[Identification of molecular species in porcine luteal glutathione S-transferase and its hormonal regulation by hypophyseal gonadotropins].
The glutathione S-transferase (GST) was purified to homogenous state from cytosol fraction of porcine corpora lutea. Present studies showed that the final enzyme preparation was consisted of a single molecular species of GST 1-1 (ligandin), which has been identified from its enzymatic properties, amino acid sequences and immunological reactivity. Furthermore, it has been suggested that the ovarian GST involves in the steroidogenesis, especially in the step of progesterone synthesis, from the following results. 1) The final enzyme preparation has a significant delta 5-3-ketosteroid isomerase activity. 2) GST activity in the cultured porcine granulosa cells was remarkably increased in the luteinizing process, which was induced by an addition of hypophyseal gonadotropins such as FSH and LH to the culture system. 3) Changes of GST activity induced by FSH and LH were closely associated with progesterone production. 4) The GST localized in the luteal cells and theca interna, but not in the granulosa cells, which has been revealed by an immunohistochemical staining using anti-luteal GST antibodies.
Keira
M
M
Department of Obstetrics and Gynecology, Hokkaido University School of Medicine, Sapporo, Japan.
D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D003338:Corpus Luteum / Q000201:enzymology*; D005260:Female; D005640:Follicle Stimulating Hormone / Q000494:pharmacology / Q000502:physiology*; D005982:Glutathione Transferase / Q000302:isolation & purification* / Q000378:metabolism* / Q000502:physiology; D006107:Granulosa Cells / Q000378:metabolism; D007986:Luteinizing Hormone / Q000494:pharmacology / Q000502:physiology*; D008969:Molecular Sequence Data; D011374:Progesterone / Q000096:biosynthesis; D013552:Swine
D011374:Progesterone; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone; D005982:Glutathione Transferase