Steroid Synthesis-Dependent, Oxygen-Mediated Damage of Mitochondrial and Microsomal Cytochrome P-450 Enzymes in Rat Leydig Cell Cultures*

Endocrinology ◽

10.1210/endo-121-4-1390 ◽

1987 ◽

Vol 121 (4) ◽

pp. 1390-1399 ◽

Author(s):

MARKOS GEORGIOU ◽

LOUISE M. PERKINS ◽

ANITA H. PAYNE

Keyword(s):

Cell Cultures ◽

Leydig Cell ◽

Steroid Synthesis ◽

Microsomal Cytochrome ◽

Cytochrome P 450

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Steroid product-induced, oxygen-mediated damage of microsomal cytochrome P-450 enzymes in Leydig cell cultures. Relationship to desensitization.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)89521-7 ◽

1985 ◽

Vol 260 (4) ◽

pp. 2092-2099

Author(s):

P G Quinn ◽

A H Payne

Keyword(s):

Cell Cultures ◽

Leydig Cell ◽

Microsomal Cytochrome ◽

Cytochrome P 450

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Noncoordinate Regulation ofde NovoSynthesis of Cytochrome P-450 Cholesterol Side-Chain Cleavage and Cytochrome P-450 17α-Hydroxylase/C17-20Lyase in Mouse Leydig Cell Cultures: Relation to Steroid Production

Molecular Endocrinology ◽

10.1210/mend-1-9-595 ◽

1987 ◽

Vol 1 (9) ◽

pp. 595-603 ◽

Author(s):

Onyeama O. Anakwe ◽

Anita H. Payne

Keyword(s):

Cell Cultures ◽

Leydig Cell ◽

Steroid Production ◽

Side Chain Cleavage ◽

Chain Cleavage ◽

Cytochrome P 450 ◽

Mouse Leydig Cell

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Testosterone inhibits cAMP-induced de Novo synthesis of Leydig cell cytochrome P-450(17 alpha) by an androgen receptor-mediated mechanism.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)60944-5 ◽

1987 ◽

Vol 262 (23) ◽

pp. 11200-11206

Author(s):

D B Hales ◽

L L Sha ◽

A H Payne

Keyword(s):

Androgen Receptor ◽

Leydig Cell ◽

De Novo ◽

De Novo Synthesis ◽

Cytochrome P 450

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Hydroxylation of prostaglandins by inducible isozymes of rabbit liver microsomal cytochrome P-450. Participation of cytochrome b5.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)33745-1 ◽

1982 ◽

Vol 257 (19) ◽

pp. 11221-11229 ◽

Author(s):

K P Vatsis ◽

A D Theoharides ◽

D Kupfer ◽

M J Coon

Keyword(s):

Cytochrome B5 ◽

Rabbit Liver ◽

Microsomal Cytochrome ◽

Cytochrome P 450

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The complete amino acid sequence of rabbit phenobarbital-induced liver microsomal cytochrome P-450.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)32605-x ◽

1983 ◽

Vol 258 (7) ◽

pp. 4195-4201 ◽

Author(s):

F S Heinemann ◽

J Ozols

Keyword(s):

Amino Acid Sequence ◽

Microsomal Cytochrome ◽

Complete Amino Acid Sequence ◽

Cytochrome P 450

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Correlation of type I, type II, and reverse type I difference spectra with absolute changes in spin state of hepatic microsomal cytochrome P-450 iron from five mammalian species

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)38109-7 ◽

1978 ◽

Vol 253 (4) ◽

pp. 1048-1058

Author(s):

K. Kumaki ◽

M. Sato ◽

H. Kon ◽

D.W. Nebert

Keyword(s):

Mammalian Species ◽

Type I ◽

Type Ii ◽

Difference Spectra ◽

Microsomal Cytochrome ◽

Cytochrome P 450

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Kinetics of the hydroperoxide-dependent dealkylation reactions catalyzed by rabbit liver microsomal cytochrome P-450.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)43447-3 ◽

1980 ◽

Vol 255 (20) ◽

pp. 9685-9692

Author(s):

D.R. Koop ◽

P.F. Hollenberg

Keyword(s):

Rabbit Liver ◽

Microsomal Cytochrome ◽

Kinetics Of ◽

Cytochrome P 450

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Microsomal cytochrome P-450 from neonatal pig testis. Purification and properties of A C21 steroid side-chain cleavage system (17 alpha-hydroxylase-C17,20 lyase).

Journal of Biological Chemistry ◽

10.1016/s0021-9258(19)69538-4 ◽

1981 ◽

Vol 256 (8) ◽

pp. 3871-3876

Author(s):

S. Nakajin ◽

P.F. Hall

Keyword(s):

Microsomal Cytochrome ◽

Side Chain Cleavage ◽

Chain Cleavage ◽

Purification And Properties ◽

Neonatal Pig ◽

Cytochrome P 450

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Separation and purification of multiple forms of microsomal cytochrome P-450. Activities of different forms of cytochrome P-450 towards several compounds of environmental interest.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)40345-0 ◽

1977 ◽

Vol 252 (11) ◽

pp. 3970-3979 ◽

Author(s):

F P Guengerich

Keyword(s):

Separation And Purification ◽

Multiple Forms ◽

Microsomal Cytochrome ◽

Cytochrome P 450

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Oxygen-mediated damage of microsomal cytochrome P-450 enzymes in cultured leydig cells. Role in steroidogenic desensitization.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)43019-5 ◽

1984 ◽

Vol 259 (7) ◽

pp. 4130-4135 ◽

Author(s):

P G Quinn ◽

A H Payne

Keyword(s):

Leydig Cells ◽

Microsomal Cytochrome ◽

Cytochrome P 450

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