The stimulatory effect of prostaglandin E<sub>2</sub> on adenyl cyclase in the bovine corpus luteum

Marsh, John M.

doi:10.1016/0014-5793(70)80182-x

Cited by 69 publications

(30 citation statements)

References 14 publications

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“…Besides PGF2α, PGE2 and PGI2 are also synthesized by the bovine CL [2,3]. PGE2 and PGI2 have been identified as luteotropic PG in vivo [17,18] and in vitro [18][19][20]. From our results and the results of other, we assume that luteal PGF2α as well as other PGs may play a luteotropic role as a paracrine and/or autocrine factor in the early to mid-bovine CL.…”

Section: Discussionsupporting

confidence: 66%

Progesterone Stimulation by Prostaglandin F2.ALPHA. Involves the Protein Kinase C Pathway in Cultured Bovine Luteal Cells.

et al. 1998

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Abstract. The intracellular mechanism that mediates the stimulatory effect of prostaglandin F2α (PGF2α) on progesterone secretion by bovine luteal cells is not well understood. In the present study, we investigated to test the hypothesis that PGF2α stimulates progesterone secretion through activation of protein kinase C (PKC) by using a cell culture system. Bovine mid-luteal cells (Days 8-12 of the estrous cycle) were cultured for 24 h and then exposed to varying concentrations of PGF2α (10 -8 , 10 -7 , 10 -6 M) or luteinizing hormone (LH; 100 ng/ml) for 4, 6, or 16 h. Treatment of the cells with the highest dose of PGF2α (10 -6 M) or LH resulted in increases in progesterone secretion for all three exposure times. Following down-regulation of PKC with a tumor-promoting phorbol ester, phorbol 12-myristate 13-acetate (PMA; 10 -6 M), the stimulatory effect of PGF2α was no longer evident, whereas the response to LH was unaffected.These results support the hypothesis that the luteotropic action of PGF2α is mediated by the activation of intracellular PKC.

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Section: Discussionsupporting

confidence: 66%

Progesterone Stimulation by Prostaglandin F2.ALPHA. Involves the Protein Kinase C Pathway in Cultured Bovine Luteal Cells.

et al. 1998

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“…However, despite the enhanced responsiveness of human granulosa cells to these agents, basal cAMP levels remained unchanged throughout culture. This stimulation of progesterone secretion by hLH is thought to be due to an increase in cAMP generation rather than an inhibition of phosphodiesterase activity (Marsh 1970), and it is known that increases in cAMP enhance steroidogenesis by increasing specific mRNAs, which encode components of the steroidogenic pathway, such as 3 -HSD and Cytochrome P450 sidechain cleavage (Strauss et al 1988).…”

Section: Discussionmentioning

confidence: 99%

“…This is an event essential to the establishment and maintenance of pregnancy (Spencer & Bazer 2002). It is generally accepted that binding of LH to its G-protein-coupled receptor leads to the activation of the adenylate cyclase/cyclic-AMP (cAMP)/protein kinase A (PKA) signalling pathway (Marsh & Savard 1966, Marsh 1970, Leung & Steele 1992, Davis 1994. Thus, LH exerts its actions on progesterone synthesis primarily by elevating intracellular cAMP levels, leading to the activation of PKA, the activity of which has been shown to influence the expression (Strauss et al 1999, Clark et al 2001 or activity (Sugawara et al 1995) of components of the steroidogenic pathway.…”

Section: Introductionmentioning

confidence: 99%

Changes in cAMP-dependent protein kinase (PKA) and progesterone secretion in luteinizing human granulosa cells

Chin

Harris

Abayasekara³

2004

Journal of Endocrinology

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Luteinization of follicular granulosa cells leads to an increase in progesterone secretion that is regulated by luteinizing hormone (LH). LH acts mainly by elevating intracellular cyclic 3 ,5 -adenosine monophosphate (cAMP) and activating cAMP-dependent protein kinase (PKA). In this study, we have examined the role of PKA in relation to progesterone output by luteinizing human granulosa cells. Human granulosa cells were obtained by percoll gradient centrifugation of follicular aspirates of patients undergoing oocyte retrieval for assisted conception. Cells were cultured in serum-supplemented medium for up to 3 days in the presence and/or absence of human (h)LH and other cAMP-elevating agents. Spent medium was assayed for cAMP and progesterone content by specific RIA. Cell lysates were collected and assessed for PKA regulatory (R)II /catalytic (C) expression by Western blotting. Although basal progesterone secretion increased progressively throughout culture, cAMP levels remained unchanged. Under basal conditions, PKA RII /C expression appeared to increase throughout the 3-day culture period. In the presence of hLH and other cAMP-elevating agents, progesterone secretion increased in a dose-dependent manner coincident with an increase in cAMP. However, despite the increase in both progesterone secretion and cAMP accumulation, there was a dose-dependent decrease in both PKA RII and C expression. Thus, data presented in this study show that increases in progesterone secretion in luteinizing human granulosa cells can be dissociated from increases in PKA expression. This notion implies that progesterone secretion may be regulated by PKA-dependent as well as PKAindependent mechanisms.

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“…It is well established that binding of luteinizing hormone (LH) in the ovary to its G protein-coupled receptor leads to the generation of intracellular cyclic AMP (cAMP) and the activation of cAMP-dependent protein kinase (PKA) (Marsh & Savard 1966, Marsh 1970, Leung & Steele 1992. Although the activation of the cAMP/PKA signalling pathway is the major signalling pathway involved in the regulation of ovarian steroidogenesis, binding of LH to its receptor can also increase phosphatidyl inositol (PI) turnover and elevate intracellular calcium (Gilchrist et al 1996, Hirsch et al 1996, hence activating PKAindependent signalling pathways such as the phospholipase C/protein kinase C and the phospholipase A 2 /arachidonic acid signalling pathways (Guderman et al 1992, Cooke 1999.…”

Section: Introductionmentioning

confidence: 99%

Progesterone secretion by luteinizing human granulosa cells: a possible cAMP-dependent but PKA-independent mechanism involved in its regulation

Chin¹,

Abayasekara²

2004

Journal of Endocrinology

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The corpus luteum formed after luteinization of follicular cells secretes progesterone under the control of luteinizing hormone (LH). Binding of LH to its G-protein-coupled receptor leads to the activation of the adenylate cyclase/ cyclic AMP (cAMP)/cAMP-dependent protein kinase (PKA) signalling pathway. The identification of a new class of cAMP-binding proteins termed 'guanine nucleotide exchange factors' (cAMP-GEFs) provides a means by which changes in cAMP could yield actions that are independent of PKA. Hence, in this study, we have explored the hypothesis that steroidogenesis in luteinizing cells is mediated in both a cAMP/PKA-dependent and cAMP-dependent, but PKA-independent, manner. Human granulosa cells were isolated from follicular aspirates of women undergoing assisted conception. Luteinizing human granulosa cells were cultured for up to 3 days in the presence of human (h)LH and the adenylate cyclase activator forskolin in the added presence or absence of increasing doses of the PKA inhibitors H89 (N-[2-(4-bromocinnamylamino)ethyl] 5-isoquinoline) and PKI (myristoylated protein kinase A inhibitor amide 14-22) or the cAMP antagonist, Rp-cAMP. Agonist-stimulated progesterone secretion was inhibited in a dose-dependent manner by the PKA inhibitors and the cAMP antagonist, with decreasing sensitivity as luteinization progressed. Pretreatment of granulosa cells for 4 h with human (h)LHreduced the effectiveness of H89 in inhibiting progesterone secretion. Under basal conditions, cAMP-GEFI expression increased progressively throughout culture, and this could be further enhanced when cells were incubated with increasing doses of LH and forskolin. Furthermore, incubation of cells in the presence of increasing concentrations of the novel cAMP-GEF-specific cAMP analogue, 8 CPT-2 ME-cAMP (8-(4-chloro-phenylthio)-2 -0-methyladenosine-3 ,5 -cyclic monophosphate), increased progesterone secretion in a dose-dependent manner. The results show that increases in cAMP generated by LH and forskolin, in addition to activating PKA, also induce increases in cAMP-GEFI protein expression in luteinizing human granulosa cells. In addition, activation of cAMP-GEFI results in increased progesterone secretion. Hence, increases in cAMP lead to the activation of PKA-dependent, as well as PKA-independent but cAMPdependent (via cAMP-GEFI), signalling mechanisms. Since cAMP-GEFs have the capacity to activate the mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3-kinase (PI3-K)/protein kinase B (PKB) signalling pathways, these may provide the potential mechanisms by which cAMP-dependent but PKAindependent progesterone synthesis is regulated.

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The stimulatory effect of prostaglandin E₂ on adenyl cyclase in the bovine corpus luteum

Cited by 69 publications

References 14 publications

Progesterone Stimulation by Prostaglandin F2.ALPHA. Involves the Protein Kinase C Pathway in Cultured Bovine Luteal Cells.

Progesterone Stimulation by Prostaglandin F2.ALPHA. Involves the Protein Kinase C Pathway in Cultured Bovine Luteal Cells.

Changes in cAMP-dependent protein kinase (PKA) and progesterone secretion in luteinizing human granulosa cells

Progesterone secretion by luteinizing human granulosa cells: a possible cAMP-dependent but PKA-independent mechanism involved in its regulation

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The stimulatory effect of prostaglandin E2 on adenyl cyclase in the bovine corpus luteum

Cited by 69 publications

References 14 publications

Progesterone Stimulation by Prostaglandin F2.ALPHA. Involves the Protein Kinase C Pathway in Cultured Bovine Luteal Cells.

Progesterone Stimulation by Prostaglandin F2.ALPHA. Involves the Protein Kinase C Pathway in Cultured Bovine Luteal Cells.

Changes in cAMP-dependent protein kinase (PKA) and progesterone secretion in luteinizing human granulosa cells

Progesterone secretion by luteinizing human granulosa cells: a possible cAMP-dependent but PKA-independent mechanism involved in its regulation

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The stimulatory effect of prostaglandin E₂ on adenyl cyclase in the bovine corpus luteum