • 61449118867 scopus 로고    scopus 로고
    • The paraoxonaSes: Role In human diseases and methodological difficulties in measurement
    • J.Camps, J.Marsillach, J.Joven (2009). The paraoxonases: role in human diseases and methodological difficulties in measurement. Crit Rev Clin Lab Sci 46:83–106.
    • (2009) Crit Rev Clin Lab Sci , vol.46 , pp. 83-106
    • Camps, J.1    Marsillach, J.2    Joven, J.3
  • 7
    • 84866600954 scopus 로고    scopus 로고
    • The emerging role of human esterases
    • T.Fukami, T.Yokoi (2012). The emerging role of human esterases. Drug Metab Pharmacokinet 27:466–77.
    • (2012) Drug Metab Pharmacokinet , vol.27 , pp. 466-477
    • Fukami, T.1    Yokoi, T.2
  • 8
    • 0031214358 scopus 로고    scopus 로고
    • Inhibition of paraoxonase activity in human liver microsomes by exposure to EDTA, metals and mercurials
    • M.C.Gonzalvo, F.Gil, A.F.Hernández,. (1997). Inhibition of paraoxonase activity in human liver microsomes by exposure to EDTA, metals and mercurials. Chem Biol Interact 105:169–79.
    • (1997) Chem Biol Interact , vol.105 , pp. 169-179
    • Gonzalvo, M.C.1    Gil, F.2    Hernández, A.F.3
  • 9
    • 78249254258 scopus 로고    scopus 로고
    • Recommended nomenclature for five mammalian carboxylesterase gene families: Human, mouse, and rat genes and proteins
    • R.S.Holmes, M.W.Wright, S.J.Laulederkind,. (2010). Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins. Mamm Genome 21:427–41.
    • (2010) Mamm Genome , vol.21 , pp. 427-441
    • Holmes, R.S.1    Wright, M.W.2    Laulederkind, S.J.3
  • 10
    • 0034162687 scopus 로고    scopus 로고
    • Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2
    • R.Humerickhouse, K.Lohrbach, L.Li,. (2000). Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2. Cancer Res 60:1189–92.
    • (2000) Cancer Res , vol.60 , pp. 1189-1192
    • Humerickhouse, R.1    Lohrbach, K.2    Li, L.3
  • 11
    • 0028127008 scopus 로고
    • Tissue distribution of human acetylcholinesterase and butyrylcholinesterase messenger RNA
    • O.Jbilo, C.F.Bartels, A.Chatonnet,. (1994). Tissue distribution of human acetylcholinesterase and butyrylcholinesterase messenger RNA. Toxicon 32:1445–57.
    • (1994) Toxicon , vol.32 , pp. 1445-1457
    • Jbilo, O.1    Bartels, C.F.2    Chatonnet, A.3
  • 12
    • 84866633738 scopus 로고    scopus 로고
    • Metabolic activation by human arylacetamide deacetylase, CYP2E1, and CYP1A2 causes phenacetin-induced methemoglobinemia
    • Y.Kobayashi, T.Fukami, R.Higuchi,. (2012). Metabolic activation by human arylacetamide deacetylase, CYP2E1, and CYP1A2 causes phenacetin-induced methemoglobinemia. Biochem Pharmacol 84:1196–206.
    • (2012) Biochem Pharmacol , vol.84 , pp. 1196-1206
    • Kobayashi, Y.1    Fukami, T.2    Higuchi, R.3
  • 13
    • 0031816430 scopus 로고    scopus 로고
    • Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activity
    • C.L.Kuo, B.N.La Du (1998). Calcium binding by human and rabbit serum paraoxonases. Structural stability and enzymatic activity. Drug Metab Dispos 26:653–60.
    • (1998) Drug Metab Dispos , vol.26 , pp. 653-660
    • Kuo, C.L.1    La Du, B.N.2
  • 14
    • 84875463958 scopus 로고    scopus 로고
    • The role of human carboxylesterases in drug metabolIsm: Have We overlooked their importance?
    • S.C.Laizure, V.Herring, Z.Hu,. (2013). The role of human carboxylesterases in drug metabolism: have we overlooked their importance? Pharmacotherapy 33:210–22.
    • (2013) Pharmacotherapy , vol.33 , pp. 210-222
    • Laizure, S.C.1    Herring, V.2    Hu, Z.3
  • 15
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • B.Li, M.Sedlacek, I.Manoharan,. (2005). Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem Pharmacol 70:1673–84.
    • (2005) Biochem Pharmacol , vol.70 , pp. 1673-1684
    • Li, B.1    Sedlacek, M.2    Manoharan, I.3
  • 16
    • 1642441331 scopus 로고    scopus 로고
    • Pharmacology of selective acetylcholinesterase inhibitors: Implications for use in Alzheimer’s disease
    • D.R.Liston, J.A.Nielsen, A.Villalobos,. (2004). Pharmacology of selective acetylcholinesterase inhibitors: implications for use in Alzheimer’s disease. Eur J Pharmacol 486:9–17.
    • (2004) Eur J Pharmacol , vol.486 , pp. 9-17
    • Liston, D.R.1    Nielsen, J.A.2    Villalobos, A.3
  • 17
    • 0035976903 scopus 로고    scopus 로고
    • Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein
    • C.J.Ng, D.J.Wadleigh, A.Gangopadhyay,. (2001). Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein. J Biol Chem 276:44444–9.
    • (2001) J Biol Chem , vol.276 , pp. 44444-44449
    • Ng, C.J.1    Wadleigh, D.J.2    Gangopadhyay, A.3
  • 18
    • 85146106485 scopus 로고    scopus 로고
    • In vitro approaches for studying the inhibition of drug-metabolizing enzymes and identifying the drug-metabolizing enzymes responsible for the metabolism of drugs (reaction phenotyping) with emphasis on cytochrome P450
    • Rodrigues A.D., (ed), 2nd ed., New York: Informa Healthcare
    • B.W.Ogilvie, E.Usuki, P.Yerino, A.Parkinson (2008). In vitro approaches for studying the inhibition of drug-metabolizing enzymes and identifying the drug-metabolizing enzymes responsible for the metabolism of drugs (reaction phenotyping) with emphasis on cytochrome P450. In: A.D.Rodrigues, ed. Drug–drug interactions. 2nd ed. New York: Informa Healthcare, 231--358.
    • (2008) Drug–drug interactions , pp. 231-358
    • Ogilvie, B.W.1    Usuki, E.2    Yerino, P.3    Parkinson, A.4
  • 19
    • 1542344547 scopus 로고    scopus 로고
    • Predicting drug clearance from recombinantly expressed CYPs: Intersystem EXtrapolation factors
    • N.J.Proctor, G.T.Tucker, A.Rostami-Hodjegan (2004). Predicting drug clearance from recombinantly expressed CYPs: intersystem extrapolation factors. Xenobiotica 34:151–78.
    • (2004) Xenobiotica , vol.34 , pp. 151-178
    • Proctor, N.J.1    Tucker, G.T.2    Rostami-Hodjegan, A.3
  • 20
    • 0027244357 scopus 로고
    • Differentiation of esterases reacting with organophosphorus compounds
    • E.Reiner, E.Pavković, Z.Radić, V.Simeon (1993). Differentiation of esterases reacting with organophosphorus compounds. Chem Biol Interact 87:77–83.
    • (1993) Chem Biol Interact , vol.87 , pp. 77-83
    • Reiner, E.1    Pavković, E.2    Radić, Z.3    Simeon, V.4
  • 21
    • 84859899711 scopus 로고    scopus 로고
    • Conclusive identification of the oxybutynin-hydrolyzing enzyme in human liver
    • Y.Sato, A.Miyashita, T.Iwatsubo, T.Usui (2012). Conclusive identification of the oxybutynin-hydrolyzing enzyme in human liver. Drug Metab Dispos 40:902–6.
    • (2012) Drug Metab Dispos , vol.40 , pp. 902-906
    • Sato, Y.1    Miyashita, A.2    Iwatsubo, T.3    Usui, T.4
  • 22
    • 84903190897 scopus 로고    scopus 로고
    • Screening of specific inhibitors for human carboxylesterases or arylacetamide deacetylase
    • M.Shimizu, T.Fukami, M.Nakajima, T.Yokoi (2014). Screening of specific inhibitors for human carboxylesterases or arylacetamide deacetylase. Drug Metab Dispos 42:1103–9.
    • (2014) Drug Metab Dispos , vol.42 , pp. 1103-1109
    • Shimizu, M.1    Fukami, T.2    Nakajima, M.3    Yokoi, T.4
  • 23
    • 33751171573 scopus 로고    scopus 로고
    • Antiplatelet agents aspirin and clopidogrel are hydrolyzed by distinct carboxylesterases, and clopidogrel is transesterificated in the presence of ethyl alcohol
    • M.Tang, M.Mukundan, J.Yang,. (2006). Antiplatelet agents aspirin and clopidogrel are hydrolyzed by distinct carboxylesterases, and clopidogrel is transesterificated in the presence of ethyl alcohol. J Pharmacol Exp Ther 319:1467–76.
    • (2006) J Pharmacol Exp Ther , vol.319 , pp. 1467-1476
    • Tang, M.1    Mukundan, M.2    Yang, J.3
  • 24
    • 79960581304 scopus 로고    scopus 로고
    • Characterization of recombinant human carboxylesterases: Fluorescein diacetate as a probe substrate for human carboxylesterase 2
    • J.Wang, E.T.Williams, J.Bourgea,. (2011). Characterization of recombinant human carboxylesterases: fluorescein diacetate as a probe substrate for human carboxylesterase 2. Drug Metab Dispos 39:1329–33.
    • (2011) Drug Metab Dispos , vol.39 , pp. 1329-1333
    • Wang, J.1    Williams, E.T.2    Bourgea, J.3
  • 25
    • 0036023423 scopus 로고    scopus 로고
    • Human carboxylesterase 2 is commonly expressed in tumor tissue and is correlated with activation of irinotecan
    • G.Xu, W.Zhang, M.K.Ma, H.L.McLeod (2002). Human carboxylesterase 2 is commonly expressed in tumor tissue and is correlated with activation of irinotecan. Clin Cancer Res 8:2605–11.
    • (2002) Clin Cancer Res , vol.8 , pp. 2605-2611
    • Xu, G.1    Zhang, W.2    Ma, M.K.3    McLeod, H.L.4
  • 26
    • 84874423935 scopus 로고    scopus 로고
    • Carboxylesterase 1 as a determinant of clopidogrel metabolism and activation
    • H.J.Zhu, X.Wang, B.E.Gawronski,. (2013). Carboxylesterase 1 as a determinant of clopidogrel metabolism and activation. J Pharmacol Exp Ther 344:665–72.
    • (2013) J Pharmacol Exp Ther , vol.344 , pp. 665-672
    • Zhu, H.J.1    Wang, X.2    Gawronski, B.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.