메뉴 건너뛰기




Volumn 1760, Issue 7, 2006, Pages 1064-1070

Metabolism of oxidized linoleic acid by glutathione transferases: Peroxidase activity toward 13-hydroperoxyoctadecadienoic acid

Author keywords

13 HODE; 13 HPODE; Enzyme induction; Glutathione transferase; Oxidized linoleic acid metabolism

Indexed keywords

13 HYDROPEROXYOCTADECADIENOIC ACID; FATTY ACID; GLUTATHIONE TRANSFERASE; GLUTATHIONE TRANSFERASE A1; GLUTATHIONE TRANSFERASE M1; GLUTATHIONE TRANSFERASE M2; GLUTATHIONE TRANSFERASE P1; LINOLEIC ACID; PEROXIDASE; UNCLASSIFIED DRUG;

EID: 33744993869     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.02.020     Document Type: Article
Times cited : (16)

References (38)
  • 1
    • 0037052584 scopus 로고    scopus 로고
    • Conjugation of the linoleic acid oxidation product, 13-oxooctadeca-9,11-dienoic acid, a bioactive endogenous substrate for mammalian glutathione transferase
    • Bull A.W., Seeley S.K., Geno J.L., and Mannervik B. Conjugation of the linoleic acid oxidation product, 13-oxooctadeca-9,11-dienoic acid, a bioactive endogenous substrate for mammalian glutathione transferase. Biochim. Biophys. Acta 1571 (2002) 77-82
    • (2002) Biochim. Biophys. Acta , vol.1571 , pp. 77-82
    • Bull, A.W.1    Seeley, S.K.2    Geno, J.L.3    Mannervik, B.4
  • 2
    • 0035968443 scopus 로고    scopus 로고
    • Energy-dependent export of the 13-oxooctadecadienoic acid-glutathione conjugate from HT-29 cells and plasma membrane vesicles
    • Podgorski I., and Bull A.W. Energy-dependent export of the 13-oxooctadecadienoic acid-glutathione conjugate from HT-29 cells and plasma membrane vesicles. Biochim. Biophys. Acta 1533 (2001) 55-65
    • (2001) Biochim. Biophys. Acta , vol.1533 , pp. 55-65
    • Podgorski, I.1    Bull, A.W.2
  • 3
    • 0030852873 scopus 로고    scopus 로고
    • The linoleic acid metabolite, (13S)-hydroperoxyoctadecadienoic acid, augments the epidermal growth factor receptor signaling pathway by attenuation of receptor phosphorylation
    • Glasgow W.C., Hui R., Everhart A.L., Jayawickreme S.P., Angerman-Stewart J., Han B.B., and Eling T.E. The linoleic acid metabolite, (13S)-hydroperoxyoctadecadienoic acid, augments the epidermal growth factor receptor signaling pathway by attenuation of receptor phosphorylation. J. Biol. Chem. 272 (1997) 19269-19276
    • (1997) J. Biol. Chem. , vol.272 , pp. 19269-19276
    • Glasgow, W.C.1    Hui, R.2    Everhart, A.L.3    Jayawickreme, S.P.4    Angerman-Stewart, J.5    Han, B.B.6    Eling, T.E.7
  • 4
    • 0027333092 scopus 로고
    • Increases in 13-hydroxyoctadecadienoic acid (13-HODE) dehydrogenase activity during differentiation of cultured cells
    • Bull A.W., Branting C., Bronstein J.C., Blackburn M.L., and Rafter J.J. Increases in 13-hydroxyoctadecadienoic acid (13-HODE) dehydrogenase activity during differentiation of cultured cells. Carcinogenesis 14 (1993) 2239-2243
    • (1993) Carcinogenesis , vol.14 , pp. 2239-2243
    • Bull, A.W.1    Branting, C.2    Bronstein, J.C.3    Blackburn, M.L.4    Rafter, J.J.5
  • 5
    • 0027524755 scopus 로고
    • The correlation between 13-hydroxyoctadecadienoate dehydrogenase (13-HODE dehydrogenase) and intestinal cell differentiation
    • Bronstein J.C., and Bull A.W. The correlation between 13-hydroxyoctadecadienoate dehydrogenase (13-HODE dehydrogenase) and intestinal cell differentiation. Prostaglandins 46 (1993) 387-395
    • (1993) Prostaglandins , vol.46 , pp. 387-395
    • Bronstein, J.C.1    Bull, A.W.2
  • 6
    • 33846304505 scopus 로고    scopus 로고
    • Decreased levels of 13-hydroxyoctadecadienoic acid (13-HODE) dehydrogenase in neoplastic tissue of human colon biopsies
    • Silverman A.L., Bronstein J.C., Krymgold S.K., Kahlon D., and Bull A.W. Decreased levels of 13-hydroxyoctadecadienoic acid (13-HODE) dehydrogenase in neoplastic tissue of human colon biopsies. Cancer Epidemiol. Biomark. Prev. 5 (1996) 53-56
    • (1996) Cancer Epidemiol. Biomark. Prev. , vol.5 , pp. 53-56
    • Silverman, A.L.1    Bronstein, J.C.2    Krymgold, S.K.3    Kahlon, D.4    Bull, A.W.5
  • 7
    • 0242661076 scopus 로고    scopus 로고
    • Activation of PPAR γ in colon tumor cell lines by oxidized metabolites of linoleic acid, endogenous ligands for PPAR γ
    • Bull A.W., Steffensen K.R., Leers J., and Rafter J.J. Activation of PPAR γ in colon tumor cell lines by oxidized metabolites of linoleic acid, endogenous ligands for PPAR γ. Carcinogenesis 24 (2003) 1717-1722
    • (2003) Carcinogenesis , vol.24 , pp. 1717-1722
    • Bull, A.W.1    Steffensen, K.R.2    Leers, J.3    Rafter, J.J.4
  • 8
    • 0028596944 scopus 로고
    • Cellular proliferation and lipid metabolism: importance of lipoxygenases in modulating epidermal growth factor-dependent mitogenesis
    • Eling T.E., and Glasgow W.C. Cellular proliferation and lipid metabolism: importance of lipoxygenases in modulating epidermal growth factor-dependent mitogenesis. Cancer Metastasis Rev. 13 (1994) 397-410
    • (1994) Cancer Metastasis Rev. , vol.13 , pp. 397-410
    • Eling, T.E.1    Glasgow, W.C.2
  • 9
    • 0025089257 scopus 로고
    • Production of unsaturated carbonyl compounds during metabolism of hydroperoxy fatty acids by colonic homogenates
    • Bull A.W., and Bronstein J.C. Production of unsaturated carbonyl compounds during metabolism of hydroperoxy fatty acids by colonic homogenates. Carcinogenesis 11 (1990) 1699-1704
    • (1990) Carcinogenesis , vol.11 , pp. 1699-1704
    • Bull, A.W.1    Bronstein, J.C.2
  • 10
    • 0031550553 scopus 로고    scopus 로고
    • Characterization of a 15-lipoxygenase in human breast carcinoma BT-20 cells: Stimulation of 13-HODE formation by TGF alpha/EGF
    • Reddy N., Everhart A., Eling T.E., and Glasgow W. Characterization of a 15-lipoxygenase in human breast carcinoma BT-20 cells: Stimulation of 13-HODE formation by TGF alpha/EGF. Biochem. Biophys. Res. Commun. 231 (1997) 111-116
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 111-116
    • Reddy, N.1    Everhart, A.2    Eling, T.E.3    Glasgow, W.4
  • 11
    • 0033568522 scopus 로고    scopus 로고
    • 13-Hydroxyoctadecadienoic acid is the mitogenic signal for linoleic acid-dependent growth in rat hepatoma 7288CTC in vivo
    • Sauer L.A., Dauchy R.T., Blask D.E., Armstrong B.J., and Scalici S. 13-Hydroxyoctadecadienoic acid is the mitogenic signal for linoleic acid-dependent growth in rat hepatoma 7288CTC in vivo. Cancer Res. 59 (1999) 4688-4692
    • (1999) Cancer Res. , vol.59 , pp. 4688-4692
    • Sauer, L.A.1    Dauchy, R.T.2    Blask, D.E.3    Armstrong, B.J.4    Scalici, S.5
  • 12
  • 13
    • 0017380842 scopus 로고
    • Glutathione peroxidase activity of glutathione-s-transferases purified from rat liver
    • Prohaska J.R., and Ganther H.E. Glutathione peroxidase activity of glutathione-s-transferases purified from rat liver. Biochem. Biophys. Res. Commun. 76 (1976) 437-445
    • (1976) Biochem. Biophys. Res. Commun. , vol.76 , pp. 437-445
    • Prohaska, J.R.1    Ganther, H.E.2
  • 14
    • 0019071999 scopus 로고
    • Interrelationship between anionic and cationic forms of glutathione-S-transferases of human liver
    • Awasthi Y.C., Dao D.D., and Saneto R.P. Interrelationship between anionic and cationic forms of glutathione-S-transferases of human liver. Biochem. J. 191 (1980) 1-10
    • (1980) Biochem. J. , vol.191 , pp. 1-10
    • Awasthi, Y.C.1    Dao, D.D.2    Saneto, R.P.3
  • 15
    • 0000107746 scopus 로고
    • Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties
    • Mannervik B., Ålin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., and Jörnvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 7202-7206
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 7202-7206
    • Mannervik, B.1    Ålin, P.2    Guthenberg, C.3    Jensson, H.4    Tahir, M.K.5    Warholm, M.6    Jörnvall, H.7
  • 18
    • 0032524233 scopus 로고    scopus 로고
    • Phospholipid hydroperoxide glutathione transferase activity of human glutathione transferases
    • Hurst R., Bao Y., Jemth P., Mannervik B., and Williamson G. Phospholipid hydroperoxide glutathione transferase activity of human glutathione transferases. Biochem. J. 332 (1998) 97-100
    • (1998) Biochem. J. , vol.332 , pp. 97-100
    • Hurst, R.1    Bao, Y.2    Jemth, P.3    Mannervik, B.4    Williamson, G.5
  • 19
    • 0032519517 scopus 로고    scopus 로고
    • Human glutathione transferase A 4-4: an Alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation
    • Hubatsch I., Ridderström M., and Mannervik B. Human glutathione transferase A 4-4: an Alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochem. J. 330 (1998) 175-179
    • (1998) Biochem. J. , vol.330 , pp. 175-179
    • Hubatsch, I.1    Ridderström, M.2    Mannervik, B.3
  • 20
    • 0032496408 scopus 로고    scopus 로고
    • J. Structure-activity relationships and thermal stability of human glutathione transferase P 1-1 governed by the H-site residue 105
    • Johansson A.-S., Stenberg G., Widersten M., and Mannervik B. J. Structure-activity relationships and thermal stability of human glutathione transferase P 1-1 governed by the H-site residue 105. J. Mol. Biol. 278 (1998) 687-698
    • (1998) J. Mol. Biol. , vol.278 , pp. 687-698
    • Johansson, A.-S.1    Stenberg, G.2    Widersten, M.3    Mannervik, B.4
  • 21
    • 0017264641 scopus 로고
    • Preparation and purification of lipid hydroperoxides from arachidonic and γ-linolenic acids
    • Funk M.O., Isaac R., and Porter N.A. Preparation and purification of lipid hydroperoxides from arachidonic and γ-linolenic acids. Lipids 11 (1976) 113-117
    • (1976) Lipids , vol.11 , pp. 113-117
    • Funk, M.O.1    Isaac, R.2    Porter, N.A.3
  • 22
    • 0018582136 scopus 로고
    • Preparation and purification of arachidonic acid hydroperoxides of biological importance
    • Porter N.A., Logan J., and Kontoyiannidou V. Preparation and purification of arachidonic acid hydroperoxides of biological importance. J. Org. Chem. 44 (1979) 3177-3181
    • (1979) J. Org. Chem. , vol.44 , pp. 3177-3181
    • Porter, N.A.1    Logan, J.2    Kontoyiannidou, V.3
  • 23
    • 0000463877 scopus 로고
    • Allylic hydroperoxide rearrangement: β-scission or concerted pathway
    • Porter N.A., and Wujek J.S. Allylic hydroperoxide rearrangement: β-scission or concerted pathway. J. Org. Chem. 52 (1987) 5085-5089
    • (1987) J. Org. Chem. , vol.52 , pp. 5085-5089
    • Porter, N.A.1    Wujek, J.S.2
  • 24
    • 0031444925 scopus 로고    scopus 로고
    • Characterization of the enzymatic and nonenzymatic reaction of 13-oxooctadecadienoic acid with glutathione
    • Blackburn M.L., Ketterer B., Meyer D.J., Juett A.M., and Bull A.W. Characterization of the enzymatic and nonenzymatic reaction of 13-oxooctadecadienoic acid with glutathione. Chem. Res. Toxicol. 10 (1997) 1364-1371
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 1364-1371
    • Blackburn, M.L.1    Ketterer, B.2    Meyer, D.J.3    Juett, A.M.4    Bull, A.W.5
  • 25
    • 0017067418 scopus 로고
    • Glutathione peroxidase activity in selenium deficient rat liver
    • Lawrence R.A., and Burk R.F. Glutathione peroxidase activity in selenium deficient rat liver. Biochem. Biophys. Res. Commun. 71 (1976) 952-958
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 952-958
    • Lawrence, R.A.1    Burk, R.F.2
  • 26
    • 0027051610 scopus 로고
    • Glutathione-S-transferases of human lung: characterization and evaluation of the protective role of the α-class enzymes against lipid peroxidation
    • Singhal S.S., Saxena M., Ahmad H., Awasthi S., Hague A.K., and Awasthi Y.C. Glutathione-S-transferases of human lung: characterization and evaluation of the protective role of the α-class enzymes against lipid peroxidation. Arch. Biochem. Biophys. 299 (1992) 232-241
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 232-241
    • Singhal, S.S.1    Saxena, M.2    Ahmad, H.3    Awasthi, S.4    Hague, A.K.5    Awasthi, Y.C.6
  • 27
    • 0016275313 scopus 로고
    • Glutathione S-transferases: the first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases: the first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 29
    • 0344915418 scopus 로고
    • Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis
    • Talalay P., De Long M.J., and Prochaska H.J. Identification of a common chemical signal regulating the induction of enzymes that protect against chemical carcinogenesis. Proc. Natl. Acad. Sci. 85 (1988) 8261-8265
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 8261-8265
    • Talalay, P.1    De Long, M.J.2    Prochaska, H.J.3
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0031752465 scopus 로고    scopus 로고
    • Linoleic acid peroxidation - the dominant lipid peroxidation process in low density lipoprotein - and its relationship to chronic diseases
    • Spiteller G. Linoleic acid peroxidation - the dominant lipid peroxidation process in low density lipoprotein - and its relationship to chronic diseases. Chem. Phys. Lipids 95 (1998) 105-162
    • (1998) Chem. Phys. Lipids , vol.95 , pp. 105-162
    • Spiteller, G.1
  • 32
    • 0024456697 scopus 로고
    • Biological interactions of α,β-unsaturated aldehydes
    • Witz G. Biological interactions of α,β-unsaturated aldehydes. Free Radical Biol. Med. 7 (1989) 333-349
    • (1989) Free Radical Biol. Med. , vol.7 , pp. 333-349
    • Witz, G.1
  • 33
    • 0031783956 scopus 로고    scopus 로고
    • Endogenous glutathione conjugates: occurrence and biological functions
    • Wang W., and Ballatori N. Endogenous glutathione conjugates: occurrence and biological functions. Pharm. Rev. 50 (1998) 335-355
    • (1998) Pharm. Rev. , vol.50 , pp. 335-355
    • Wang, W.1    Ballatori, N.2
  • 35
    • 0035626833 scopus 로고    scopus 로고
    • Microsomal glutathione-S-transferase A 1-1 with glutathione peroxidase activity from sheep liver: molecular cloning, expression and characterization
    • Prabhu K.S., Reddy P.V., Gumpricht E., Hildebrandt G.R., Scholz R.W., Sordillo L.M., and Reddy C.C. Microsomal glutathione-S-transferase A 1-1 with glutathione peroxidase activity from sheep liver: molecular cloning, expression and characterization. Biochem. J. 360 (2001) 345-354
    • (2001) Biochem. J. , vol.360 , pp. 345-354
    • Prabhu, K.S.1    Reddy, P.V.2    Gumpricht, E.3    Hildebrandt, G.R.4    Scholz, R.W.5    Sordillo, L.M.6    Reddy, C.C.7
  • 37
    • 0032540325 scopus 로고    scopus 로고
    • Oxidized LDL regulates macrophage gene expression through ligand activation of PPAR gamma
    • Nagy L., Tontonoz P., Alvarez J.G.A., Chen H., and Evans R.M. Oxidized LDL regulates macrophage gene expression through ligand activation of PPAR gamma. Cell 93 (1998) 229-240
    • (1998) Cell , vol.93 , pp. 229-240
    • Nagy, L.1    Tontonoz, P.2    Alvarez, J.G.A.3    Chen, H.4    Evans, R.M.5
  • 38
    • 0035851187 scopus 로고    scopus 로고
    • PPARγ: a Nuclear regulator of metabolism, differentiation, and cell growth
    • Rosen E.D., and Spiegelman B.M. PPARγ: a Nuclear regulator of metabolism, differentiation, and cell growth. J. Biol. Chem. 276 (2001) 37731-37734
    • (2001) J. Biol. Chem. , vol.276 , pp. 37731-37734
    • Rosen, E.D.1    Spiegelman, B.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.