메뉴 건너뛰기




Volumn 113, Issue 1-2, 2009, Pages 98-104

The role of porcine cytochrome b5A and cytochrome b5B in the regulation of cytochrome P45017A1 activities

Author keywords

17 Hydroxylase; Androstenone; C17,20 lyase; CYB5; CYP17A1

Indexed keywords

ANDIEN BETA SYNTHASE; ANDROST 16 ENE; ANDROSTANE DERIVATIVE; CYTOCHROME; CYTOCHROME B5; CYTOCHROME B5 REDUCTASE; CYTOCHROME B5A; CYTOCHROME B5B; CYTOCHROME P450 17A1; CYTOCHROME P450 REDUCTASE; GLUCOCORTICOID; PREGNENOLONE; SEX HORMONE; STEROID 17,20 LYASE; STEROID 17ALPHA MONOOXYGENASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 59849095112     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2008.11.012     Document Type: Article
Times cited : (25)

References (27)
  • 1
    • 0039440136 scopus 로고
    • Physiological aspects of androstenone and skatole formation in boar: a review with experimental data
    • Claus R., Weiler U., and Herzog A. Physiological aspects of androstenone and skatole formation in boar: a review with experimental data. Meat Sci. 38 (1994) 289-305
    • (1994) Meat Sci. , vol.38 , pp. 289-305
    • Claus, R.1    Weiler, U.2    Herzog, A.3
  • 2
    • 0015268597 scopus 로고
    • 16-Unsaturated C19 steroids: a review of their chemistry, biochemistry and possible physiological role
    • Gower D.B. 16-Unsaturated C19 steroids: a review of their chemistry, biochemistry and possible physiological role. J. Steroid Biochem. 3 (1972) 45-103
    • (1972) J. Steroid Biochem. , vol.3 , pp. 45-103
    • Gower, D.B.1
  • 3
    • 58149322606 scopus 로고    scopus 로고
    • Investigation of factors responsible for the development of boar taint
    • Babol J., Squires E.J., and Gullet E.A. Investigation of factors responsible for the development of boar taint. Food Res. Int. 28 (1996) 573-581
    • (1996) Food Res. Int. , vol.28 , pp. 573-581
    • Babol, J.1    Squires, E.J.2    Gullet, E.A.3
  • 4
    • 0015184926 scopus 로고
    • Determination of 5-androst-16-ene-3-one, a boar taint steroid in pigs, with reference to relationship to testosterone
    • Claus R., Hoffman B., and Karg H. Determination of 5-androst-16-ene-3-one, a boar taint steroid in pigs, with reference to relationship to testosterone. J. Anim. Sci. 33 (1971) 1293-1297
    • (1971) J. Anim. Sci. , vol.33 , pp. 1293-1297
    • Claus, R.1    Hoffman, B.2    Karg, H.3
  • 5
    • 0024366126 scopus 로고
    • Involvement of cytochrome P450 in the synthesis of 5,16, androstadien-3β-ol from pregnenolone in pig testis microsomes
    • Squires E.J. Involvement of cytochrome P450 in the synthesis of 5,16, androstadien-3β-ol from pregnenolone in pig testis microsomes. J. Steroid Biochem. 33 (1989) 621-626
    • (1989) J. Steroid Biochem. , vol.33 , pp. 621-626
    • Squires, E.J.1
  • 6
    • 0027490161 scopus 로고
    • Cytochrome P450c17 from porcine and bovine adrenal catalyses the formation of 5,16-androstadien-3β-ol from pregnenolone in the presence of cytochrome b5
    • Meadus W.J., Mason J.I., and Squires E.J. Cytochrome P450c17 from porcine and bovine adrenal catalyses the formation of 5,16-androstadien-3β-ol from pregnenolone in the presence of cytochrome b5. J. Steroid Biochem. Mol. Biol. 46 (1993) 565-572
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 565-572
    • Meadus, W.J.1    Mason, J.I.2    Squires, E.J.3
  • 7
    • 0022270532 scopus 로고
    • Cytochrome b5 promotes the synthesis Δ16-C19 steroids by homogenous cytochrome P-450 C21 side-chain clevage from pig testis
    • Nakajin S., Takahashi M., Shinoda M., and Hall P.F. Cytochrome b5 promotes the synthesis Δ16-C19 steroids by homogenous cytochrome P-450 C21 side-chain clevage from pig testis. Biochem. Biophys. Res. Commun. 132 (1985) 708-713
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , pp. 708-713
    • Nakajin, S.1    Takahashi, M.2    Shinoda, M.3    Hall, P.F.4
  • 8
    • 0037742310 scopus 로고    scopus 로고
    • Identification of outer mitochondrial membrane cytochrome b5 as a modulator for androgen synthesis in leydig cells
    • Ogishima T., Kinoshita J., Mitani F., Suematsu M., and Ito A. Identification of outer mitochondrial membrane cytochrome b5 as a modulator for androgen synthesis in leydig cells. J. Biol. Chem. 278 (2003) 21204-21211
    • (2003) J. Biol. Chem. , vol.278 , pp. 21204-21211
    • Ogishima, T.1    Kinoshita, J.2    Mitani, F.3    Suematsu, M.4    Ito, A.5
  • 9
    • 0017136501 scopus 로고
    • The role of microsomal cytochrome b5 in the metabolism of ethanol, drugs and the desaturation of fatty acids
    • Ozols J. The role of microsomal cytochrome b5 in the metabolism of ethanol, drugs and the desaturation of fatty acids. Ann. Clin. Res. 8 (1976) 182-192
    • (1976) Ann. Clin. Res. , vol.8 , pp. 182-192
    • Ozols, J.1
  • 10
    • 0018651542 scopus 로고
    • Properties of cytochrome b5 and methemoglobin reduction in human erythrocytes
    • Abe K., and Sugita Y. Properties of cytochrome b5 and methemoglobin reduction in human erythrocytes. Eur. J. Biochem. 101 (1979) 423-428
    • (1979) Eur. J. Biochem. , vol.101 , pp. 423-428
    • Abe, K.1    Sugita, Y.2
  • 12
    • 0018140102 scopus 로고
    • Reconstituted mammalian mixed-function oxidases: requirements, specificities and other properties
    • Lu A.Y.H., and West S.B. Reconstituted mammalian mixed-function oxidases: requirements, specificities and other properties. Pharmacol. Ther. Part A 2 (1978) 337-359
    • (1978) Pharmacol. Ther. Part A , vol.2 , pp. 337-359
    • Lu, A.Y.H.1    West, S.B.2
  • 13
    • 0017900548 scopus 로고
    • Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • Yoshida T., and Kikuchi G. Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J. Biol. Chem. 253 (1978) 4230-4236
    • (1978) J. Biol. Chem. , vol.253 , pp. 4230-4236
    • Yoshida, T.1    Kikuchi, G.2
  • 14
    • 0019877474 scopus 로고
    • Evidence for a new physiological role of hepatic NADPH: ferricytochrome (P-450) oxidoreductase
    • Ilan Z., Ilan R., and Cinit D.l. Evidence for a new physiological role of hepatic NADPH: ferricytochrome (P-450) oxidoreductase. J. Biol. Chem. 256 (1981) 10066-10072
    • (1981) J. Biol. Chem. , vol.256 , pp. 10066-10072
    • Ilan, Z.1    Ilan, R.2    Cinit, D.l.3
  • 15
    • 0024418975 scopus 로고
    • The organization and complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene
    • Tomatsu S., Kobayashi Y., Fukumaki Y., Yubishi T., Orii T., and Sakaki Y. The organization and complete nucleotide sequence of the human NADH-cytochrome b5 reductase gene. Gene 80 (1989) 353-361
    • (1989) Gene , vol.80 , pp. 353-361
    • Tomatsu, S.1    Kobayashi, Y.2    Fukumaki, Y.3    Yubishi, T.4    Orii, T.5    Sakaki, Y.6
  • 17
    • 0022413770 scopus 로고
    • Complete amino acid sequence of steer liver microsomal NADH-cytochrome b5 reductase
    • Ozols J., Korza G., Heinemann F.S., Hediger M.A., and Strittmatter P. Complete amino acid sequence of steer liver microsomal NADH-cytochrome b5 reductase. J. Biol. Chem. 260 (1985) 11953-11961
    • (1985) J. Biol. Chem. , vol.260 , pp. 11953-11961
    • Ozols, J.1    Korza, G.2    Heinemann, F.S.3    Hediger, M.A.4    Strittmatter, P.5
  • 18
    • 0001429526 scopus 로고    scopus 로고
    • Characteristics of a highly labile human type 5 17β-hydroxysteroid dehydrogenase
    • Dufort I., Rheault P., Huang X.F., Soucy P., and Luu-The V. Characteristics of a highly labile human type 5 17β-hydroxysteroid dehydrogenase. Endocrinology 140 (1999) 568-574
    • (1999) Endocrinology , vol.140 , pp. 568-574
    • Dufort, I.1    Rheault, P.2    Huang, X.F.3    Soucy, P.4    Luu-The, V.5
  • 19
    • 59849096740 scopus 로고    scopus 로고
    • Characteristics of human types 1, 2 and 3 17β-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition
    • Luu-The V., Zhang L., Poirier D., and Labrie F. Characteristics of human types 1, 2 and 3 17β-hydroxysteroid dehydrogenase activities: oxidation/reduction and inhibition. J. Steroid Biochem. Mol. Biol. 96 (2005) 217-228
    • (2005) J. Steroid Biochem. Mol. Biol. , vol.96 , pp. 217-228
    • Luu-The, V.1    Zhang, L.2    Poirier, D.3    Labrie, F.4
  • 20
    • 59849128572 scopus 로고
    • Synthesis of free and sulphoconjugated 16-androstene steroids by the Leydig cells of the mature domestic boar
    • Sinclair P.A., Squires E.J., Raeside J.I., and Renaud R. Synthesis of free and sulphoconjugated 16-androstene steroids by the Leydig cells of the mature domestic boar. J. Steroid Biochem. Mol. Biol. 55 (1995) 581-587
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.55 , pp. 581-587
    • Sinclair, P.A.1    Squires, E.J.2    Raeside, J.I.3    Renaud, R.4
  • 21
    • 21144473644 scopus 로고
    • Effects of exogenous porcine somatotropin on performance, testicular steroid production and fat levels of boar-taint-related compounds in young boars
    • Bonneau M., Meadus W.J., and Squires E.J. Effects of exogenous porcine somatotropin on performance, testicular steroid production and fat levels of boar-taint-related compounds in young boars. Can. J. Anim. Sci. 72 (1992) 537-545
    • (1992) Can. J. Anim. Sci. , vol.72 , pp. 537-545
    • Bonneau, M.1    Meadus, W.J.2    Squires, E.J.3
  • 22
    • 0029054788 scopus 로고
    • Modulation of the activity of human 17α-hydroxylase-17,20-lyase (CYP17) by cytochrome b5: endocrinological and mechanistic implications
    • Lee-Robichaud P., Wright J.N., Akhtar M.E., and Akhtar M. Modulation of the activity of human 17α-hydroxylase-17,20-lyase (CYP17) by cytochrome b5: endocrinological and mechanistic implications. Biochem. J. 308 (1995) 901-908
    • (1995) Biochem. J. , vol.308 , pp. 901-908
    • Lee-Robichaud, P.1    Wright, J.N.2    Akhtar, M.E.3    Akhtar, M.4
  • 23
    • 0019887951 scopus 로고
    • Microsomal cytochrome P-450 from neonatal pig testis
    • Nakajin S., and Hall P.F. Microsomal cytochrome P-450 from neonatal pig testis. J. Biol. Chem. 256 (1981) 3871-3876
    • (1981) J. Biol. Chem. , vol.256 , pp. 3871-3876
    • Nakajin, S.1    Hall, P.F.2
  • 24
    • 0036180356 scopus 로고    scopus 로고
    • Assessment of the ability of type 2 cytochrome b5 to modulate 17,20-lyase activity of human P450c17
    • Soucy P., and Luu-The V. Assessment of the ability of type 2 cytochrome b5 to modulate 17,20-lyase activity of human P450c17. J. Steroid Biochem. Mol. Biol. 80 (2002) 71-75
    • (2002) J. Steroid Biochem. Mol. Biol. , vol.80 , pp. 71-75
    • Soucy, P.1    Luu-The, V.2
  • 25
    • 0032488666 scopus 로고    scopus 로고
    • Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer
    • Auchus R.J., Lee T.C., and Miller W.L. Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J. Biol. Chem. 273 (1998) 3158-3165
    • (1998) J. Biol. Chem. , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 26
    • 0034039492 scopus 로고    scopus 로고
    • Conversion of pregnenolone to DHEA by human 17α-hydroxylase/17,20-lyase (P450c17)
    • Soucy P., and Luu-The V. Conversion of pregnenolone to DHEA by human 17α-hydroxylase/17,20-lyase (P450c17). Eur. J. Biochem. 267 (2000) 3243-3247
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3243-3247
    • Soucy, P.1    Luu-The, V.2
  • 27
    • 0031045446 scopus 로고    scopus 로고
    • Interaction of human CYP17 (P-45017α, 17α-hydroxylase-17,20-lyase) with cytochrome b5: importance of the orientation of the hydrophobic domain of cytochrome b5
    • Lee-Robichaud P., Kaderbhai M.A., Kaderbhai N., Wright J.N., and Akhtar M. Interaction of human CYP17 (P-45017α, 17α-hydroxylase-17,20-lyase) with cytochrome b5: importance of the orientation of the hydrophobic domain of cytochrome b5. Biochem. J. 321 (1997) 857-863
    • (1997) Biochem. J. , vol.321 , pp. 857-863
    • Lee-Robichaud, P.1    Kaderbhai, M.A.2    Kaderbhai, N.3    Wright, J.N.4    Akhtar, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.