메뉴 건너뛰기




Volumn 1770, Issue 1, 2007, Pages 130-136

Differences between bovine and human steroid double-bond isomerase activities of Alpha-class glutathione transferases selectively expressed in steroidogenic tissues

Author keywords

Alpha class glutathione transferases; Bovine GST A1 1; Steroid double bond isomerase; Steroidogenesis; Steroidogenic organ

Indexed keywords

3(OR 17)BETA HYDROXYSTEROID DEHYDROGENASE; ANDROSTENEDIOL; GLUTATHIONE TRANSFERASE; ISOMERASE; STEROID;

EID: 33845465202     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.06.015     Document Type: Article
Times cited : (16)

References (25)
  • 1
    • 10644266103 scopus 로고    scopus 로고
    • Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones
    • Payne A.H., and Hales D.B. Overview of steroidogenic enzymes in the pathway from cholesterol to active steroid hormones. Endocr. Rev. 25 (2004) 947-970
    • (2004) Endocr. Rev. , vol.25 , pp. 947-970
    • Payne, A.H.1    Hales, D.B.2
  • 2
    • 0035980083 scopus 로고    scopus 로고
    • Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones
    • Johansson A.-S., and Mannervik B. Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J. Biol. Chem. 276 (2001) 33061-33065
    • (2001) J. Biol. Chem. , vol.276 , pp. 33061-33065
    • Johansson, A.-S.1    Mannervik, B.2
  • 4
    • 0036016308 scopus 로고    scopus 로고
    • The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter
    • Morel F., Rauch C., Coles B., Le Ferrec E., and Guillouzo A. The human glutathione transferase alpha locus: genomic organization of the gene cluster and functional characterization of the genetic polymorphism in the hGSTA1 promoter. Pharmacogenetics 12 (2002) 277-286
    • (2002) Pharmacogenetics , vol.12 , pp. 277-286
    • Morel, F.1    Rauch, C.2    Coles, B.3    Le Ferrec, E.4    Guillouzo, A.5
  • 5
    • 0033017370 scopus 로고    scopus 로고
    • Distribution of glutathione S-transferases in the human ovary: an immunohistochemical study
    • Tiltman A.J., and Haffajee Z. Distribution of glutathione S-transferases in the human ovary: an immunohistochemical study. Gynecol. Obstet. Invest. 47 (1999) 247-250
    • (1999) Gynecol. Obstet. Invest. , vol.47 , pp. 247-250
    • Tiltman, A.J.1    Haffajee, Z.2
  • 6
    • 0037053335 scopus 로고    scopus 로고
    • Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3
    • Johansson A.-S., and Mannervik B. Active-site residues governing high steroid isomerase activity in human glutathione transferase A3-3. J. Biol. Chem. 277 (2002) 16648-16654
    • (2002) J. Biol. Chem. , vol.277 , pp. 16648-16654
    • Johansson, A.-S.1    Mannervik, B.2
  • 7
    • 0037119451 scopus 로고    scopus 로고
    • Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase
    • Pettersson P.L., Johansson A.-S., and Mannervik B. Transmutation of human glutathione transferase A2-2 with peroxidase activity into an efficient steroid isomerase. J. Biol. Chem. 277 (2002) 30019-30022
    • (2002) J. Biol. Chem. , vol.277 , pp. 30019-30022
    • Pettersson, P.L.1    Johansson, A.-S.2    Mannervik, B.3
  • 8
    • 0033305427 scopus 로고    scopus 로고
    • High expression of bovine alpha glutathione S-transferase (GSTA1, GSTA2) subunits is mainly associated with steroidogenically active cells and regulated by gonadotropins in bovine ovarian follicles
    • Rabahi F., Brule S., Sirois J., Beckers J.F., Silversides D.W., and Lussier J.G. High expression of bovine alpha glutathione S-transferase (GSTA1, GSTA2) subunits is mainly associated with steroidogenically active cells and regulated by gonadotropins in bovine ovarian follicles. Endocrinology 140 (1999) 3507-3517
    • (1999) Endocrinology , vol.140 , pp. 3507-3517
    • Rabahi, F.1    Brule, S.2    Sirois, J.3    Beckers, J.F.4    Silversides, D.W.5    Lussier, J.G.6
  • 9
    • 0742306207 scopus 로고    scopus 로고
    • Gene expression profiling of differentially expressed genes in granulosa cells of bovine dominant follicles using suppression subtractive hybridization
    • Fayad T., Levesque V., Sirois J., Silversides D.W., and Lussier J.G. Gene expression profiling of differentially expressed genes in granulosa cells of bovine dominant follicles using suppression subtractive hybridization. Biol. Reprod. 70 (2004) 523-533
    • (2004) Biol. Reprod. , vol.70 , pp. 523-533
    • Fayad, T.1    Levesque, V.2    Sirois, J.3    Silversides, D.W.4    Lussier, J.G.5
  • 10
    • 0001306237 scopus 로고
    • Glutathione transferases
    • Pacifici G.M., and Fracchia G.N. (Eds), European Commission, Luxembourg
    • Mannervik B., and Widersten M. Glutathione transferases. In: Pacifici G.M., and Fracchia G.N. (Eds). Advances in Drug Metabolism in Man (1995), European Commission, Luxembourg 407-459
    • (1995) Advances in Drug Metabolism in Man , pp. 407-459
    • Mannervik, B.1    Widersten, M.2
  • 11
    • 0028892567 scopus 로고
    • Isothiocyanates as substrates for human glutathione transferases: structure-activity studies
    • Kolm R.H., Danielson U.H., Zhang Y., Talalay P., and Mannervik B. Isothiocyanates as substrates for human glutathione transferases: structure-activity studies. Biochem. J. 311 (1995) 453-459
    • (1995) Biochem. J. , vol.311 , pp. 453-459
    • Kolm, R.H.1    Danielson, U.H.2    Zhang, Y.3    Talalay, P.4    Mannervik, B.5
  • 12
    • 0032519517 scopus 로고    scopus 로고
    • 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
    • Hubatsch I., Ridderström M., and Mannervik B. 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. Biochem. J. 330 (1998) 175-179
    • (1998) Biochem. J. , vol.330 , pp. 175-179
    • Hubatsch, I.1    Ridderström, M.2    Mannervik, B.3
  • 13
    • 0024427521 scopus 로고
    • Human placental 3 b-hydroxy-5-ene-steroid dehydrogenase and steroid 5 → 4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes
    • Thomas J.L., Myers R.P., and Strickler R.C. Human placental 3 b-hydroxy-5-ene-steroid dehydrogenase and steroid 5 → 4-ene-isomerase: purification from mitochondria and kinetic profiles, biophysical characterization of the purified mitochondrial and microsomal enzymes. J. Steroid Biochem. 33 (1989) 209-217
    • (1989) J. Steroid Biochem. , vol.33 , pp. 209-217
    • Thomas, J.L.1    Myers, R.P.2    Strickler, R.C.3
  • 14
    • 0033233309 scopus 로고    scopus 로고
    • Bovine adrenal 3b-hydroxysteroid dehydrogenase (E.C. 1.1.1. 145)/5-ene-4-ene isomerase (E.C. 5.3.3.1): characterization and its inhibition by isoflavones
    • Wong C.K., and Keung W.M. Bovine adrenal 3b-hydroxysteroid dehydrogenase (E.C. 1.1.1. 145)/5-ene-4-ene isomerase (E.C. 5.3.3.1): characterization and its inhibition by isoflavones. J. Steroid Biochem. Mol. Biol. 71 (1999) 191-202
    • (1999) J. Steroid Biochem. Mol. Biol. , vol.71 , pp. 191-202
    • Wong, C.K.1    Keung, W.M.2
  • 15
    • 10844293503 scopus 로고    scopus 로고
    • Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity
    • Gu Y., Guo J., Pal A., Pan S.-S., Zimniak P., Singh S.V., and Ji X. Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity. Biochemistry 43 (2004) 15673-15679
    • (2004) Biochemistry , vol.43 , pp. 15673-15679
    • Gu, Y.1    Guo, J.2    Pal, A.3    Pan, S.-S.4    Zimniak, P.5    Singh, S.V.6    Ji, X.7
  • 16
    • 0037040250 scopus 로고    scopus 로고
    • Membrane association of glutathione S-transferase mGSTA4-4, an enzyme that metabolizes lipid peroxidation products
    • Singh S.P., Janecki A.J., Srivastava S.K., Awasthi S., Awasthi Y.C., Xia S.J., and Zimniak P. Membrane association of glutathione S-transferase mGSTA4-4, an enzyme that metabolizes lipid peroxidation products. J. Biol. Chem. 277 (2002) 4232-4239
    • (2002) J. Biol. Chem. , vol.277 , pp. 4232-4239
    • Singh, S.P.1    Janecki, A.J.2    Srivastava, S.K.3    Awasthi, S.4    Awasthi, Y.C.5    Xia, S.J.6    Zimniak, P.7
  • 17
    • 1542298935 scopus 로고    scopus 로고
    • Characterization of a class alpha glutathione-S-transferase with glutathione peroxidase activity in human liver microsomes
    • Prabhu K.S., Reddy P.V., Jones E.C., Liken A.D., and Reddy C.C. Characterization of a class alpha glutathione-S-transferase with glutathione peroxidase activity in human liver microsomes. Arch. Biochem. Biophys. 424 (2004) 72-80
    • (2004) Arch. Biochem. Biophys. , vol.424 , pp. 72-80
    • Prabhu, K.S.1    Reddy, P.V.2    Jones, E.C.3    Liken, A.D.4    Reddy, C.C.5
  • 18
    • 0035374455 scopus 로고    scopus 로고
    • Role of glutathione S-transferases in protection against lipid peroxidation. Overexpression of hGSTA2-2 in K562 cells protects against hydrogen peroxide-induced apoptosis and inhibits JNK and caspase 3 activation
    • Yang Y., Cheng J.-Z., Singhal S.S., Saini M., Pandya U., Awasthi S., and Awasthi Y.C. Role of glutathione S-transferases in protection against lipid peroxidation. Overexpression of hGSTA2-2 in K562 cells protects against hydrogen peroxide-induced apoptosis and inhibits JNK and caspase 3 activation. J. Biol. Chem. 276 (2001) 19220-19230
    • (2001) J. Biol. Chem. , vol.276 , pp. 19220-19230
    • Yang, Y.1    Cheng, J.-Z.2    Singhal, S.S.3    Saini, M.4    Pandya, U.5    Awasthi, S.6    Awasthi, Y.C.7
  • 19
    • 0028923332 scopus 로고
    • Electron leakage from the adrenal cortex mitochondrial P450scc and P450c11 systems: NADPH and steroid dependence
    • Rapoport R., Sklan D., and Hanukoglu I. Electron leakage from the adrenal cortex mitochondrial P450scc and P450c11 systems: NADPH and steroid dependence. Arch. Biochem. Biophys. 317 (1995) 412-416
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 412-416
    • Rapoport, R.1    Sklan, D.2    Hanukoglu, I.3
  • 20
    • 0031665666 scopus 로고    scopus 로고
    • Glutathione S-transferases and prevention of cellular free radical damage
    • Ketterer B. Glutathione S-transferases and prevention of cellular free radical damage. Free Radical Res. 28 (1998) 647-658
    • (1998) Free Radical Res. , vol.28 , pp. 647-658
    • Ketterer, B.1
  • 21
    • 0036680017 scopus 로고    scopus 로고
    • Quinoids, quinoid radicals, and phenoxyl radicals formed from estrogens and antiestrogens
    • Bolton J.L. Quinoids, quinoid radicals, and phenoxyl radicals formed from estrogens and antiestrogens. Toxicology 177 (2002) 55-65
    • (2002) Toxicology , vol.177 , pp. 55-65
    • Bolton, J.L.1
  • 22
    • 27944453968 scopus 로고    scopus 로고
    • Glutathione transferases: new functions
    • Oakley A.J. Glutathione transferases: new functions. Curr. Opin. Struct. Biol. 15 (2005) 716-723
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 716-723
    • Oakley, A.J.1
  • 25
    • 1542304694 scopus 로고    scopus 로고
    • Functional role of the lock and key motif at the subunit interface of glutathione transferase P1-1
    • Hegazy U.M., Mannervik B., and Stenberg G. Functional role of the lock and key motif at the subunit interface of glutathione transferase P1-1. J. Biol. Chem. 279 (2004) 9586-9596
    • (2004) J. Biol. Chem. , vol.279 , pp. 9586-9596
    • Hegazy, U.M.1    Mannervik, B.2    Stenberg, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.