Glutathione Transferase P1-1 an Enzyme Useful in Biomedicine and as Biomarker in Clinical Practice and in Environmental Pollution

Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to detoxify the cell from endogenous and exogenous toxic compounds by using glutathione (GSH) or by acting as a ligandin. This review collects...

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Published inNutrients Vol. 11; no. 8; p. 1741
Main Authors Bocedi, Alessio, Noce, Annalisa, Marrone, Giulia, Noce, Gianluca, Cattani, Giada, Gambardella, Giorgia, Di Lauro, Manuela, Di Daniele, Nicola, Ricci, Giorgio
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Abstract Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to detoxify the cell from endogenous and exogenous toxic compounds by using glutathione (GSH) or by acting as a ligandin. This review collects studies that propose GSTP1-1 as a useful biomarker in different fields of application. The most relevant studies are focused on GSTP1-1 as a biosensor to detect blood toxicity in patients affected by kidney diseases. In fact, this detoxifying enzyme is over-expressed in erythrocytes when unusual amounts of toxins are present in the body. Here we review articles concerning the level of GST in chronic kidney disease patients, in maintenance hemodialysis patients and to assess dialysis adequacy. GST is also over-expressed in autoimmune disease like scleroderma, and in kidney transplant patients and it may be used to check the efficiency of transplanted kidneys. The involvement of GSTP in the oxidative stress and in other human pathologies like cancer, liver and neurodegenerative diseases, and psychiatric disorders is also reported. Promising applications of e-GST discussed in the present review are its use for monitoring human subjects living in polluted areas and mammals for veterinary purpose.
AbstractList Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to detoxify the cell from endogenous and exogenous toxic compounds by using glutathione (GSH) or by acting as a ligandin. This review collects studies that propose GSTP1-1 as a useful biomarker in different fields of application. The most relevant studies are focused on GSTP1-1 as a biosensor to detect blood toxicity in patients affected by kidney diseases. In fact, this detoxifying enzyme is over-expressed in erythrocytes when unusual amounts of toxins are present in the body. Here we review articles concerning the level of GST in chronic kidney disease patients, in maintenance hemodialysis patients and to assess dialysis adequacy. GST is also over-expressed in autoimmune disease like scleroderma, and in kidney transplant patients and it may be used to check the efficiency of transplanted kidneys. The involvement of GSTP in the oxidative stress and in other human pathologies like cancer, liver and neurodegenerative diseases, and psychiatric disorders is also reported. Promising applications of e-GST discussed in the present review are its use for monitoring human subjects living in polluted areas and mammals for veterinary purpose.
Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to detoxify the cell from endogenous and exogenous toxic compounds by using glutathione (GSH) or by acting as a ligandin. This review collects studies that propose GSTP1-1 as a useful biomarker in different fields of application. The most relevant studies are focused on GSTP1-1 as a biosensor to detect blood toxicity in patients affected by kidney diseases. In fact, this detoxifying enzyme is over-expressed in erythrocytes when unusual amounts of toxins are present in the body. Here we review articles concerning the level of GST in chronic kidney disease patients, in maintenance hemodialysis patients and to assess dialysis adequacy. GST is also over-expressed in autoimmune disease like scleroderma, and in kidney transplant patients and it may be used to check the efficiency of transplanted kidneys. The involvement of GSTP in the oxidative stress and in other human pathologies like cancer, liver and neurodegenerative diseases, and psychiatric disorders is also reported. Promising applications of e-GST discussed in the present review are its use for monitoring human subjects living in polluted areas and mammals for veterinary purpose.Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to detoxify the cell from endogenous and exogenous toxic compounds by using glutathione (GSH) or by acting as a ligandin. This review collects studies that propose GSTP1-1 as a useful biomarker in different fields of application. The most relevant studies are focused on GSTP1-1 as a biosensor to detect blood toxicity in patients affected by kidney diseases. In fact, this detoxifying enzyme is over-expressed in erythrocytes when unusual amounts of toxins are present in the body. Here we review articles concerning the level of GST in chronic kidney disease patients, in maintenance hemodialysis patients and to assess dialysis adequacy. GST is also over-expressed in autoimmune disease like scleroderma, and in kidney transplant patients and it may be used to check the efficiency of transplanted kidneys. The involvement of GSTP in the oxidative stress and in other human pathologies like cancer, liver and neurodegenerative diseases, and psychiatric disorders is also reported. Promising applications of e-GST discussed in the present review are its use for monitoring human subjects living in polluted areas and mammals for veterinary purpose.
Author Marrone, Giulia
Gambardella, Giorgia
Noce, Annalisa
Cattani, Giada
Di Lauro, Manuela
Bocedi, Alessio
Noce, Gianluca
Di Daniele, Nicola
Ricci, Giorgio
AuthorAffiliation 1 Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy
4 Section of Legal Medicine, Social Security and Forensic Toxicology, Department of Biomedicine and Prevention, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy
2 UOC of Internal Medicine-Center of Hypertension and Nephrology, Department of Systems Medicine, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy
3 PhD School of Applied Medical-Surgical Sciences, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy
AuthorAffiliation_xml – name: 4 Section of Legal Medicine, Social Security and Forensic Toxicology, Department of Biomedicine and Prevention, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy
– name: 2 UOC of Internal Medicine-Center of Hypertension and Nephrology, Department of Systems Medicine, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy
– name: 3 PhD School of Applied Medical-Surgical Sciences, University of Rome Tor Vergata, Via Montpellier 1, 00133 Rome, Italy
– name: 1 Department of Chemical Sciences and Technologies, University of Rome Tor Vergata, Via della Ricerca Scientifica 1, 00133 Rome, Italy
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/31357662$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1021/mp2000692
10.1038/nsb0498-267
10.1089/ars.2010.3508
10.1016/S0021-9258(19)40723-0
10.1042/bj3300175
10.3390/ijerph13040379
10.3892/mmr.2017.6328
10.1016/S0896-6273(00)00115-X
10.3109/10715762.2013.861901
10.1002/ijc.23044
10.3390/nu4101399
10.1016/j.ygyno.2011.10.034
10.1016/0378-4274(87)90167-6
10.1016/j.jchromb.2005.04.023
10.1182/blood-2003-02-0444
10.1038/cmi.2014.121
10.1016/j.freeradbiomed.2007.03.034
10.1097/00125817-200207000-00003
10.1093/aje/kwv292
10.1074/jbc.M102344200
10.1016/S0278-5846(03)00043-5
10.1007/s11033-012-1965-5
10.1016/j.atherosclerosis.2008.06.022
10.1182/blood.V58.4.733.733
10.1016/j.ejca.2009.06.029
10.1021/bi962813z
10.1074/jbc.M007874200
10.1016/j.neulet.2004.05.061
10.1007/s11926-011-0221-7
10.1016/j.febslet.2010.12.009
10.1186/ar2067
10.4103/0019-5545.58308
10.1111/j.1365-2443.2007.01074.x
10.1515/cclm-2017-0703
10.1097/WCO.0000000000000174
10.1042/bj20030860
10.1038/cddiscovery.2016.29
10.1016/0009-8981(81)90040-1
10.1023/B:BIRY.0000043541.80075.fd
10.1136/fn.81.2.F130
10.1016/j.freeradbiomed.2015.06.039
10.1016/S0301-0082(99)00060-X
10.1155/2015/892579
10.1016/S0076-6879(81)77053-8
10.1016/S0076-6879(05)01017-7
10.2174/1568026615666141208110721
10.1053/ajkd.2001.20748
10.1016/j.clinbiochem.2012.02.017
10.1021/bi971902o
10.1074/jbc.274.27.19276
10.1111/j.1365-2133.2012.10831.x
10.1007/s00592-014-0683-y
10.1016/j.pop.2015.07.006
10.1158/1055-9965.EPI-08-0443
10.1007/s40620-014-0126-4
10.1080/13543776.2017.1254192
10.1074/jbc.M101355200
10.1158/1078-0432.CCR-04-2038
10.1042/bj3600001
10.1002/jbt.20088
10.3748/wjg.v12.i3.354
10.1007/978-3-642-77260-3_35
10.17116/jnevro201811811177
10.1016/j.bbamcr.2012.06.019
10.1074/jbc.M507916200
10.1016/0167-4838(89)90111-8
10.1023/A:1005464610585
10.1186/1471-2407-12-196
10.1006/jmbi.1998.2270
10.1080/08039480902767286
10.1016/0041-008X(85)90170-X
10.1177/0960327112474835
10.1016/j.neuint.2015.01.008
10.1111/j.1471-4159.2011.07343.x
10.1016/j.freeradbiomed.2011.04.013
10.1038/nature05292
10.1016/j.jhep.2018.05.010
10.3346/jkms.2010.25.6.846
10.1007/s00592-013-0497-3
10.1007/s11882-018-0771-0
10.1056/NEJM199804093381507
10.1016/j.cca.2013.05.002
10.1111/j.1432-1033.1993.tb18177.x
10.1101/cshperspect.a030361
10.1038/cddiscovery.2016.26
10.1007/s11033-014-3496-8
10.1038/sj.onc.1209576
10.1016/j.transproceed.2015.03.008
10.1177/0394632015572564
10.1006/jmbi.1997.1364
10.1002/hep.510280512
10.1007/s11064-005-6771-1
10.1016/j.tcb.2006.11.003
10.3109/14756366.2015.1064406
10.1159/000028396
10.1002/cncr.22468
10.1016/j.rasd.2014.12.008
10.1093/carcin/bgm205
10.1016/j.bbrc.2012.08.037
10.1002/9780470122778.ch5
10.1016/j.psychres.2010.10.008
10.1038/s41389-017-0025-3
10.1016/j.jadohealth.2012.04.019
10.4149/neo_2010_06_512
10.1002/jbt.22205
10.17116/jnevro201911904147
10.3727/096504010X12626118080064
10.1016/0009-2797(90)90069-Y
10.1007/978-1-4419-0284-9_1
10.1074/jbc.270.3.1243
10.1038/cddis.2013.255
10.1146/annurev.pharmtox.45.120403.095857
10.1002/mc.21939
10.1016/S0002-9440(10)63469-4
10.3109/21678421.2014.964259
10.1111/ecc.12197
10.1080/10428190902878455
10.1016/j.mrfmmm.2014.11.009
10.1016/S0891-5849(00)00252-5
10.1515/revneuro-2014-0046
10.1016/j.bbagen.2012.11.016
10.1016/S0140-6736(10)61156-7
10.1016/S0021-9258(17)46731-7
10.1186/1471-2350-11-46
10.1007/s13277-014-1917-x
10.1016/j.ejfs.2011.04.012
10.1042/bj0790516
10.1590/0004-282X20130060
10.3109/10409239509083491
10.1074/jbc.M116.750299
10.1007/BF00805943
10.1016/j.abb.2010.05.012
10.1002/cncr.27599
10.1016/j.freeradbiomed.2010.08.013
10.1093/clinchem/45.10.1781
10.1158/1055-9965.EPI-05-0105
10.1111/cas.13896
10.1373/clinchem.2004.045955
10.1371/journal.pone.0112797
10.1016/0006-291X(84)91390-1
10.1038/sj.onc.1209373
10.1002/cncr.20729
10.1016/j.aquatox.2010.04.007
10.1021/tx960072x
10.1158/0008-5472.CAN-07-5840
10.1016/S1382-6689(02)00126-6
10.1074/jbc.M113.476135
10.1093/carcin/15.10.2201
10.1007/s13277-015-3871-7
10.47102/annals-acadmedsg.V38N5p396
10.5114/aoms.2010.14458
10.1186/1471-2202-9-67
10.1002/cncr.21619
10.1038/cddis.2012.112
10.1016/j.jhep.2017.03.011
10.1038/ki.1996.307
10.1007/BF00380668
10.1007/s10549-010-0969-x
10.1186/s12937-016-0173-x
10.1056/NEJM199912023412303
10.2174/0929867323666160112122858
10.1016/j.ejca.2010.02.009
10.1371/journal.pmed.0030091
10.4238/gmr.15038034
10.4103/0973-1482.181179
10.1038/s41419-018-0289-3
10.3389/fphar.2014.00170
10.1074/jbc.M002359200
10.1016/j.ejmech.2016.05.063
10.1002/jcc.20084
10.1074/jbc.M116.749507
10.1002/pmic.200300822
10.3390/nu11051073
10.1016/j.canlet.2018.06.028
10.1002/cncr.25006
10.1007/s00726-011-1085-x
10.1200/JCO.2005.03.6640
10.1038/nrurol.2009.49
10.1016/S0022-5347(05)66982-0
10.1515/CCLM.2008.102
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Issue 8
Keywords glutathione transferase
chronic kidney disease
neurodegenerative disease
liver disease
glutathione
environmental pollution
kidney transplantation
hemodialysis
cancer
biomarker
Language English
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References Orru (ref_164) 2018; 69
Muller (ref_98) 2007; 43
ref_99
ref_130
Nuccetelli (ref_21) 1998; 284
Dulhunty (ref_28) 2001; 276
ref_135
ref_95
Perra (ref_166) 2008; 29
Bernardini (ref_61) 2005; 51
Lafuente (ref_133) 1998; 18
Neefjes (ref_90) 1999; 81
Yang (ref_126) 2017; 15
Oakley (ref_18) 1997; 36
Liu (ref_158) 2014; 35
Turkan (ref_195) 2018; 32
Sun (ref_60) 2011; 118
Vos (ref_188) 1990; 75
Rudneva (ref_174) 2010; 1
Wang (ref_157) 2015; 24
Rovcanin (ref_50) 2016; 23
Longo (ref_59) 2013; 71
Primavera (ref_181) 2008; 17
Prokhorova (ref_73) 2019; 119
Pastore (ref_39) 2015; 28
Kiernan (ref_66) 2011; 377
Mignani (ref_110) 2016; 122
Lu (ref_148) 2006; 106
Ivanetich (ref_15) 1989; 998
Bocedi (ref_49) 2018; 9
Guimaraes (ref_51) 2015; 47
Kin (ref_165) 2000; 16
Pae (ref_76) 2003; 27
Nuccetelli (ref_22) 2001; 276
Kose (ref_196) 2016; 31
Wood (ref_69) 2009; 38
ref_71
Lai (ref_123) 2005; 14
Kumar (ref_65) 2017; 27
ref_150
Slatinska (ref_176) 2008; 52
Kanwal (ref_131) 2014; 53
Hubatsch (ref_9) 1998; 330
ref_156
Lescuyer (ref_56) 2004; 4
Fietta (ref_81) 2006; 8
Berendsen (ref_134) 2000; 164
Hsu (ref_154) 2015; 2015
Lord (ref_77) 2000; 28
Habig (ref_7) 1981; 77
Parker (ref_17) 1993; 268
Ricci (ref_24) 2003; 376
Hiyama (ref_145) 2007; 121
Sakaida (ref_160) 1994; 15
Beyer (ref_173) 2003; 13
Simic (ref_132) 2009; 6
Li (ref_169) 2018; 14
Circu (ref_91) 2012; 1823
Yang (ref_159) 2003; 163
Cesareo (ref_12) 2005; 280
McIlwain (ref_105) 2006; 25
Coughlin (ref_127) 2002; 4
Gravina (ref_75) 2011; 187
Kilpikari (ref_180) 1984; 53
Ogino (ref_143) 2019; 110
Milic (ref_92) 2015; 776
Eum (ref_67) 2015; 16
Li (ref_142) 2010; 25
Noce (ref_43) 2014; 51
Nguyen (ref_141) 2010; 18
Lin (ref_103) 2006; 443
Boyland (ref_189) 1969; 32
Bertuccio (ref_163) 2017; 67
Allocati (ref_57) 2018; 7
Pasello (ref_108) 2008; 68
Booth (ref_3) 1961; 79
Caccuri (ref_20) 1999; 274
Song (ref_87) 2012; 39
Storz (ref_102) 2007; 17
Salminen (ref_89) 2014; 25
Lazaro (ref_153) 2012; 166
Harshbarger (ref_113) 2017; 292
Ketley (ref_190) 1975; 250
Johansson (ref_8) 2010; 49
Oakley (ref_5) 1997; 274
Fabrini (ref_13) 2011; 585
Hayes (ref_104) 2000; 61
Wang (ref_170) 2016; 37
Mannervik (ref_10) 2005; 401
Deng (ref_58) 2004; 366
Wu (ref_144) 2006; 24
Singh (ref_179) 1985; 81
Kopple (ref_37) 2001; 37
Hayes (ref_1) 2005; 45
Evelo (ref_185) 1992; 15
Pettersen (ref_35) 2004; 25
Broen (ref_80) 2012; 14
Tezuka (ref_147) 2018; 8
Morozova (ref_52) 2007; 12
Fabrini (ref_84) 2013; 4
Wolfe (ref_47) 1999; 341
Dringen (ref_100) 2000; 62
Crew (ref_138) 2006; 12
Ricci (ref_16) 1995; 270
Galli (ref_42) 2014; 48
Rahbar (ref_78) 2015; 12
Rund (ref_72) 2009; 63
Simic (ref_34) 1992; 2
Gao (ref_136) 2009; 45
Welch (ref_40) 1998; 338
Carmagnol (ref_33) 1981; 117
Wang (ref_93) 2013; 52
Johansson (ref_114) 2011; 8
Agundez (ref_88) 2015; 12
Bocedi (ref_194) 2016; 2
Lei (ref_152) 2015; 8
Noce (ref_96) 2016; 2
Kelishadi (ref_171) 2009; 203
LeRoy (ref_79) 1988; 15
Neto (ref_139) 2014; 35
Galal (ref_112) 2015; 14
Bartolini (ref_30) 2015; 88
Medsger (ref_82) 2003; 21
Glesse (ref_86) 2014; 41
Fabrini (ref_177) 2012; 426
Johnson (ref_53) 2012; 4
Valentini (ref_83) 2003; 21
Hensley (ref_101) 2000; 28
Sharma (ref_183) 2013; 32
Ottaviani (ref_155) 2009; 152
Chowdari (ref_70) 2011; 15
Sheehan (ref_2) 2001; 360
Noce (ref_44) 2015; 52
Bartling (ref_11) 1993; 216
Rose (ref_85) 2016; 183
Hayes (ref_192) 1995; 30
Wu (ref_29) 2006; 25
Sakaida (ref_161) 1998; 28
Bocedi (ref_6) 2013; 288
Pinhel (ref_62) 2008; 46
Sailaja (ref_118) 2010; 11
Lourenco (ref_117) 2009; 50
Sen (ref_175) 2004; 69
Amir (ref_128) 2012; 124
Chatterjee (ref_106) 2018; 433
Tesauro (ref_45) 2015; 28
Savushkina (ref_74) 2018; 118
Wu (ref_111) 2013; 1830
Kilburn (ref_122) 2010; 116
Sakaida (ref_162) 2000; 45
ref_55
Jiao (ref_146) 2007; 109
Awasthi (ref_14) 1984; 125
Dai (ref_182) 2018; 18
Qu (ref_115) 2013; 424
Yang (ref_125) 2005; 103
Lee (ref_167) 2007; 13
Nicotra (ref_19) 1998; 37
Galli (ref_36) 1999; 45
Usarek (ref_68) 2005; 30
Sau (ref_109) 2010; 500
Laupacis (ref_48) 1996; 50
Mazzetti (ref_54) 2015; 82
Mariani (ref_97) 2005; 827
Dasgupta (ref_121) 2003; 102
Linares (ref_151) 2015; 42
Kelishadi (ref_172) 2010; 6
ref_64
ref_168
Chan (ref_129) 2005; 11
Economopoulos (ref_137) 2010; 46
Lu (ref_124) 2011; 125
Ansari (ref_178) 1987; 37
Gurioli (ref_116) 2018; 56
Gouda (ref_94) 2016; 15
Orhan (ref_184) 2005; 19
Kampranis (ref_27) 2000; 275
Tew (ref_107) 2011; 51
ref_31
Vodela (ref_193) 1997; 39
Armstrong (ref_4) 1997; 10
Fabrini (ref_32) 2012; 45
Dunna (ref_119) 2012; 91
Schnekenburger (ref_120) 2014; 5
ref_46
Ada (ref_149) 2010; 57
Hegazi (ref_187) 2010; 99
Mecdad (ref_186) 2011; 1
Xu (ref_140) 2012; 118
Wang (ref_26) 2001; 276
Fisher (ref_63) 2015; 28
Becker (ref_23) 1998; 5
Noce (ref_41) 2012; 3
Dessi (ref_38) 2012; 43
Awasthi (ref_191) 1981; 58
Bocedi (ref_25) 2016; 291
References_xml – volume: 8
  start-page: 1698
  year: 2011
  ident: ref_114
  article-title: Characterization of new potential anticancer drugs designed to overcome glutathione transferase mediated resistance
  publication-title: Mol. Pharm.
  doi: 10.1021/mp2000692
– volume: 5
  start-page: 267
  year: 1998
  ident: ref_23
  article-title: Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers
  publication-title: Nat. Struct. Biol.
  doi: 10.1038/nsb0498-267
– volume: 15
  start-page: 2037
  year: 2011
  ident: ref_70
  article-title: Genetic association studies of antioxidant pathway genes and schizophrenia
  publication-title: Antioxid Redox Signal.
  doi: 10.1089/ars.2010.3508
– volume: 250
  start-page: 8670
  year: 1975
  ident: ref_190
  article-title: Binding of nonsubstrate ligands to the glutathione S-transferases
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(19)40723-0
– volume: 330
  start-page: 175
  year: 1998
  ident: ref_9
  article-title: Human glutathione transferase A4-4: An alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation
  publication-title: Biochem. J.
  doi: 10.1042/bj3300175
– ident: ref_55
  doi: 10.3390/ijerph13040379
– volume: 15
  start-page: 2802
  year: 2017
  ident: ref_126
  article-title: Expression levels of resistant genes affect cervical cancer prognosis
  publication-title: Mol. Med. Rep.
  doi: 10.3892/mmr.2017.6328
– volume: 28
  start-page: 355
  year: 2000
  ident: ref_77
  article-title: Autism spectrum disorders
  publication-title: Neuron
  doi: 10.1016/S0896-6273(00)00115-X
– volume: 48
  start-page: 273
  year: 2014
  ident: ref_42
  article-title: Blood thiol status and erythrocyte glutathione-S-transferase in chronic kidney disease patients on treatment with frequent (daily) hemodialysis
  publication-title: Free Radic. Res.
  doi: 10.3109/10715762.2013.861901
– volume: 121
  start-page: 1643
  year: 2007
  ident: ref_145
  article-title: Genetic polymorphisms and esophageal cancer risk
  publication-title: Int. J. Cancer
  doi: 10.1002/ijc.23044
– volume: 4
  start-page: 1399
  year: 2012
  ident: ref_53
  article-title: Dysregulation of glutathione homeostasis in neurodegenerative diseases
  publication-title: Nutrients
  doi: 10.3390/nu4101399
– volume: 124
  start-page: 354
  year: 2012
  ident: ref_128
  article-title: Genetic polymorphisms as predictive and prognostic biomarkers in gynecological cancers: A systematic review
  publication-title: Gynecol. Oncol.
  doi: 10.1016/j.ygyno.2011.10.034
– volume: 37
  start-page: 57
  year: 1987
  ident: ref_178
  article-title: Human erythrocyte glutathione S-transferase: A possible marker of chemical exposure
  publication-title: Toxicol Lett.
  doi: 10.1016/0378-4274(87)90167-6
– volume: 827
  start-page: 65
  year: 2005
  ident: ref_97
  article-title: Oxidative stress in brain aging, neurodegenerative and vascular diseases: An overview
  publication-title: J. Chromatogr. B Anal. Technol. Biomed. Life Sci.
  doi: 10.1016/j.jchromb.2005.04.023
– volume: 102
  start-page: 2345
  year: 2003
  ident: ref_121
  article-title: Polymorphic variation in GSTP1 modulates outcome following therapy for multiple myeloma
  publication-title: Blood
  doi: 10.1182/blood-2003-02-0444
– volume: 12
  start-page: 777
  year: 2015
  ident: ref_88
  article-title: The GSTP1 gene variant rs1695 is not associated with an increased risk of multiple sclerosis
  publication-title: Cell Mol. Immunol.
  doi: 10.1038/cmi.2014.121
– volume: 43
  start-page: 477
  year: 2007
  ident: ref_98
  article-title: Trends in oxidative aging theories
  publication-title: Free Radic. Biol. Med.
  doi: 10.1016/j.freeradbiomed.2007.03.034
– volume: 4
  start-page: 250
  year: 2002
  ident: ref_127
  article-title: Glutathione S-transferase polymorphisms and risk of ovarian cancer: a HuGE review
  publication-title: Genet. Med.
  doi: 10.1097/00125817-200207000-00003
– volume: 183
  start-page: 403
  year: 2016
  ident: ref_85
  article-title: Prediction and Prevention of Autoimmune Disease in the 21st Century: A Review and Preview
  publication-title: Am. J. Epidemiol.
  doi: 10.1093/aje/kwv292
– volume: 276
  start-page: 42138
  year: 2001
  ident: ref_22
  article-title: Human glutathione transferase P1-1 and nitric oxide carriers; a new role for an old enzyme
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M102344200
– volume: 1
  start-page: 141
  year: 2010
  ident: ref_174
  article-title: Glutathione-S-Transferase Activity in Tissues of Black Sea Fish Species
  publication-title: Asian J. Exp. Biol. Sci.
– volume: 27
  start-page: 519
  year: 2003
  ident: ref_76
  article-title: Association study between glutathione S-transferase P1 polymorphism and schizophrenia in the Korean population
  publication-title: Prog. Neuropsychopharmacol. Biol. Psychiatry
  doi: 10.1016/S0278-5846(03)00043-5
– volume: 39
  start-page: 10739
  year: 2012
  ident: ref_87
  article-title: The glutathione S-transferase M1 and P1 polymorphisms and rheumatoid arthritis: A meta-analysis
  publication-title: Mol. Biol. Rep.
  doi: 10.1007/s11033-012-1965-5
– volume: 203
  start-page: 311
  year: 2009
  ident: ref_171
  article-title: Lifestyle and environmental factors associated with inflammation, oxidative stress and insulin resistance in children
  publication-title: Atherosclerosis
  doi: 10.1016/j.atherosclerosis.2008.06.022
– volume: 58
  start-page: 733
  year: 1981
  ident: ref_191
  article-title: Enzymatic conjugation of erythrocyte glutathione with 1-chloro-2,4-dinitrobenzene: The fate of glutathione conjugate in erythrocytes and the effect of glutathione depletion on hemoglobin
  publication-title: Blood
  doi: 10.1182/blood.V58.4.733.733
– volume: 45
  start-page: 3303
  year: 2009
  ident: ref_136
  article-title: Glutathione S-transferase P1 Ile105Val polymorphism and colorectal cancer risk: A meta-analysis and HuGE review
  publication-title: Eur. J. Cancer
  doi: 10.1016/j.ejca.2009.06.029
– volume: 36
  start-page: 6207
  year: 1997
  ident: ref_18
  article-title: Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme
  publication-title: Biochemistry
  doi: 10.1021/bi962813z
– volume: 276
  start-page: 3319
  year: 2001
  ident: ref_28
  article-title: The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M007874200
– volume: 366
  start-page: 326
  year: 2004
  ident: ref_58
  article-title: Case-only study of interactions between genetic polymorphisms of GSTM1, P1, T1 and Z1 and smoking in Parkinson’s disease
  publication-title: Neurosci. Lett.
  doi: 10.1016/j.neulet.2004.05.061
– volume: 14
  start-page: 11
  year: 2012
  ident: ref_80
  article-title: Genetics of systemic sclerosis: An update
  publication-title: Curr. Rheumatol. Rep.
  doi: 10.1007/s11926-011-0221-7
– volume: 585
  start-page: 341
  year: 2011
  ident: ref_13
  article-title: The extended catalysis of glutathione transferase
  publication-title: FEBS Lett.
  doi: 10.1016/j.febslet.2010.12.009
– volume: 8
  start-page: R160
  year: 2006
  ident: ref_81
  article-title: Analysis of bronchoalveolar lavage fluid proteome from systemic sclerosis patients with or without functional, clinical and radiological signs of lung fibrosis
  publication-title: Arthritis Res. Ther.
  doi: 10.1186/ar2067
– ident: ref_71
  doi: 10.4103/0019-5545.58308
– volume: 12
  start-page: 561
  year: 2007
  ident: ref_52
  article-title: Glutathione depletion in hippocampal cells increases levels of H and L ferritin and glutathione S-transferase mRNAs
  publication-title: Genes Cells
  doi: 10.1111/j.1365-2443.2007.01074.x
– volume: 56
  start-page: 702
  year: 2018
  ident: ref_116
  article-title: GSTP1 methylation in cancer: A liquid biopsy biomarker?
  publication-title: Clin. Chem. Lab. Med.
  doi: 10.1515/cclm-2017-0703
– volume: 28
  start-page: 130
  year: 2015
  ident: ref_63
  article-title: Redefining epilepsy
  publication-title: Curr. Opin. Neurol.
  doi: 10.1097/WCO.0000000000000174
– volume: 376
  start-page: 71
  year: 2003
  ident: ref_24
  article-title: Glutathione transferase P1-1: Self-preservation of an anti-cancer enzyme
  publication-title: Biochem. J.
  doi: 10.1042/bj20030860
– volume: 2
  start-page: 16029
  year: 2016
  ident: ref_194
  article-title: Erythrocyte glutathione transferase: A general probe for chemical contaminations in mammals
  publication-title: Cell Death Discov.
  doi: 10.1038/cddiscovery.2016.29
– volume: 117
  start-page: 209
  year: 1981
  ident: ref_33
  article-title: Glutathione-S-transferase of human red blood cells; assay, values in normal subjects and in two pathological circumstances: Hyperbilirubinemia and impaired renal function
  publication-title: Clin. Chim. Acta
  doi: 10.1016/0009-8981(81)90040-1
– volume: 69
  start-page: 993
  year: 2004
  ident: ref_175
  article-title: Biochemical characterization and distribution of glutathione S-transferases in leaping mullet (Liza saliens)
  publication-title: Biochemistry (Mosc.)
  doi: 10.1023/B:BIRY.0000043541.80075.fd
– volume: 52
  start-page: 129
  year: 2008
  ident: ref_176
  article-title: Biochemical markers of aquatic pollution in fish-glutathione S-transferase
  publication-title: Folia Vet. Lat.
– volume: 81
  start-page: F130
  year: 1999
  ident: ref_90
  article-title: Erythrocyte glutathione S transferase as a marker of oxidative stress at birth
  publication-title: Arch. Dis. Child. Fetal Neonatal Ed.
  doi: 10.1136/fn.81.2.F130
– volume: 88
  start-page: 466
  year: 2015
  ident: ref_30
  article-title: Glutathione S-transferase pi expression regulates the Nrf2-dependent response to hormetic diselenides
  publication-title: Free Radic. Biol. Med.
  doi: 10.1016/j.freeradbiomed.2015.06.039
– volume: 15
  start-page: 202
  year: 1988
  ident: ref_79
  article-title: Scleroderma (systemic sclerosis): Classification, subsets and pathogenesis
  publication-title: J. Rheumatol.
– volume: 62
  start-page: 649
  year: 2000
  ident: ref_100
  article-title: Metabolism and functions of glutathione in brain
  publication-title: Prog. Neurobiol.
  doi: 10.1016/S0301-0082(99)00060-X
– volume: 2015
  start-page: 892579
  year: 2015
  ident: ref_154
  article-title: Association of Environmental Arsenic Exposure, Genetic Polymorphisms of Susceptible Genes, and Skin Cancers in Taiwan
  publication-title: Biomed Res. Int.
  doi: 10.1155/2015/892579
– volume: 77
  start-page: 398
  year: 1981
  ident: ref_7
  article-title: Assays for differentiation of glutathione S-transferases
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(81)77053-8
– volume: 401
  start-page: 265
  year: 2005
  ident: ref_10
  article-title: Human glutathione transferase A3-3 active as steroid double-bond isomerase
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(05)01017-7
– volume: 14
  start-page: 2802
  year: 2015
  ident: ref_112
  article-title: Induction of GST and related events by dietary phytochemicals: Sources, chemistry, and possible contribution to chemoprevention
  publication-title: Curr. Top. Med. Chem.
  doi: 10.2174/1568026615666141208110721
– volume: 37
  start-page: S66
  year: 2001
  ident: ref_37
  article-title: National kidney foundation K/DOQI clinical practice guidelines for nutrition in chronic renal failure
  publication-title: Am. J. Kidney Dis.
  doi: 10.1053/ajkd.2001.20748
– volume: 45
  start-page: 668
  year: 2012
  ident: ref_32
  article-title: Spectrophotometric assay for serum glutathione transferase: A re-examination
  publication-title: Clin. Biochem.
  doi: 10.1016/j.clinbiochem.2012.02.017
– volume: 37
  start-page: 3020
  year: 1998
  ident: ref_19
  article-title: Solution structure of glutathione bound to human glutathione transferase P1-1: Comparison of NMR measurements with the crystal structure
  publication-title: Biochemistry
  doi: 10.1021/bi971902o
– volume: 274
  start-page: 19276
  year: 1999
  ident: ref_20
  article-title: Temperature adaptation of glutathione S-transferase P1-1. A case for homotropic regulation of substrate binding
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.27.19276
– volume: 166
  start-page: 1176
  year: 2012
  ident: ref_153
  article-title: Role of glutathione S-transferases in melanoma susceptibility: Association with GSTP1 rs1695 polymorphism
  publication-title: Br. J. Dermatol.
  doi: 10.1111/j.1365-2133.2012.10831.x
– volume: 13
  start-page: 70
  year: 2007
  ident: ref_167
  article-title: Expression of ErbB receptor proteins and TGF-alpha during diethylnitrosamine-induced hepatocarcinogenesis in the rat liver
  publication-title: Korean J. Hepatol.
– volume: 52
  start-page: 813
  year: 2015
  ident: ref_44
  article-title: Erythrocyte glutathione transferase in uremic diabetic patients: Additional data
  publication-title: Acta Diabetol.
  doi: 10.1007/s00592-014-0683-y
– volume: 42
  start-page: 645
  year: 2015
  ident: ref_151
  article-title: Skin Cancer
  publication-title: Prim. Care
  doi: 10.1016/j.pop.2015.07.006
– volume: 17
  start-page: 3004
  year: 2008
  ident: ref_181
  article-title: Glutathione transferases and glutathionylated hemoglobin in workers exposed to low doses of 1,3-butadiene
  publication-title: Cancer Epidemiol. Biomark. Prev.
  doi: 10.1158/1055-9965.EPI-08-0443
– volume: 28
  start-page: 571
  year: 2015
  ident: ref_39
  article-title: Homocysteine, cysteine, folate and vitamin B(1)(2) status in type 2 diabetic patients with chronic kidney disease
  publication-title: J. Nephrol.
  doi: 10.1007/s40620-014-0126-4
– volume: 27
  start-page: 299
  year: 2017
  ident: ref_65
  article-title: Role of Glutathione-S-transferases in neurological problems
  publication-title: Expert Opin. Ther. Pat.
  doi: 10.1080/13543776.2017.1254192
– volume: 276
  start-page: 20999
  year: 2001
  ident: ref_26
  article-title: Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M101355200
– volume: 11
  start-page: 2981
  year: 2005
  ident: ref_129
  article-title: Single nucleotide polymorphism of pi-class glutathione s-transferase and susceptibility to endometrial carcinoma
  publication-title: Clin. Cancer Res.
  doi: 10.1158/1078-0432.CCR-04-2038
– volume: 360
  start-page: 1
  year: 2001
  ident: ref_2
  article-title: Structure, function and evolution of glutathione transferases: Implications for classification of non-mammalian members of an ancient enzyme superfamily
  publication-title: Biochem. J.
  doi: 10.1042/bj3600001
– volume: 19
  start-page: 226
  year: 2005
  ident: ref_184
  article-title: Erythrocyte antioxidant defense response against cigarette smoking in humans--the glutathione S-transferase vulnerability
  publication-title: J. Biochem. Mol. Toxicol.
  doi: 10.1002/jbt.20088
– volume: 12
  start-page: 354
  year: 2006
  ident: ref_138
  article-title: Epidemiology of gastric cancer
  publication-title: World J. Gastroenterol.
  doi: 10.3748/wjg.v12.i3.354
– volume: 15
  start-page: 268
  year: 1992
  ident: ref_185
  article-title: Biological effect monitoring
  publication-title: Arch. Toxicol. Suppl.
  doi: 10.1007/978-3-642-77260-3_35
– volume: 118
  start-page: 77
  year: 2018
  ident: ref_74
  article-title: [The activity of erythrocyte and platelet glutathione reductase and glutathione-S-transferase in paranoid schizophrenia]
  publication-title: Zh. Nevrol. Psikhiatr. Im. S S Korsakova
  doi: 10.17116/jnevro201811811177
– volume: 1823
  start-page: 1767
  year: 2012
  ident: ref_91
  article-title: Glutathione and modulation of cell apoptosis
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbamcr.2012.06.019
– volume: 280
  start-page: 42172
  year: 2005
  ident: ref_12
  article-title: Nitrosylation of human glutathione transferase P1-1 with dinitrosyl diglutathionyl iron complex in vitro and in vivo
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M507916200
– volume: 91
  start-page: e60
  year: 2012
  ident: ref_119
  article-title: Association of GSTP1 gene (I105V) polymorphism with acute leukaemia
  publication-title: J. Genet.
– volume: 998
  start-page: 7
  year: 1989
  ident: ref_15
  article-title: A rapid equilibrium random sequential bi-bi mechanism for human placental glutathione S-transferase
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/0167-4838(89)90111-8
– volume: 45
  start-page: 325
  year: 2000
  ident: ref_162
  article-title: Loss of inhibitory growth regulation by TGF-beta1 in preneoplastic lesions in rat liver
  publication-title: Dig. Dis. Sci.
  doi: 10.1023/A:1005464610585
– ident: ref_135
  doi: 10.1186/1471-2407-12-196
– volume: 284
  start-page: 1717
  year: 1998
  ident: ref_21
  article-title: Mutations of Gly to Ala in human glutathione transferase P1-1 affect helix 2 (G-site) and induce positive cooperativity in the binding of glutathione
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1998.2270
– volume: 63
  start-page: 196
  year: 2009
  ident: ref_72
  article-title: Is schizophrenia a neurodegenerative disorder?
  publication-title: Nord. J. Psychiatry
  doi: 10.1080/08039480902767286
– volume: 81
  start-page: 328
  year: 1985
  ident: ref_179
  article-title: Inhibition of human glutathione S-transferases by 2,4-dichlorophenoxyacetate (2,4-D) and 2,4,5-trichlorophenoxyacetate (2,4,5-T)
  publication-title: Toxicol. Appl. Pharmacol.
  doi: 10.1016/0041-008X(85)90170-X
– volume: 32
  start-page: 1213
  year: 2013
  ident: ref_183
  article-title: Pesticides-induced biochemical alterations in occupational North Indian suburban population
  publication-title: Hum. Exp. Toxicol.
  doi: 10.1177/0960327112474835
– volume: 82
  start-page: 10
  year: 2015
  ident: ref_54
  article-title: Glutathione transferases and neurodegenerative diseases
  publication-title: Neurochem. Int.
  doi: 10.1016/j.neuint.2015.01.008
– volume: 118
  start-page: 902
  year: 2011
  ident: ref_60
  article-title: Glutathione-S-transferase P1 is a critical regulator of Cdk5 kinase activity
  publication-title: J. Neurochem.
  doi: 10.1111/j.1471-4159.2011.07343.x
– volume: 51
  start-page: 299
  year: 2011
  ident: ref_107
  article-title: The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer
  publication-title: Free Radic. Biol. Med.
  doi: 10.1016/j.freeradbiomed.2011.04.013
– volume: 443
  start-page: 787
  year: 2006
  ident: ref_103
  article-title: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
  publication-title: Nature
  doi: 10.1038/nature05292
– volume: 69
  start-page: 635
  year: 2018
  ident: ref_164
  article-title: Genetic inactivation of Nrf2 prevents clonal expansion of initiated cells in a nutritional model of rat hepatocarcinogenesis
  publication-title: J. Hepatol.
  doi: 10.1016/j.jhep.2018.05.010
– volume: 21
  start-page: S42
  year: 2003
  ident: ref_82
  article-title: Assessment of disease severity and prognosis
  publication-title: Clin. Exp. Rheumatol.
– volume: 18
  start-page: 3771
  year: 1998
  ident: ref_133
  article-title: Limitations in the use of glutathione S-transferase P1 in urine as a marker for bladder cancer
  publication-title: Anticancer. Res.
– volume: 25
  start-page: 846
  year: 2010
  ident: ref_142
  article-title: Genetic polymorphism of GSTP1: Prediction of clinical outcome to oxaliplatin/5-FU-based chemotherapy in advanced gastric cancer
  publication-title: J. Korean Med. Sci.
  doi: 10.3346/jkms.2010.25.6.846
– volume: 51
  start-page: 219
  year: 2014
  ident: ref_43
  article-title: Erythrocyte glutathione transferase activity: A possible early biomarker for blood toxicity in uremic diabetic patients
  publication-title: Acta Diabetol.
  doi: 10.1007/s00592-013-0497-3
– volume: 18
  start-page: 20
  year: 2018
  ident: ref_182
  article-title: Do Glutathione S-Transferase Genes Modify the Link between Indoor Air Pollution and Asthma, Allergies, and Lung Function? A Systematic Review
  publication-title: Curr. Allergy Asthma Rep.
  doi: 10.1007/s11882-018-0771-0
– volume: 338
  start-page: 1042
  year: 1998
  ident: ref_40
  article-title: Homocysteine and atherothrombosis
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJM199804093381507
– volume: 424
  start-page: 53
  year: 2013
  ident: ref_115
  article-title: Gene methylation in gastric cancer
  publication-title: Clin. Chim. Acta
  doi: 10.1016/j.cca.2013.05.002
– volume: 216
  start-page: 579
  year: 1993
  ident: ref_11
  article-title: A glutathione S-transferase with glutathione-peroxidase activity from Arabidopsis thaliana. Molecular cloning and functional characterization
  publication-title: Eur. J. Biochem.
  doi: 10.1111/j.1432-1033.1993.tb18177.x
– ident: ref_130
  doi: 10.1101/cshperspect.a030361
– volume: 2
  start-page: 16026
  year: 2016
  ident: ref_96
  article-title: Is low-protein diet a possible risk factor of malnutrition in chronic kidney disease patients?
  publication-title: Cell Death Discov.
  doi: 10.1038/cddiscovery.2016.26
– volume: 41
  start-page: 6167
  year: 2014
  ident: ref_86
  article-title: Genetic polymorphisms of glutathione S-transferases and cytochrome P450 enzymes as susceptibility factors to systemic lupus erythematosus in southern Brazilian patients
  publication-title: Mol. Biol. Rep.
  doi: 10.1007/s11033-014-3496-8
– volume: 25
  start-page: 5787
  year: 2006
  ident: ref_29
  article-title: Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1209576
– volume: 47
  start-page: 958
  year: 2015
  ident: ref_51
  article-title: Living-donor and Deceased-donor Renal Transplantation: Differences in Early Outcome--A Single-center Experience
  publication-title: Transpl. Proc.
  doi: 10.1016/j.transproceed.2015.03.008
– volume: 28
  start-page: 129
  year: 2015
  ident: ref_45
  article-title: The possible role of glutathione-S-transferase activity in diabetic nephropathy
  publication-title: Int. J. Immunopathol. Pharmacol.
  doi: 10.1177/0394632015572564
– volume: 8
  start-page: 2096
  year: 2018
  ident: ref_147
  article-title: Predictive value of ERCC1, ERCC2, ERCC4, and glutathione S-Transferase Pi expression for the efficacy and safety of FOLFIRINOX in patients with unresectable pancreatic cancer
  publication-title: Am. J. Cancer Res.
– ident: ref_99
– volume: 274
  start-page: 84
  year: 1997
  ident: ref_5
  article-title: The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution
  publication-title: J. Mol. Biol.
  doi: 10.1006/jmbi.1997.1364
– volume: 21
  start-page: S39
  year: 2003
  ident: ref_83
  article-title: Assessment of disease activity
  publication-title: Clin. Exp. Rheumatol.
– volume: 28
  start-page: 1247
  year: 1998
  ident: ref_161
  article-title: Fibrosis accelerates the development of enzyme-altered lesions in the rat liver
  publication-title: Hepatology
  doi: 10.1002/hep.510280512
– volume: 30
  start-page: 1003
  year: 2005
  ident: ref_68
  article-title: A study of glutathione S-transferase pi expression in central nervous system of subjects with amyotrophic lateral sclerosis using RNA extraction from formalin-fixed, paraffin-embedded material
  publication-title: Neurochem. Res.
  doi: 10.1007/s11064-005-6771-1
– volume: 17
  start-page: 13
  year: 2007
  ident: ref_102
  article-title: Mitochondrial ROS--radical detoxification, mediated by protein kinase D
  publication-title: Trends Cell Biol.
  doi: 10.1016/j.tcb.2006.11.003
– volume: 31
  start-page: 773
  year: 2016
  ident: ref_196
  article-title: The effects of some avermectins on bovine carbonic anhydrase enzyme
  publication-title: J. Enzym. Inhib. Med. Chem.
  doi: 10.3109/14756366.2015.1064406
– volume: 61
  start-page: 154
  year: 2000
  ident: ref_104
  article-title: Glutathione S-transferase polymorphisms and their biological consequences
  publication-title: Pharmacology
  doi: 10.1159/000028396
– volume: 109
  start-page: 840
  year: 2007
  ident: ref_146
  article-title: Glutathione S-transferase gene polymorphisms and risk and survival of pancreatic cancer
  publication-title: Cancer
  doi: 10.1002/cncr.22468
– volume: 12
  start-page: 1
  year: 2015
  ident: ref_78
  article-title: Interaction between GSTT1 and GSTP1 allele variants as a risk modulating-factor for autism spectrum disorders
  publication-title: Res. Autism Spectr. Disord.
  doi: 10.1016/j.rasd.2014.12.008
– volume: 29
  start-page: 161
  year: 2008
  ident: ref_166
  article-title: Alpha-lipoic acid promotes the growth of rat hepatic pre-neoplastic lesions in the choline-deficient model
  publication-title: Carcinogenesis
  doi: 10.1093/carcin/bgm205
– volume: 426
  start-page: 71
  year: 2012
  ident: ref_177
  article-title: Erythrocyte glutathione transferase: A novel biomarker to check environmental pollution hazardous for humans
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2012.08.037
– volume: 32
  start-page: 173
  year: 1969
  ident: ref_189
  article-title: The role of glutathione and glutathione S-transferases in mercapturic acid biosynthesis
  publication-title: Adv. Enzymol. Relat. Areas Mol. Biol.
  doi: 10.1002/9780470122778.ch5
– volume: 187
  start-page: 454
  year: 2011
  ident: ref_75
  article-title: Genetic polymorphisms of glutathione S-transferases GSTM1, GSTT1, GSTP1 and GSTA1 as risk factors for schizophrenia
  publication-title: Psychiatry Res.
  doi: 10.1016/j.psychres.2010.10.008
– volume: 7
  start-page: 8
  year: 2018
  ident: ref_57
  article-title: Glutathione transferases: Substrates, inihibitors and pro-drugs in cancer and neurodegenerative diseases
  publication-title: Oncogenesis
  doi: 10.1038/s41389-017-0025-3
– volume: 52
  start-page: S14
  year: 2013
  ident: ref_93
  article-title: Epigenetics and early life origins of chronic noncommunicable diseases
  publication-title: J. Adolesc. Health
  doi: 10.1016/j.jadohealth.2012.04.019
– volume: 57
  start-page: 512
  year: 2010
  ident: ref_149
  article-title: CYP and GST polymorphisms and survival in advanced non-small cell lung cancer patients
  publication-title: Neoplasma
  doi: 10.4149/neo_2010_06_512
– volume: 32
  start-page: e22205
  year: 2018
  ident: ref_195
  article-title: The toxicological impact of some avermectins on human erythrocytes glutathione S-transferase enzyme
  publication-title: J. Biochem. Mol. Toxicol.
  doi: 10.1002/jbt.22205
– volume: 119
  start-page: 47
  year: 2019
  ident: ref_73
  article-title: [The activity of enzymes of glutathione metabolism in blood cells of patients with a high risk of manifestation of endogenous psychoses and patients with the first psychotic episode]
  publication-title: Zh. Nevrol. Psikhiatr. Im. S S Korsakova
  doi: 10.17116/jnevro201911904147
– volume: 18
  start-page: 349
  year: 2010
  ident: ref_141
  article-title: Genetic polymorphisms in GSTA1, GSTP1, GSTT1, and GSTM1 and gastric cancer risk in a Vietnamese population
  publication-title: Oncol. Res.
  doi: 10.3727/096504010X12626118080064
– volume: 75
  start-page: 241
  year: 1990
  ident: ref_188
  article-title: Glutathione S-transferases in relation to their role in the biotransformation of xenobiotics
  publication-title: Chem. Biol. Interact.
  doi: 10.1016/0009-2797(90)90069-Y
– volume: 152
  start-page: 3
  year: 2009
  ident: ref_155
  article-title: The epidemiology of osteosarcoma
  publication-title: Cancer Treat. Res.
  doi: 10.1007/978-1-4419-0284-9_1
– volume: 270
  start-page: 1243
  year: 1995
  ident: ref_16
  article-title: Site-directed mutagenesis of human glutathione transferase P1-1. Mutation of Cys-47 induces a positive cooperativity in glutathione transferase P1-1
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.270.3.1243
– volume: 4
  start-page: e736
  year: 2013
  ident: ref_84
  article-title: Erythrocyte glutathione transferase: A non-antibody biomarker for systemic sclerosis, which correlates with severity and activity of the disease
  publication-title: Cell Death Dis.
  doi: 10.1038/cddis.2013.255
– volume: 45
  start-page: 51
  year: 2005
  ident: ref_1
  article-title: Glutathione transferases
  publication-title: Annu. Rev. Pharmacol. Toxicol.
  doi: 10.1146/annurev.pharmtox.45.120403.095857
– volume: 53
  start-page: 8
  year: 2014
  ident: ref_131
  article-title: Protection against oxidative DNA damage and stress in human prostate by glutathione S-transferase P1
  publication-title: Mol. Carcinog.
  doi: 10.1002/mc.21939
– volume: 163
  start-page: 1101
  year: 2003
  ident: ref_159
  article-title: Aberrant promoter methylation profiles of tumor suppressor genes in hepatocellular carcinoma
  publication-title: Am. J. Pathol.
  doi: 10.1016/S0002-9440(10)63469-4
– volume: 16
  start-page: 72
  year: 2015
  ident: ref_67
  article-title: Modification of the association between lead exposure and amyotrophic lateral sclerosis by iron and oxidative stress related gene polymorphisms
  publication-title: Amyotroph. Lateral Scler. Front. Degener.
  doi: 10.3109/21678421.2014.964259
– volume: 24
  start-page: 417
  year: 2015
  ident: ref_157
  article-title: The association of glutathione S-transferase polymorphisms in patients with osteosarcoma: Evidence from a meta-analysis
  publication-title: Eur. J. Cancer Care (Engl.)
  doi: 10.1111/ecc.12197
– volume: 50
  start-page: 1005
  year: 2009
  ident: ref_117
  article-title: Polymorphisms of glutathione S-transferase Mu 1, glutathione S-transferase theta 1 and glutathione S-transferase Pi 1 genes in Hodgkin’s lymphoma susceptibility and progression
  publication-title: Leuk. Lymphoma
  doi: 10.1080/10428190902878455
– volume: 776
  start-page: 118
  year: 2015
  ident: ref_92
  article-title: DNA damage in non-communicable diseases: A clinical and epidemiological perspective
  publication-title: Mutat. Res.
  doi: 10.1016/j.mrfmmm.2014.11.009
– volume: 28
  start-page: 1456
  year: 2000
  ident: ref_101
  article-title: Reactive oxygen species, cell signaling, and cell injury
  publication-title: Free Radic. Biol. Med.
  doi: 10.1016/S0891-5849(00)00252-5
– volume: 25
  start-page: 805
  year: 2014
  ident: ref_89
  article-title: Oxidative stress and genetic markers of suboptimal antioxidant defense in the aging brain: A theoretical review
  publication-title: Rev. Neurosci.
  doi: 10.1515/revneuro-2014-0046
– volume: 1830
  start-page: 3350
  year: 2013
  ident: ref_111
  article-title: Glutathione and glutathione analogues; therapeutic potentials
  publication-title: Biochim. Biophys. Acta
  doi: 10.1016/j.bbagen.2012.11.016
– volume: 377
  start-page: 942
  year: 2011
  ident: ref_66
  article-title: Amyotrophic lateral sclerosis
  publication-title: Lancet
  doi: 10.1016/S0140-6736(10)61156-7
– volume: 268
  start-page: 19033
  year: 1993
  ident: ref_17
  article-title: Peculiar spectroscopic and kinetic properties of Cys-47 in human placental glutathione transferase. Evidence for an atypical thiolate ion pair near the active site
  publication-title: J. Biol. Chem.
  doi: 10.1016/S0021-9258(17)46731-7
– volume: 16
  start-page: 375
  year: 2000
  ident: ref_165
  article-title: Angiogenesis inhibitor TNP-470 suppresses the progression of experimentally-induced hepatocellular carcinoma in rats
  publication-title: Int. J. Oncol.
– ident: ref_168
  doi: 10.1186/1471-2350-11-46
– volume: 35
  start-page: 9897
  year: 2014
  ident: ref_158
  article-title: Predictive potential of ABCB1, ABCC3, and GSTP1 gene polymorphisms on osteosarcoma survival after chemotherapy
  publication-title: Tumour Biol.
  doi: 10.1007/s13277-014-1917-x
– volume: 1
  start-page: 93
  year: 2011
  ident: ref_186
  article-title: A Study on Oxidative Stress Biomarkers and Immunomodulatory Effects of Pesticides in Pesticide-Sprayers
  publication-title: Egypt. J. Forensic Sci.
  doi: 10.1016/j.ejfs.2011.04.012
– volume: 79
  start-page: 516
  year: 1961
  ident: ref_3
  article-title: An enzyme from rat liver catalysing conjugations with glutathione
  publication-title: Biochem. J.
  doi: 10.1042/bj0790516
– volume: 71
  start-page: 446
  year: 2013
  ident: ref_59
  article-title: Exposure to pesticides and heterozygote genotype of GSTP1-Alw26I are associated to Parkinson’s disease
  publication-title: Arq. Neuropsiquiatr.
  doi: 10.1590/0004-282X20130060
– volume: 30
  start-page: 445
  year: 1995
  ident: ref_192
  article-title: The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
  publication-title: Crit. Rev. Biochem. Mol. Biol.
  doi: 10.3109/10409239509083491
– volume: 292
  start-page: 112
  year: 2017
  ident: ref_113
  article-title: Structural and Biochemical Analyses Reveal the Mechanism of Glutathione S-Transferase Pi 1 Inhibition by the Anti-cancer Compound Piperlongumine
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M116.750299
– volume: 2
  start-page: 215
  year: 1992
  ident: ref_34
  article-title: Glutathione and its associated enzymes in peripheral blood cells in different stages of chronic renal insufficiency
  publication-title: Amino Acids
  doi: 10.1007/BF00805943
– volume: 500
  start-page: 116
  year: 2010
  ident: ref_109
  article-title: Glutathione transferases and development of new principles to overcome drug resistance
  publication-title: Arch. Biochem. Biophys.
  doi: 10.1016/j.abb.2010.05.012
– volume: 118
  start-page: 5489
  year: 2012
  ident: ref_140
  article-title: Clinical significance of SOD2 and GSTP1 gene polymorphisms in Chinese patients with gastric cancer
  publication-title: Cancer
  doi: 10.1002/cncr.27599
– volume: 49
  start-page: 1638
  year: 2010
  ident: ref_8
  article-title: Multiple roles of microsomal glutathione transferase 1 in cellular protection: A mechanistic study
  publication-title: Free Radic. Biol. Med.
  doi: 10.1016/j.freeradbiomed.2010.08.013
– volume: 45
  start-page: 1781
  year: 1999
  ident: ref_36
  article-title: Overexpression of erythrocyte glutathione S-transferase in uremia and dialysis
  publication-title: Clin. Chem.
  doi: 10.1093/clinchem/45.10.1781
– volume: 14
  start-page: 1784
  year: 2005
  ident: ref_123
  article-title: Genetic polymorphisms of glutathione S-transferases and the risk of adult brain tumors: A meta-analysis
  publication-title: Cancer Epidemiol. Biomark. Prev.
  doi: 10.1158/1055-9965.EPI-05-0105
– volume: 110
  start-page: 795
  year: 2019
  ident: ref_143
  article-title: Glutathione S-transferase Pi 1 is a valuable predictor for cancer drug resistance in esophageal squamous cell carcinoma
  publication-title: Cancer Sci.
  doi: 10.1111/cas.13896
– volume: 51
  start-page: 944
  year: 2005
  ident: ref_61
  article-title: Glutathione S-transferase P1 *C allelic variant increases susceptibility for late-onset Alzheimer disease: Association study and relationship with apolipoprotein E epsilon4 allele
  publication-title: Clin. Chem.
  doi: 10.1373/clinchem.2004.045955
– ident: ref_31
  doi: 10.1371/journal.pone.0112797
– volume: 125
  start-page: 1053
  year: 1984
  ident: ref_14
  article-title: Purification and characterization of a new form of glutathione S-transferase from human erythrocytes
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/0006-291X(84)91390-1
– volume: 25
  start-page: 1639
  year: 2006
  ident: ref_105
  article-title: Glutathione S-transferase polymorphisms: cancer incidence and therapy
  publication-title: Oncogene
  doi: 10.1038/sj.onc.1209373
– volume: 103
  start-page: 52
  year: 2005
  ident: ref_125
  article-title: Genetic polymorphisms in glutathione-S-transferase genes (GSTM1, GSTT1, GSTP1) and survival after chemotherapy for invasive breast carcinoma
  publication-title: Cancer
  doi: 10.1002/cncr.20729
– volume: 99
  start-page: 118
  year: 2010
  ident: ref_187
  article-title: Oxidative stress and antioxidant enzymes in liver and white muscle of Nile tilapia juveniles in chronic ammonia exposure
  publication-title: Aquat. Toxicol.
  doi: 10.1016/j.aquatox.2010.04.007
– volume: 10
  start-page: 2
  year: 1997
  ident: ref_4
  article-title: Structure, catalytic mechanism, and evolution of the glutathione transferases
  publication-title: Chem. Res. Toxicol.
  doi: 10.1021/tx960072x
– volume: 68
  start-page: 6661
  year: 2008
  ident: ref_108
  article-title: Overcoming glutathione S-transferase P1-related cisplatin resistance in osteosarcoma
  publication-title: Cancer Res.
  doi: 10.1158/0008-5472.CAN-07-5840
– volume: 13
  start-page: 57
  year: 2003
  ident: ref_173
  article-title: Fish bioaccumulation and biomarkers in environmental risk assessment: A review
  publication-title: Environ. Toxicol. Pharmacol.
  doi: 10.1016/S1382-6689(02)00126-6
– volume: 288
  start-page: 24936
  year: 2013
  ident: ref_6
  article-title: The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: A proposal for an evolutionary driving force
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.476135
– volume: 8
  start-page: 377
  year: 2015
  ident: ref_152
  article-title: Contribution of glutathione S-transferase gene polymorphisms to development of skin cancer
  publication-title: Int. J. Clin. Exp. Med.
– volume: 15
  start-page: 2201
  year: 1994
  ident: ref_160
  article-title: Prevention of fibrosis reduces enzyme-altered lesions in the rat liver
  publication-title: Carcinogenesis
  doi: 10.1093/carcin/15.10.2201
– volume: 37
  start-page: 943
  year: 2016
  ident: ref_170
  article-title: Glutathione S-transferase P1 gene rs4147581 polymorphism predicts overall survival of patients with hepatocellular carcinoma: Evidence from an enlarged study
  publication-title: Tumour Biol.
  doi: 10.1007/s13277-015-3871-7
– volume: 38
  start-page: 396
  year: 2009
  ident: ref_69
  article-title: Neurobiology of schizophrenia spectrum disorders: The role of oxidative stress
  publication-title: Ann. Acad Med. Singap.
  doi: 10.47102/annals-acadmedsg.V38N5p396
– volume: 35
  start-page: 4983
  year: 2014
  ident: ref_139
  article-title: Association study of SNPs of genes IFNGR1 (rs137854905), GSTT1 (rs71748309), and GSTP1 (rs1695) in gastric cancer development in samples of patient in the northern and northeastern Brazil
  publication-title: Tumour. Biol.
– volume: 6
  start-page: 483
  year: 2010
  ident: ref_172
  article-title: Air pollution and non-respiratory health hazards for children
  publication-title: Arch. Med. Sci.
  doi: 10.5114/aoms.2010.14458
– ident: ref_64
  doi: 10.1186/1471-2202-9-67
– volume: 106
  start-page: 441
  year: 2006
  ident: ref_148
  article-title: Association between glutathione S-transferase pi polymorphisms and survival in patients with advanced nonsmall cell lung carcinoma
  publication-title: Cancer
  doi: 10.1002/cncr.21619
– volume: 3
  start-page: e377
  year: 2012
  ident: ref_41
  article-title: Erythrocyte glutathione transferase: A new biomarker for hemodialysis adequacy, overcoming the Kt/V(urea) dogma?
  publication-title: Cell Death Dis.
  doi: 10.1038/cddis.2012.112
– volume: 67
  start-page: 302
  year: 2017
  ident: ref_163
  article-title: Global trends and predictions in hepatocellular carcinoma mortality
  publication-title: J. Hepatol.
  doi: 10.1016/j.jhep.2017.03.011
– volume: 50
  start-page: 235
  year: 1996
  ident: ref_48
  article-title: A study of the quality of life and cost-utility of renal transplantation
  publication-title: Kidney Int.
  doi: 10.1038/ki.1996.307
– volume: 53
  start-page: 299
  year: 1984
  ident: ref_180
  article-title: Decreased erythrocyte glutathione s-transferase activity in rubber workers
  publication-title: Int. Arch. Occup. Environ. Health
  doi: 10.1007/BF00380668
– volume: 125
  start-page: 253
  year: 2011
  ident: ref_124
  article-title: Glutathione S-transferase P1 Ile105Val polymorphism and breast cancer risk: A meta-analysis involving 34,658 subjects
  publication-title: Breast Cancer Res. Treat.
  doi: 10.1007/s10549-010-0969-x
– volume: 15
  start-page: 52
  year: 2016
  ident: ref_94
  article-title: Three week dietary intervention using apricots, pomegranate juice or/and fermented sour sobya and impact on biomarkers of antioxidative activity, oxidative stress and erythrocytic glutathione transferase activity among adults
  publication-title: Nutr. J.
  doi: 10.1186/s12937-016-0173-x
– volume: 341
  start-page: 1725
  year: 1999
  ident: ref_47
  article-title: Comparison of mortality in all patients on dialysis, patients on dialysis awaiting transplantation, and recipients of a first cadaveric transplant
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJM199912023412303
– volume: 23
  start-page: 1965
  year: 2016
  ident: ref_50
  article-title: Molecular Dissection of Renal Ischemia-Reperfusion: Oxidative Stress and Cellular Events
  publication-title: Curr. Med. Chem.
  doi: 10.2174/0929867323666160112122858
– volume: 46
  start-page: 1617
  year: 2010
  ident: ref_137
  article-title: GSTM1, GSTT1, GSTP1, GSTA1 and colorectal cancer risk: A comprehensive meta-analysis
  publication-title: Eur. J. Cancer
  doi: 10.1016/j.ejca.2010.02.009
– ident: ref_150
  doi: 10.1371/journal.pmed.0030091
– ident: ref_156
  doi: 10.4238/gmr.15038034
– volume: 14
  start-page: S486
  year: 2018
  ident: ref_169
  article-title: Clinical significance and association of GSTP1 hypermethylation with hepatocellular carcinoma: A meta-analysis
  publication-title: J. Cancer Res. Ther.
  doi: 10.4103/0973-1482.181179
– volume: 9
  start-page: 288
  year: 2018
  ident: ref_49
  article-title: Erythrocyte glutathione transferase in kidney transplantation: A probe for kidney detoxification efficiency
  publication-title: Cell Death Dis.
  doi: 10.1038/s41419-018-0289-3
– volume: 5
  start-page: 170
  year: 2014
  ident: ref_120
  article-title: Regulation of epigenetic traits of the glutathione S-transferase P1 gene: From detoxification toward cancer prevention and diagnosis
  publication-title: Front. Pharmacol.
  doi: 10.3389/fphar.2014.00170
– volume: 275
  start-page: 29207
  year: 2000
  ident: ref_27
  article-title: A novel plant glutathione S-transferase/peroxidase suppresses Bax lethality in yeast
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M002359200
– volume: 122
  start-page: 656
  year: 2016
  ident: ref_110
  article-title: A novel class of ethacrynic acid derivatives as promising drug-like potent generation of anticancer agents with established mechanism of action
  publication-title: Eur. J. Med. Chem.
  doi: 10.1016/j.ejmech.2016.05.063
– volume: 25
  start-page: 1605
  year: 2004
  ident: ref_35
  article-title: UCSF Chimera—A visualization system for exploratory research and analysis
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.20084
– volume: 291
  start-page: 26739
  year: 2016
  ident: ref_25
  article-title: Evolution of Negative Cooperativity in Glutathione Transferase Enabled Preservation of Enzyme Function
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M116.749507
– ident: ref_46
– volume: 4
  start-page: 2234
  year: 2004
  ident: ref_56
  article-title: Identification of post-mortem cerebrospinal fluid proteins as potential biomarkers of ischemia and neurodegeneration
  publication-title: Proteomics
  doi: 10.1002/pmic.200300822
– ident: ref_95
  doi: 10.3390/nu11051073
– volume: 433
  start-page: 33
  year: 2018
  ident: ref_106
  article-title: The multifaceted role of glutathione S-transferases in cancer
  publication-title: Cancer Lett.
  doi: 10.1016/j.canlet.2018.06.028
– volume: 116
  start-page: 2242
  year: 2010
  ident: ref_122
  article-title: Glutathione S-transferase polymorphisms are associated with survival in anaplastic glioma patients
  publication-title: Cancer
  doi: 10.1002/cncr.25006
– volume: 11
  start-page: 461
  year: 2010
  ident: ref_118
  article-title: Association of the GSTP1 gene (Ile105Val) polymorphism with chronic myeloid leukemia
  publication-title: Asian Pac. J. Cancer Prev.
– volume: 43
  start-page: 347
  year: 2012
  ident: ref_38
  article-title: Erythrocyte glutathione transferase: A potential new biomarker in chronic kidney diseases which correlates with plasma homocysteine
  publication-title: Amino Acids
  doi: 10.1007/s00726-011-1085-x
– volume: 24
  start-page: 3789
  year: 2006
  ident: ref_144
  article-title: Genetic variations in radiation and chemotherapy drug action pathways predict clinical outcomes in esophageal cancer
  publication-title: J. Clin. Oncol.
  doi: 10.1200/JCO.2005.03.6640
– volume: 6
  start-page: 281
  year: 2009
  ident: ref_132
  article-title: Glutathione S-transferases in kidney and urinary bladder tumors
  publication-title: Nat. Rev. Urol.
  doi: 10.1038/nrurol.2009.49
– volume: 39
  start-page: 9
  year: 1997
  ident: ref_193
  article-title: Erythrocyte glutathione-S-transferase activity in animal species
  publication-title: Vet. Hum. Toxicol.
– volume: 164
  start-page: 2126
  year: 2000
  ident: ref_134
  article-title: Plasma glutathione S-transferase pi 1-1 AND alpha 1-1 levels in patients with bladder cancer
  publication-title: J. Urol.
  doi: 10.1016/S0022-5347(05)66982-0
– volume: 46
  start-page: 439
  year: 2008
  ident: ref_62
  article-title: Glutathione S-transferase variants increase susceptibility for late-onset Alzheimer’s disease: Association study and relationship with apolipoprotein E epsilon4 allele
  publication-title: Clin. Chem. Lab. Med.
  doi: 10.1515/CCLM.2008.102
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Snippet Glutathione transferase P1-1 (GSTP1-1) is expressed in some human tissues and is abundant in mammalian erythrocytes (here termed e-GST). This enzyme is able to...
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SubjectTerms Animals
autoimmune diseases
behavior disorders
Biomarkers
Biomarkers - blood
biosensors
dialysis
Environmental Exposure - adverse effects
Environmental Monitoring - methods
Environmental Pollutants - adverse effects
erythrocytes
Erythrocytes - drug effects
Erythrocytes - enzymology
Glutathione
Glutathione S-Transferase pi - blood
Glutathione S-Transferase pi - genetics
glutathione transferase
Health Status
Health Status Indicators
Hemodialysis
Humans
kidney diseases
kidney transplant
Kidney transplants
kidneys
liver
medicine
monitoring
neoplasms
neurodegenerative diseases
oxidative stress
Oxidative Stress - drug effects
pathogenesis
patients
pollution
Predictive Value of Tests
Review
Risk Assessment
Risk Factors
tissues
toxicity
toxins
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Title Glutathione Transferase P1-1 an Enzyme Useful in Biomedicine and as Biomarker in Clinical Practice and in Environmental Pollution
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Volume 11
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