Sex difference of cytochrome P-450 in the rat: Purification, characterization, and quantitation of constitutive forms of cytochrome P-450 from liver microsomes of male and female rats

Kamataki, Tetsuya; Maeda, Kaori; Yamazoe, Yasushi; Nagai, Tsuneji; Kato, Ryuichi

doi:10.1016/0003-9861(83)90087-5

Cited by 229 publications

(59 citation statements)

References 28 publications

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“…We proved immunochemically that P-450-male and P 450-female exist specifically in liver micro somes from male and female rats, respectively, and their contents are about one-third of the total cytochrome P-450 (9,10). P-450-male shows distinctly higher activities in the oxidation of various drugs and testosterone in comparison with those of P-450-female (9,(11)(12)(13). Moreover, Waxman (14) purified male specific cytochrome P-450, P-450 2c, which is responsible for the 16a-hydroxylation of testosterone in rat liver microsomes; and Ryan et al (15) and MacGeoch et al (16) purified female specific cytochrome P-450, designated as P-450i and P-450 5p, respectively, which are responsible for 15 (3-hydroxylation of 5a androstane-3a,1713-diol-3,17-disulfate in rat liver microsomes.…”

mentioning

confidence: 74%

“…The characteristics of P-450-male, P-450 female and monospecific antibodies to these cytochromes were described previously (9,22).…”

Section: Animalsmentioning

confidence: 99%

“…With the advances in the purification of cytochrome P-450, the presence of multiple forms of cytochrome P 450 has been demonstrated (4-6). We purified male-specific cytochrome P 450 from male rat liver and female-specific cytochrome P-450 from female rat liver and have designated them as P-450-male and P-450-female, respectively (7)(8)(9). We proved immunochemically that P-450-male and P 450-female exist specifically in liver micro somes from male and female rats, respectively, and their contents are about one-third of the total cytochrome P-450 (9,10).…”

mentioning

confidence: 99%

“…We purified male-specific cytochrome P 450 from male rat liver and female-specific cytochrome P-450 from female rat liver and have designated them as P-450-male and P-450-female, respectively (7)(8)(9). We proved immunochemically that P-450-male and P 450-female exist specifically in liver micro somes from male and female rats, respectively, and their contents are about one-third of the total cytochrome P-450 (9,10). P-450-male shows distinctly higher activities in the oxidation of various drugs and testosterone in comparison with those of P-450-female (9,(11)(12)(13).…”

mentioning

confidence: 99%

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Effects of Hypophysectomy and Growth Hormone Treatment on Sex-Specific Forms of Cytochrome P-450 in Relation to Drug and Steroid Metabolisms in Rat Liver Microsomes

Yamazoe

Shimada

Kamataki

et al. 1986

Japanese Journal of Pharmacology

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Abstract-Hypophysectomy decreased the content of a male specific cytochrome P-450, P-450-male, in male rats, while it expressed P-450-male and completely depressed a female specific cytochrome P-450, P-450-female, in female rats. Intermittent injections of human growth hormone (GH), which mimic the secretion in males, restored P-450-male in hypophysectomized (Hypox) male rats and partially restored P-450-female in Hypox female rats. Continuous infusion of GH, which mimics the female secretion pattern, into Hypox male rats caused a further decrease in P-450-male content, and it caused the expression of P-450-female. In Hypox female rats, the same treatment depressed P-450-male and expressed P-450-female to the level of an intact female. These results indicate that the diurnal changes in the pattern of serum growth hormone level regulate the expression of P-450-male and P-450-female. The activities of testosterone 2a and 16a hydroxylases were closely correlated to P-450-male content with the correlation coefficients (r) of 0.955 and 0.929, respectively. Benzo(a)pyrene hydroxylation was also correlated to P-450-male content (r=0.850).Aminopyrine N-deme thylation and propoxycoumarin 0-depropylation were correlated to less extents (r=0.692 and r=0.720), while aniline hydroxylation and 0-ethylresorufin 0 deethylation were not correlated to P-450-male content. These results indicate that testosterone 2a and 16a-hydroxylations are closely dependent, but the metabolism of a variety of drugs are dependent to different extents on P-450-male in rat liver microsomes.

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mentioning

confidence: 74%

“…The characteristics of P-450-male, P-450 female and monospecific antibodies to these cytochromes were described previously (9,22).…”

Section: Animalsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Effects of Hypophysectomy and Growth Hormone Treatment on Sex-Specific Forms of Cytochrome P-450 in Relation to Drug and Steroid Metabolisms in Rat Liver Microsomes

Yamazoe

Shimada

Kamataki

et al. 1986

Japanese Journal of Pharmacology

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“…The N-terminal sequence of PB25 was identical with that described by Hanniu et al [26] as 'form h' and by Waxman [27] as 'form 2c', by Cheng & Schenkman as 'RLM.' [28] and by Kamataki et al [29] as 'P450 male'. Form 2d appears to be a protein different from, but structurally related to, PB2a.…”

Section: Discussionmentioning

confidence: 96%

Multiple forms of cytochrome P-450 related to forms induced marginally by phenobarbital. Differences in structure and in the metabolism of alkoxyresorufins

Wolf¹,

Seilman²,

Oesch³

et al. 1986

Biochemical Journal

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The properties of five structurally related forms of cytochrome P-450 (PB1a, PB1b, PB2a, PB2b and PB2d) isolated from rats treated with phenobarbital have been compared with two forms isolated previously now termed ‘PB1c’ and ‘PB2c’ These enzymes were characterized by their marginal inducibility by phenobarbital and are clearly distinguishable from the major phenobarbital-inducible proteins. PB1a and PB1b differed in Mr (52,700 and 52,900), absorption spectra and papain-proteolysis fragments. However, they had identical N-terminal sequences. PB2a, PB2b and PB2d had apparent Mr values of 52,900, 52,900 and 50,800. PB2a and PB2b had different N-terminal sequences and, after digestion with papain, gave different papain-proteolysis fragments. The N-terminal sequence of PB2b was similar to, but not identical with, that of pregnenolone-16 alpha-carbonitrile-inducible P-450 species, and PB2b was the protein most closely related to PB2c. The extent of immunocross-reactivity among the forms was stronger within, than between, the PB1 and PB2 groups. Even structurally similar forms were functionally diverse, exhibiting large differences in metabolic specificity in the dealkylation of a series of alkoxyresorufins.

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P ‐450 Cytochromes: Structure and Function

Black

Coon

1987

Advances in Enzymology - And Related Areas of Molecular Biology

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Sex difference of cytochrome P-450 in the rat: Purification, characterization, and quantitation of constitutive forms of cytochrome P-450 from liver microsomes of male and female rats

Cited by 229 publications

References 28 publications

Effects of Hypophysectomy and Growth Hormone Treatment on Sex-Specific Forms of Cytochrome P-450 in Relation to Drug and Steroid Metabolisms in Rat Liver Microsomes

Effects of Hypophysectomy and Growth Hormone Treatment on Sex-Specific Forms of Cytochrome P-450 in Relation to Drug and Steroid Metabolisms in Rat Liver Microsomes

Multiple forms of cytochrome P-450 related to forms induced marginally by phenobarbital. Differences in structure and in the metabolism of alkoxyresorufins

P ‐450 Cytochromes: Structure and Function

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