메뉴 건너뛰기




Volumn 21, Issue 8, 2008, Pages 1524-1529

Serum albumin is as efficient as paraxonase in the detoxication of paraoxon at toxicologically relevant concentrations

Author keywords

[No Author keywords available]

Indexed keywords

ARYLDIALKYLPHOSPHATASE; CHLORPYRIFOS; LIPOPROTEIN; PARAOXON; SERUM ALBUMIN;

EID: 51449095739     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx800075x     Document Type: Article
Times cited : (58)

References (39)
  • 2
    • 5344229364 scopus 로고    scopus 로고
    • Paraoxonase 1 and atherosclerosis: Is the gene or the protein more important?
    • Mackness, M., and Mackness, B. (2004) Paraoxonase 1 and atherosclerosis: is the gene or the protein more important? Free Radical Biol. Med. 37, 1317-1323.
    • (2004) Free Radical Biol. Med , vol.37 , pp. 1317-1323
    • Mackness, M.1    Mackness, B.2
  • 3
    • 0034635449 scopus 로고    scopus 로고
    • Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation
    • Jakubowski, H. (2000) Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation. J. Biol. Chem. 75, 3957-3962.
    • (2000) J. Biol. Chem , vol.75 , pp. 3957-3962
    • Jakubowski, H.1
  • 4
    • 5344238178 scopus 로고    scopus 로고
    • Paraoxonases 1, 2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development
    • Aviram, M., and Rosenblat, M. (2004) Paraoxonases 1, 2, and 3, oxidative stress, and macrophage foam cell formation during atherosclerosis development. Free Radical Biol. Med. 37, 1304-1316.
    • (2004) Free Radical Biol. Med , vol.37 , pp. 1304-1316
    • Aviram, M.1    Rosenblat, M.2
  • 5
    • 33646202459 scopus 로고    scopus 로고
    • The catalytic histidine dyad of high density lipoprotein-associated serum paraoxonase-1 (PON1) is essential for PON1-mediated inhibition of low density lipoprotein oxidation and stimulation of macrophage cholesterol efflux
    • Rosenblat, M., Gaidukov, L., Khersonsky, O., Vaya, J., Oren, R., Tawfik, D. S., and Aviram, M. (2006) The catalytic histidine dyad of high density lipoprotein-associated serum paraoxonase-1 (PON1) is essential for PON1-mediated inhibition of low density lipoprotein oxidation and stimulation of macrophage cholesterol efflux. J. Biol. Chem. 281, 7657-7665.
    • (2006) J. Biol. Chem , vol.281 , pp. 7657-7665
    • Rosenblat, M.1    Gaidukov, L.2    Khersonsky, O.3    Vaya, J.4    Oren, R.5    Tawfik, D.S.6    Aviram, M.7
  • 6
    • 33745964245 scopus 로고    scopus 로고
    • Human paraoxonase-1 overexpression inhibits atherosclerosis in a mouse model of metabolic syndrome
    • Mackness, B., Quarck, R., Verreth, W., Mackness, M., and Holvoet, P. (2006) Human paraoxonase-1 overexpression inhibits atherosclerosis in a mouse model of metabolic syndrome. Arterioscler., Thromb., Vasc. Biol. 26, 1545-1550.
    • (2006) Arterioscler., Thromb., Vasc. Biol , vol.26 , pp. 1545-1550
    • Mackness, B.1    Quarck, R.2    Verreth, W.3    Mackness, M.4    Holvoet, P.5
  • 13
    • 33846961096 scopus 로고    scopus 로고
    • Direct detection of stereospecific soman hydrolysis by wild-type human serum paraoxonase
    • Yeung, D. T., Smith, J. R., Sweeney, R. E., Lenz, D. E., and Cerasoli, D. M. (2007) Direct detection of stereospecific soman hydrolysis by wild-type human serum paraoxonase. FEBS J. 274, 1183-1191.
    • (2007) FEBS J , vol.274 , pp. 1183-1191
    • Yeung, D.T.1    Smith, J.R.2    Sweeney, R.E.3    Lenz, D.E.4    Cerasoli, D.M.5
  • 14
    • 11844296648 scopus 로고    scopus 로고
    • Measurement of paraoxonase (PON1) status as a potential biomarker of susceptibility to organophosphate toxicity
    • Costa, L. G., Cole, T. B., Vitalone, A., and Furlong, C. E. (2005) Measurement of paraoxonase (PON1) status as a potential biomarker of susceptibility to organophosphate toxicity. Clin. Chim. Acta 352, 37-47.
    • (2005) Clin. Chim. Acta , vol.352 , pp. 37-47
    • Costa, L.G.1    Cole, T.B.2    Vitalone, A.3    Furlong, C.E.4
  • 15
    • 0034524737 scopus 로고    scopus 로고
    • Catalytic efficiency determines the in-vivo efficacy of PON1 for detoxifying organophosphorus compounds
    • Li, W. F., Costa, L. G., Richter, R. J., Hagen, T., Shih, D. M., Tward, A., Lusis, A. J., and Furlong, C. E. (2000) Catalytic efficiency determines the in-vivo efficacy of PON1 for detoxifying organophosphorus compounds. Pharmacogenetics 10, 767-779.
    • (2000) Pharmacogenetics , vol.10 , pp. 767-779
    • Li, W.F.1    Costa, L.G.2    Richter, R.J.3    Hagen, T.4    Shih, D.M.5    Tward, A.6    Lusis, A.J.7    Furlong, C.E.8
  • 16
    • 0030293198 scopus 로고    scopus 로고
    • The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin
    • Davies, H. G., Richter, R. J., Keifer, M., Broomfield, C. A., Sowalla, J., and Furlong, C. E. (1996) The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat. Genet. 14, 334-336.
    • (1996) Nat. Genet , vol.14 , pp. 334-336
    • Davies, H.G.1    Richter, R.J.2    Keifer, M.3    Broomfield, C.A.4    Sowalla, J.5    Furlong, C.E.6
  • 17
    • 0032963556 scopus 로고    scopus 로고
    • The role of phosphotriesterases in the detoxication of organophosphorus compounds
    • Vilanova, E., and Sogorb, M. A. (1999) The role of phosphotriesterases in the detoxication of organophosphorus compounds. Crit. Rev. Toxicol. 29, 21-57.
    • (1999) Crit. Rev. Toxicol , vol.29 , pp. 21-57
    • Vilanova, E.1    Sogorb, M.A.2
  • 18
    • 0016804683 scopus 로고
    • Acetylation of human serum albumin by p-nitrophenyl acetate
    • Means, G. E., and Bender, M. (1975) Acetylation of human serum albumin by p-nitrophenyl acetate. Biochemistry 14, 4989-4994.
    • (1975) Biochemistry , vol.14 , pp. 4989-4994
    • Means, G.E.1    Bender, M.2
  • 19
    • 0018291713 scopus 로고
    • On the genetics of the human serum paraoxonase (EC 3.1.1.2)
    • Geldmacher-von Mallinckrodt, M., Hommel, G., and Dumbach, J. (1979) On the genetics of the human serum paraoxonase (EC 3.1.1.2). Hum. Genet. 50, 313-326.
    • (1979) Hum. Genet , vol.50 , pp. 313-326
    • Geldmacher-von Mallinckrodt, M.1    Hommel, G.2    Dumbach, J.3
  • 20
    • 0021351483 scopus 로고
    • Paraoxon hydrolysis in human serum mediated by a genetically variable arylesterase and albumin
    • Ortigoza-Ferado, J., Richter, R. J., Hornung, S. K., Motulsky, A. G., and Furlong, E. (1984) Paraoxon hydrolysis in human serum mediated by a genetically variable arylesterase and albumin. Am. J. Hum. Genet. 36, 295-305.
    • (1984) Am. J. Hum. Genet , vol.36 , pp. 295-305
    • Ortigoza-Ferado, J.1    Richter, R.J.2    Hornung, S.K.3    Motulsky, A.G.4    Furlong, E.5
  • 21
    • 33845951083 scopus 로고    scopus 로고
    • Markers of organophosphate exposure in human serum
    • Wieseler, S., Schopfer, L., and Lockridge, O. (2006) Markers of organophosphate exposure in human serum. J. Mol. Neurosci. 30, 93-94.
    • (2006) J. Mol. Neurosci , vol.30 , pp. 93-94
    • Wieseler, S.1    Schopfer, L.2    Lockridge, O.3
  • 22
    • 33846389181 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry assay for organophosphorus toxicants bound to human albumin at Tyr411
    • Li, B., Schopfer, L. M., Hinrichs, S. H., Masson, P., and Lockridge, O. (2007) Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry assay for organophosphorus toxicants bound to human albumin at Tyr411. Anal. Biochem. 361, 263-272.
    • (2007) Anal. Biochem , vol.361 , pp. 263-272
    • Li, B.1    Schopfer, L.M.2    Hinrichs, S.H.3    Masson, P.4    Lockridge, O.5
  • 23
    • 34248383598 scopus 로고    scopus 로고
    • Differential protein adduction by seven organophosphorus pesticides in both brain and thymus
    • Carter, W. G., Tarhoni, M., Rathbone, A. J., and Ray, D. E. (2007) Differential protein adduction by seven organophosphorus pesticides in both brain and thymus. Hum. Exp. Toxicol. 26, 347-353.
    • (2007) Hum. Exp. Toxicol , vol.26 , pp. 347-353
    • Carter, W.G.1    Tarhoni, M.2    Rathbone, A.J.3    Ray, D.E.4
  • 25
    • 0344699371 scopus 로고    scopus 로고
    • EDTA-resistant and sensitive phosphodiesterase activities associated with albumin and lipoproteins in rabbit serum
    • Sogorb, M. A., Sellero, I., López-Rivadulla, M., Céspedes, V., and Vilanova, E. (1999) EDTA-resistant and sensitive phosphodiesterase activities associated with albumin and lipoproteins in rabbit serum. Drug Metab. Dispos. 27, 53-59.
    • (1999) Drug Metab. Dispos , vol.27 , pp. 53-59
    • Sogorb, M.A.1    Sellero, I.2    López-Rivadulla, M.3    Céspedes, V.4    Vilanova, E.5
  • 27
    • 11244349982 scopus 로고    scopus 로고
    • Hydrolysis of carbaryl by human serum albumin
    • Sogorb, M. A., Carrera, V., and Vilanova, E. (2004) Hydrolysis of carbaryl by human serum albumin. Arch. Toxicol. 78, 629-334.
    • (2004) Arch. Toxicol , vol.78 , pp. 629-334
    • Sogorb, M.A.1    Carrera, V.2    Vilanova, E.3
  • 28
    • 0031967954 scopus 로고    scopus 로고
    • Phosphodiesterase activity identified in purified serum albumins
    • Sogorb, M. A., Díaz-Alejo, N., Escudero, M. A., and Vilanova, E. (1998) Phosphodiesterase activity identified in purified serum albumins. Arch. Toxicol. 72, 219-226.
    • (1998) Arch. Toxicol , vol.72 , pp. 219-226
    • Sogorb, M.A.1    Díaz-Alejo, N.2    Escudero, M.A.3    Vilanova, E.4
  • 29
    • 34848896346 scopus 로고    scopus 로고
    • Comparative hydrolysis of O-hexyl O-2,5-dichlorophenyl phosphoramidate and paraoxon in different tissues of vertebrates
    • Monroy-Noyola, A., Rojas, P., Vilanova, E., and Sogorb, M. A. (2007) Comparative hydrolysis of O-hexyl O-2,5-dichlorophenyl phosphoramidate and paraoxon in different tissues of vertebrates. Arch. Toxicol. 81, 689-695.
    • (2007) Arch. Toxicol , vol.81 , pp. 689-695
    • Monroy-Noyola, A.1    Rojas, P.2    Vilanova, E.3    Sogorb, M.A.4
  • 30
    • 33846818304 scopus 로고    scopus 로고
    • An in vitro approach for demonstrating the critical role of serum albumin in the detoxication of the carbamate carbaryl at in vivo toxicologically relevant concentrations
    • Sogorb, M. A., Alvarez-Escalante, C., Carrera, V., and Vilanova, E. (2007) An in vitro approach for demonstrating the critical role of serum albumin in the detoxication of the carbamate carbaryl at in vivo toxicologically relevant concentrations. Arch. Toxicol. 81, 113-119.
    • (2007) Arch. Toxicol , vol.81 , pp. 113-119
    • Sogorb, M.A.1    Alvarez-Escalante, C.2    Carrera, V.3    Vilanova, E.4
  • 31
  • 32
    • 0023806064 scopus 로고
    • Role of genetic polymorphism of human plasma paraoxonase/arylesterase in hydrolysis of the insecticide metabolites chlorpyrifos oxon and paraoxon
    • Furlong, C. E., Richter, R. J., Seidel, S. L., and Motulsky, A. G. (1988) Role of genetic polymorphism of human plasma paraoxonase/arylesterase in hydrolysis of the insecticide metabolites chlorpyrifos oxon and paraoxon. Am. J. Hum. Genet. 43, 230-238.
    • (1988) Am. J. Hum. Genet , vol.43 , pp. 230-238
    • Furlong, C.E.1    Richter, R.J.2    Seidel, S.L.3    Motulsky, A.G.4
  • 34
    • 0008841068 scopus 로고    scopus 로고
    • Chemical Aspects: Albumin in Medicine
    • Peters, T, Jr. Eds, pp, Academic Press Inc, San Diego, CA
    • Peters, T., Jr. (1996) Chemical Aspects: Albumin in Medicine. In All about Albumin. Biochemistry, Genetics, and Medical Applications (Peters, T., Jr. Eds.) pp 251-284, Academic Press Inc., San Diego, CA.
    • (1996) All about Albumin. Biochemistry, Genetics, and Medical Applications , pp. 251-284
    • Peters Jr., T.1
  • 35
    • 0002634916 scopus 로고
    • Percutaneous absorption of parathion and its metabolites, paraoxon and p-nitrophenol, administered alone or in combination: In vitro flow-through diffusion cell studies
    • Chang, S. K., Dauterman, W. C., and Riviere, J. E. (1994) Percutaneous absorption of parathion and its metabolites, paraoxon and p-nitrophenol, administered alone or in combination: in vitro flow-through diffusion cell studies. Pest. Biochem. Physiol. 48, 56-62.
    • (1994) Pest. Biochem. Physiol , vol.48 , pp. 56-62
    • Chang, S.K.1    Dauterman, W.C.2    Riviere, J.E.3
  • 38
    • 0023633188 scopus 로고
    • The effect of carboxylesterase inhibition on interspecies differences in soman toxicity
    • Maxwell, D. M., Brecht, K. M., and O'Neill, B. L. (1987) The effect of carboxylesterase inhibition on interspecies differences in soman toxicity. Toxicol. Lett. 39, 35-42.
    • (1987) Toxicol. Lett , vol.39 , pp. 35-42
    • Maxwell, D.M.1    Brecht, K.M.2    O'Neill, B.L.3
  • 39
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • Li, B., Sedlacek, M., Manoharan, I., Boopathy, R., Duysen, E. G., Masson, P., and Lockridge, O. (2005) Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma. Biochem. Pharmacol. 70, 1673-1684.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 1673-1684
    • Li, B.1    Sedlacek, M.2    Manoharan, I.3    Boopathy, R.4    Duysen, E.G.5    Masson, P.6    Lockridge, O.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.