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Distribution of glutathione S-transferase isoenzymes in human ovary

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Distribution of glutathione S-transferase isoenzymes in human ovary. / Rahilly, M; Carder, P J; Al-Nafussi, Awatif; Harrison, D J.

In: Journal of Reproduction and Fertility, Vol. 93, No. 2, 11.1991, p. 303-311.

Research output: Contribution to journalArticlepeer-review

Harvard

Rahilly, M, Carder, PJ, Al-Nafussi, A & Harrison, DJ 1991, 'Distribution of glutathione S-transferase isoenzymes in human ovary', Journal of Reproduction and Fertility, vol. 93, no. 2, pp. 303-311.

APA

Rahilly, M., Carder, P. J., Al-Nafussi, A., & Harrison, D. J. (1991). Distribution of glutathione S-transferase isoenzymes in human ovary. Journal of Reproduction and Fertility, 93(2), 303-311.

Vancouver

Rahilly M, Carder PJ, Al-Nafussi A, Harrison DJ. Distribution of glutathione S-transferase isoenzymes in human ovary. Journal of Reproduction and Fertility. 1991 Nov;93(2):303-311.

Author

Rahilly, M ; Carder, P J ; Al-Nafussi, Awatif ; Harrison, D J. / Distribution of glutathione S-transferase isoenzymes in human ovary. In: Journal of Reproduction and Fertility. 1991 ; Vol. 93, No. 2. pp. 303-311.

Bibtex - Download

@article{517bf9263e3243298dd7e5aa3a2cd69b,
title = "Distribution of glutathione S-transferase isoenzymes in human ovary",
abstract = "Glutathione S-transferases (GST) are drug-metabolizing and detoxification enzymes involved in the intracellular transport and metabolism of steroid hormones. We studied expression of pi, alpha, mu and microsomal GST by immunohistochemistry in normal human ovaries at different stages of the menstrual cycle and pregnancy and after the menopause. Antibodies were raised in rabbits to purified GST subunits and formalin-fixed, paraffin-embedded sections were studied using the peroxidase-antiperoxidase method. Staining density was graded from very strong to negative. All four isoenzymes were identified in the ovary and their distribution was heterogeneous. The staining pattern of follicles varied with the stage of the menstrual cycle for each isoenzyme. All the ovaries contained abundant GST pi in stroma. GST alpha is closely associated with the glutathione-dependent enzyme delta-5,3-ketosteroid isomerase, which catalyses the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. GST alpha was localized to the steroid-producing cells and thus may be useful in studying ovaries in conditions where there are assumed alterations in steroid production.",
keywords = "Corpus Luteum, Cytoplasm, Female, Glutathione transferase, Gonadal Steroid Hormones, Humans, Immunoenzyme techniques, Isoenzymes, Menstruation, Microsomes, Ovarian follicle, Ovary, Pregnancy",
author = "M Rahilly and Carder, {P J} and Awatif Al-Nafussi and Harrison, {D J}",
note = "M1 - Article",
year = "1991",
month = nov,
language = "English",
volume = "93",
pages = "303--311",
journal = "Journal of Reproduction and Fertility",
issn = "0022-4251",
publisher = "Society for Reproduction and Fertility",
number = "2",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Distribution of glutathione S-transferase isoenzymes in human ovary

AU - Rahilly, M

AU - Carder, P J

AU - Al-Nafussi, Awatif

AU - Harrison, D J

N1 - M1 - Article

PY - 1991/11

Y1 - 1991/11

N2 - Glutathione S-transferases (GST) are drug-metabolizing and detoxification enzymes involved in the intracellular transport and metabolism of steroid hormones. We studied expression of pi, alpha, mu and microsomal GST by immunohistochemistry in normal human ovaries at different stages of the menstrual cycle and pregnancy and after the menopause. Antibodies were raised in rabbits to purified GST subunits and formalin-fixed, paraffin-embedded sections were studied using the peroxidase-antiperoxidase method. Staining density was graded from very strong to negative. All four isoenzymes were identified in the ovary and their distribution was heterogeneous. The staining pattern of follicles varied with the stage of the menstrual cycle for each isoenzyme. All the ovaries contained abundant GST pi in stroma. GST alpha is closely associated with the glutathione-dependent enzyme delta-5,3-ketosteroid isomerase, which catalyses the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. GST alpha was localized to the steroid-producing cells and thus may be useful in studying ovaries in conditions where there are assumed alterations in steroid production.

AB - Glutathione S-transferases (GST) are drug-metabolizing and detoxification enzymes involved in the intracellular transport and metabolism of steroid hormones. We studied expression of pi, alpha, mu and microsomal GST by immunohistochemistry in normal human ovaries at different stages of the menstrual cycle and pregnancy and after the menopause. Antibodies were raised in rabbits to purified GST subunits and formalin-fixed, paraffin-embedded sections were studied using the peroxidase-antiperoxidase method. Staining density was graded from very strong to negative. All four isoenzymes were identified in the ovary and their distribution was heterogeneous. The staining pattern of follicles varied with the stage of the menstrual cycle for each isoenzyme. All the ovaries contained abundant GST pi in stroma. GST alpha is closely associated with the glutathione-dependent enzyme delta-5,3-ketosteroid isomerase, which catalyses the conversion of pregnenolone to progesterone and dehydroepiandrosterone to androstenedione. GST alpha was localized to the steroid-producing cells and thus may be useful in studying ovaries in conditions where there are assumed alterations in steroid production.

KW - Corpus Luteum

KW - Cytoplasm

KW - Female

KW - Glutathione transferase

KW - Gonadal Steroid Hormones

KW - Humans

KW - Immunoenzyme techniques

KW - Isoenzymes

KW - Menstruation

KW - Microsomes

KW - Ovarian follicle

KW - Ovary

KW - Pregnancy

M3 - Article

VL - 93

SP - 303

EP - 311

JO - Journal of Reproduction and Fertility

JF - Journal of Reproduction and Fertility

SN - 0022-4251

IS - 2

ER -

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