Localization of prostaglandin F(2α) inhibition of lipoprotein use by bovine luteal cells

D. P. Grusenmeyer, Joy Lee Pate

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Prostaglandin F(2α) (PGF(2α)) inhibits lipoprotein-stimulated progesterone production by bovine luteal cells in vitro and the objective of this study was to localized the site of action of PGF(2α). Cultured bovine luteal cells were treated with PGF(2α) for seven days, and then with either lipoproteins or 25-hydroxycholesterol in the presence of aminoglutethimide (which inhibits cholesterol side-chain cleavage) for the final 48 h. The effects of PGF(2α) on progesterone production, cellular cholesterol content, mitochondrial cholesterol content and cholesterol side-chain cleavage activity were determined. As expected, PGF(2α) inhibited (p < 0.05) lipoprotein-stimulated progesterone production. However, PGF(2α) did not inhibit low-density lipoprotein-stimulated, of high density lipoprotein-stimulated, increases in cellular cholesterol (p < 0.05) or inhibit lipoprotein-induced increases in mitochondrial cholesterol content (P < 0.05). Additionally, cholesterol content of mitochondria increased (p < 0.05) in the presence of PGF(2α) alone. To determine if the PGF(2α)-induced inhibition of steroidogenesis occurred at, or after, the side-chain cleavage reaction, we treated cells with the readily diffusable sterol, 25-hydroxycholesterol. Prostaglandin F(2α) did not inhibit 25-hydroxycholesterol-stimulated progesterone production (P < 0.05). Prostaglandin F(2α) may therefore exert its luteolytic effect at a site after cholesterol transport to the mitochondria but before cholesterol side-chain cleavage.

Original languageEnglish (US)
Pages (from-to)311-318
Number of pages8
JournalJournal of reproduction and fertility
Volume94
Issue number2
StatePublished - Jan 1 1992

Fingerprint

Luteal Cells
Prostaglandins F
Lipoproteins
Cholesterol
Progesterone
Mitochondria
Luteolytic Agents
Aminoglutethimide
Sterols
HDL Lipoproteins
LDL Lipoproteins

All Science Journal Classification (ASJC) codes

  • Physiology
  • Embryology
  • Molecular Biology
  • Obstetrics and Gynecology
  • Developmental Biology

Cite this

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title = "Localization of prostaglandin F(2α) inhibition of lipoprotein use by bovine luteal cells",
abstract = "Prostaglandin F(2α) (PGF(2α)) inhibits lipoprotein-stimulated progesterone production by bovine luteal cells in vitro and the objective of this study was to localized the site of action of PGF(2α). Cultured bovine luteal cells were treated with PGF(2α) for seven days, and then with either lipoproteins or 25-hydroxycholesterol in the presence of aminoglutethimide (which inhibits cholesterol side-chain cleavage) for the final 48 h. The effects of PGF(2α) on progesterone production, cellular cholesterol content, mitochondrial cholesterol content and cholesterol side-chain cleavage activity were determined. As expected, PGF(2α) inhibited (p < 0.05) lipoprotein-stimulated progesterone production. However, PGF(2α) did not inhibit low-density lipoprotein-stimulated, of high density lipoprotein-stimulated, increases in cellular cholesterol (p < 0.05) or inhibit lipoprotein-induced increases in mitochondrial cholesterol content (P < 0.05). Additionally, cholesterol content of mitochondria increased (p < 0.05) in the presence of PGF(2α) alone. To determine if the PGF(2α)-induced inhibition of steroidogenesis occurred at, or after, the side-chain cleavage reaction, we treated cells with the readily diffusable sterol, 25-hydroxycholesterol. Prostaglandin F(2α) did not inhibit 25-hydroxycholesterol-stimulated progesterone production (P < 0.05). Prostaglandin F(2α) may therefore exert its luteolytic effect at a site after cholesterol transport to the mitochondria but before cholesterol side-chain cleavage.",
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Localization of prostaglandin F(2α) inhibition of lipoprotein use by bovine luteal cells. / Grusenmeyer, D. P.; Pate, Joy Lee.

In: Journal of reproduction and fertility, Vol. 94, No. 2, 01.01.1992, p. 311-318.

Research output: Contribution to journalArticle

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