메뉴 건너뛰기




Volumn 1774, Issue 7, 2007, Pages 874-883

Stability of highly purified human paraoxonase (PON1): Association with human phosphate binding protein (HPBP) is essential for preserving its active conformation(s)

Author keywords

Biopharmaceutical; Catalytic scavenger; Enzyme therapy; Nerve agent; Paraoxonase; Protein stability

Indexed keywords

ARYLDIALKYLPHOSPHATASE 1; HYBRID PROTEIN; ORGANOPHOSPHATE; PHOSPHATE BINDING PROTEIN; RECOMBINANT PROTEIN;

EID: 34250882686     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.05.001     Document Type: Article
Times cited : (40)

References (42)
  • 2
    • 0034635449 scopus 로고    scopus 로고
    • Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation
    • Jakubowski H. Calcium-dependent human serum homocysteine thiolactone hydrolase. A protective mechanism against protein N-homocysteinylation. J. Biol. Chem. 275 (2000) 3957-3962
    • (2000) J. Biol. Chem. , vol.275 , pp. 3957-3962
    • Jakubowski, H.1
  • 3
    • 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., Sowala J., and Furlong C.E. The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat. Genet. 14 (1996) 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    Sowala, J.5    Furlong, C.E.6
  • 4
    • 17644367506 scopus 로고    scopus 로고
    • Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
    • Khersonsky O., and Tawfik D.S. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44 (2005) 6371-6382
    • (2005) Biochemistry , vol.44 , pp. 6371-6382
    • Khersonsky, O.1    Tawfik, D.S.2
  • 5
    • 0347635518 scopus 로고    scopus 로고
    • Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization
    • Aharoni A., Gaidukov L., Yagur S., Toker L., Silman I., and Tawfik D.S. Directed evolution of mammalian paraoxonases PON1 and PON3 for bacterial expression and catalytic specialization. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 482-487
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 482-487
    • Aharoni, A.1    Gaidukov, L.2    Yagur, S.3    Toker, L.4    Silman, I.5    Tawfik, D.S.6
  • 6
    • 0034648768 scopus 로고    scopus 로고
    • Atherosclerosis
    • Lusis A.J. Atherosclerosis. Nature 407 (2000) 233-241
    • (2000) Nature , vol.407 , pp. 233-241
    • Lusis, A.J.1
  • 7
    • 33947619646 scopus 로고    scopus 로고
    • Human paraoxonase: a promising approach for pre-treatment and therapy of organophosphorus poisoning
    • Rochu D., Chabrière E., and Masson P. Human paraoxonase: a promising approach for pre-treatment and therapy of organophosphorus poisoning. Toxicology 233 (2007) 47-59
    • (2007) Toxicology , vol.233 , pp. 47-59
    • Rochu, D.1    Chabrière, E.2    Masson, P.3
  • 8
    • 8544270882 scopus 로고    scopus 로고
    • The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity
    • James R.W., and Deakin S.P. The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity. Free Radical Biol. Med. 37 (2004) 1986-1994
    • (2004) Free Radical Biol. Med. , vol.37 , pp. 1986-1994
    • James, R.W.1    Deakin, S.P.2
  • 9
    • 24344460308 scopus 로고    scopus 로고
    • High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDLwith apoA-I
    • Gaidukov L., and Tawfik D.S. High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDLwith apoA-I. Biochemistry 44 (2005) 11843-11854
    • (2005) Biochemistry , vol.44 , pp. 11843-11854
    • Gaidukov, L.1    Tawfik, D.S.2
  • 13
    • 34250881203 scopus 로고    scopus 로고
    • Functional states, storage and thermal stability of human paraoxonase: drawbacks, advantages and potentialities
    • Rochu D., Chabrière E., Renault F., Elias M., Cléry-Barraud C., and Masson P. Functional states, storage and thermal stability of human paraoxonase: drawbacks, advantages and potentialities. Toxicology 233 (2007) 226
    • (2007) Toxicology , vol.233 , pp. 226
    • Rochu, D.1    Chabrière, E.2    Renault, F.3    Elias, M.4    Cléry-Barraud, C.5    Masson, P.6
  • 14
    • 10044261174 scopus 로고    scopus 로고
    • Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH
    • Teiber J.F., Draganov D.I., and La Du B.N. Purified human serum PON1 does not protect LDL against oxidation in the in vitro assays initiated with copper or AAPH. J. Lipid Res. 45 (2004) 2260-2268
    • (2004) J. Lipid Res. , vol.45 , pp. 2260-2268
    • Teiber, J.F.1    Draganov, D.I.2    La Du, B.N.3
  • 15
    • 10644283921 scopus 로고    scopus 로고
    • Paraoxonase-1 does not reduce or modify oxidation of phospholipids by peroxinitrite
    • Connelly P.W., Draganov D., and Maguire G.F. Paraoxonase-1 does not reduce or modify oxidation of phospholipids by peroxinitrite. Free Radical Biol. Med. 38 (2005) 164-174
    • (2005) Free Radical Biol. Med. , vol.38 , pp. 164-174
    • Connelly, P.W.1    Draganov, D.2    Maguire, G.F.3
  • 16
    • 21244491480 scopus 로고    scopus 로고
    • Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
    • Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., and La Du B.N. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46 (2005) 1239-1247
    • (2005) J. Lipid Res. , vol.46 , pp. 1239-1247
    • Draganov, D.I.1    Teiber, J.F.2    Speelman, A.3    Osawa, Y.4    Sunahara, R.5    La Du, B.N.6
  • 17
    • 20644436041 scopus 로고    scopus 로고
    • Paraoxonase-1 promoter polymorphism C-107T and serum apolipoprotein AI interact to modulate serum paraoxonase-1 status
    • James R.W., Kalix B., Bioletto S., and Brulhart-Meynet M.-C. Paraoxonase-1 promoter polymorphism C-107T and serum apolipoprotein AI interact to modulate serum paraoxonase-1 status. Pharmacogenet. Genomics 15 (2005) 441-446
    • (2005) Pharmacogenet. Genomics , vol.15 , pp. 441-446
    • James, R.W.1    Kalix, B.2    Bioletto, S.3    Brulhart-Meynet, M.-C.4
  • 18
    • 0033515056 scopus 로고    scopus 로고
    • Identification of residues essential for human paraoxonase (PON1) arylesterase/organophosphatase activities
    • Josse D., Xie W., Renault F., Rochu D., Schopfer L.M., Masson P., and Lockridge O. Identification of residues essential for human paraoxonase (PON1) arylesterase/organophosphatase activities. Biochemistry 38 (1999) 2816-2825
    • (1999) Biochemistry , vol.38 , pp. 2816-2825
    • Josse, D.1    Xie, W.2    Renault, F.3    Rochu, D.4    Schopfer, L.M.5    Masson, P.6    Lockridge, O.7
  • 19
    • 0026096803 scopus 로고
    • Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities
    • Gan K.N., Smolen A., Eckerson H.W., and La Du B.N. Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities. Drug Metab. Dispos. 19 (1991) 100-106
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 100-106
    • Gan, K.N.1    Smolen, A.2    Eckerson, H.W.3    La Du, B.N.4
  • 20
    • 33646256546 scopus 로고    scopus 로고
    • Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography
    • Renault F., Chabrière E., Andrieu J.P., Dublet B., Masson P., and Rochu D. Tandem purification of two HDL-associated partner proteins in human plasma, paraoxonase (PON1) and phosphate binding protein (HPBP) using hydroxyapatite chromatography. J. Chromatogr., B 836 (2006) 15-21
    • (2006) J. Chromatogr., B , vol.836 , pp. 15-21
    • Renault, F.1    Chabrière, E.2    Andrieu, J.P.3    Dublet, B.4    Masson, P.5    Rochu, D.6
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0032909892 scopus 로고    scopus 로고
    • Measuring conformational stability of proteins using an optimized temperature-controlled capillary electrophoresis approach
    • Rochu D., Ducret G., and Masson P. Measuring conformational stability of proteins using an optimized temperature-controlled capillary electrophoresis approach. J. Chromatogr., A 838 (1999) 157-165
    • (1999) J. Chromatogr., A , vol.838 , pp. 157-165
    • Rochu, D.1    Ducret, G.2    Masson, P.3
  • 24
    • 0027478269 scopus 로고
    • Analysis of thermally induced protein folding/unfolding transitions using free solution capillary electrophoresis
    • Hilser V.J., Worosila G.D., and Freire E. Analysis of thermally induced protein folding/unfolding transitions using free solution capillary electrophoresis. Anal. Biochem. 208 (1993) 125-131
    • (1993) Anal. Biochem. , vol.208 , pp. 125-131
    • Hilser, V.J.1    Worosila, G.D.2    Freire, E.3
  • 25
    • 0036178618 scopus 로고    scopus 로고
    • Multiple advantages of capillary zone electrophoresis for exploring protein conformational stability
    • Rochu D., and Masson P. Multiple advantages of capillary zone electrophoresis for exploring protein conformational stability. Electrophoresis 23 (2002) 189-202
    • (2002) Electrophoresis , vol.23 , pp. 189-202
    • Rochu, D.1    Masson, P.2
  • 26
    • 0026026523 scopus 로고
    • Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase
    • Smolen A., Eckerson H.W., Gan K.N., Hailat N., and La Du B.N. Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase. Drug Metab. Dispos. 19 (1991) 107-112
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 107-112
    • Smolen, A.1    Eckerson, H.W.2    Gan, K.N.3    Hailat, N.4    La Du, B.N.5
  • 28
    • 0029165744 scopus 로고
    • Comparison of purified human and rabbit serum paraoxonases
    • Kuo C.-L., and La Du B.N. Comparison of purified human and rabbit serum paraoxonases. Drug Metab. Dispos. 23 (1995) 935-944
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 935-944
    • Kuo, C.-L.1    La Du, B.N.2
  • 29
    • 22144463636 scopus 로고
    • Serum 'A' esterases and organophosphates toxicity in man
    • Reiner E., Aldridge W.N., and Hoskin F.C.G. (Eds), Ellis Horwood, New York
    • Lotti M., Moretto A., and Traverso R. Serum 'A' esterases and organophosphates toxicity in man. In: Reiner E., Aldridge W.N., and Hoskin F.C.G. (Eds). Enzymes hydrolyzing organophosphorus compounds (1989), Ellis Horwood, New York 192-201
    • (1989) Enzymes hydrolyzing organophosphorus compounds , pp. 192-201
    • Lotti, M.1    Moretto, A.2    Traverso, R.3
  • 30
    • 0142138852 scopus 로고    scopus 로고
    • Beneficial effect of oleoylated lipids on paraoxonase1: protection against oxidative inactivation and stabilization
    • Nguyen S.D., and Sok E.-E. Beneficial effect of oleoylated lipids on paraoxonase1: protection against oxidative inactivation and stabilization. Biochem. J. 375 (2003) 275-285
    • (2003) Biochem. J. , vol.375 , pp. 275-285
    • Nguyen, S.D.1    Sok, E.-E.2
  • 31
    • 9244245550 scopus 로고
    • Studies of aromatic esterases and cholinesterase of human serum
    • Marton A., and Kalow W. Studies of aromatic esterases and cholinesterase of human serum. Can. J. Biochem. Physiol. 37 (1959) 1367-1373
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 1367-1373
    • Marton, A.1    Kalow, W.2
  • 32
    • 0001724351 scopus 로고
    • Arylesterase in blood: effects of calcium and inhibitors
    • Erdos E.G., Debay C.R., and Westerman M.P. Arylesterase in blood: effects of calcium and inhibitors. Biochem. Pharmacol. 5 (1960) 173-186
    • (1960) Biochem. Pharmacol. , vol.5 , pp. 173-186
    • Erdos, E.G.1    Debay, C.R.2    Westerman, M.P.3
  • 33
    • 0028036743 scopus 로고
    • Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver
    • Gil F., Gonzalvo M.C., Hernández A.F., Villanueva E., and Pla A. Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver. Biochem. Pharmacol. 48 (1994) 1559-1568
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1559-1568
    • Gil, F.1    Gonzalvo, M.C.2    Hernández, A.F.3    Villanueva, E.4    Pla, A.5
  • 35
    • 0031044916 scopus 로고    scopus 로고
    • Purification and characterization of paraoxon hydrolase from rat liver
    • Rodrigo L., Gil F., Hernández A.F., Marina A., Vazquez J., and Pla A. Purification and characterization of paraoxon hydrolase from rat liver. Biochem. J. 321 (1997) 595-601
    • (1997) Biochem. J. , vol.321 , pp. 595-601
    • Rodrigo, L.1    Gil, F.2    Hernández, A.F.3    Marina, A.4    Vazquez, J.5    Pla, A.6
  • 36
    • 0033029010 scopus 로고    scopus 로고
    • Identification of two rat liver proteins with paraoxonase activity: biochemical evidence for the identity of paraoxonase and arylesterase
    • Rodrigo L., Gil F., Hernández A.F., and Pla A. Identification of two rat liver proteins with paraoxonase activity: biochemical evidence for the identity of paraoxonase and arylesterase. Chem.-Biol. Interact. 119-120 (1999) 263-275
    • (1999) Chem.-Biol. Interact. , vol.119-120 , pp. 263-275
    • Rodrigo, L.1    Gil, F.2    Hernández, A.F.3    Pla, A.4
  • 37
    • 0033104680 scopus 로고    scopus 로고
    • Isolation and complete covalent structure of liver microsomal paraoxonase
    • Ozols J. Isolation and complete covalent structure of liver microsomal paraoxonase. Biochem. J. 338 (1999) 265-272
    • (1999) Biochem. J. , vol.338 , pp. 265-272
    • Ozols, J.1
  • 38
    • 0345256493 scopus 로고    scopus 로고
    • Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties
    • Rodrigo L., Gil F., Hernández A.F., Lopez O., and Pla A. Identification of paraoxonase 3 in rat liver microsomes: purification and biochemical properties. Biochem. J. 376 (2003) 261-268
    • (2003) Biochem. J. , vol.376 , pp. 261-268
    • Rodrigo, L.1    Gil, F.2    Hernández, A.F.3    Lopez, O.4    Pla, A.5
  • 39
    • 33947177549 scopus 로고    scopus 로고
    • Effect of metal ions and calcium on purified PON1 and PON3 from rat liver
    • Pla A., Rodrigo L., Hernández A.F., Gil F., and Lopez O. Effect of metal ions and calcium on purified PON1 and PON3 from rat liver. Chem.-Biol. Interact. 167 (2007) 63-70
    • (2007) Chem.-Biol. Interact. , vol.167 , pp. 63-70
    • Pla, A.1    Rodrigo, L.2    Hernández, A.F.3    Gil, F.4    Lopez, O.5
  • 40
    • 33845572689 scopus 로고    scopus 로고
    • The 192R/Q polymorphs of serum paraoxonase PON1 differ in HDL binding, stimulation of lipo-lactonase, and macrophage cholesterol efflux
    • Gaidukov L., Rosenblat M., Aviram M., and Tawfik D.S. The 192R/Q polymorphs of serum paraoxonase PON1 differ in HDL binding, stimulation of lipo-lactonase, and macrophage cholesterol efflux. J. Lipid Res. 47 (2006) 2492-2502
    • (2006) J. Lipid Res. , vol.47 , pp. 2492-2502
    • Gaidukov, L.1    Rosenblat, M.2    Aviram, M.3    Tawfik, D.S.4
  • 41
    • 32244447946 scopus 로고    scopus 로고
    • Capillary electrophoresis versus differential scanning calorimetry for the analysis of free enzyme versus enzyme-ligand complexes: in the search of the ligand-free status of cholinesterases
    • Rochu D., Cléry-Barraud C., Renault F., Chevalier A., Bon C., and Masson P. Capillary electrophoresis versus differential scanning calorimetry for the analysis of free enzyme versus enzyme-ligand complexes: in the search of the ligand-free status of cholinesterases. Electrophoresis 27 (2006) 442-451
    • (2006) Electrophoresis , vol.27 , pp. 442-451
    • Rochu, D.1    Cléry-Barraud, C.2    Renault, F.3    Chevalier, A.4    Bon, C.5    Masson, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.