Inhibition of the adenylyl cyclase and activation of the phosphatidylinositol pathway in oocytes through expression of serotonin receptors does not induce oocyte maturation

Noh, Seung-Jae; Han, Jin‐Kwan

doi:10.1002/(sici)1097-010x(19980101)280:1<45::aid-jez6>3.0.co;2-h

Cited by 21 publications

(14 citation statements)

References 48 publications

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“…Whereas some studies detect a 10-60% drop in cAMP levels from 15 s up to 6 h after P4 addition (Bravo et al, 1978;Cicirelli and Smith, 1985;Gelerstein et al, 1988;Maller et al, 1979;Mulner et al, 1979;Nader et al, 2014;Sadler and Maller, 1981;SchorderetSlatkine et al, 1982), others failed to detect any changes in cAMP levels in response to P4 (Noh and Han, 1998;O'Connor and Smith, 1976;Schutter et al, 1975;Thibier et al, 1982). Furthermore, some studies found that a decrease in cAMP levels was not sufficient to induce spontaneous maturation, and that an increase in cAMP accelerates maturation (Gelerstein et al, 1988;Noh and Han, 1998).…”

Section: Introductionsupporting

confidence: 86%

“…Furthermore, some studies found that a decrease in cAMP levels was not sufficient to induce spontaneous maturation, and that an increase in cAMP accelerates maturation (Gelerstein et al, 1988;Noh and Han, 1998). Consistently, exposing oocytes to P4 for <30 min induced a decrease in cAMP but did not induce oocyte maturation, which required ≥30 min incubation with P4 (Nader et al, 2014).…”

Section: Introductionsupporting

confidence: 77%

“…However, PKI significantly (P=0.0044) enhanced the rate of P4-induced oocyte maturation (Fig. 5C,D), as previously reported (Noh and Han, 1998). The poor activation of oocyte maturation by PKI (Fig.…”

Section: Pka Anchoring To Akap Is Not Essential For Releasing Meioticmentioning

confidence: 99%

“…Consistently, injection of PDE, the PKA regulatory subunit (PKAr), or the PKA pseudo-substrate inhibitor (PKI) all release meiotic arrest (Andersen et al, 1998;Daar et al, 1993;Eyers et al, 2005). However, others found that inhibition of PKA activity using H-89 or PKI injection failed to stimulate oocyte maturation (Noh and Han, 1998). Furthermore, induction of a drop in cAMP levels through stimulation of exogenously expressed Gi-coupled serotonin receptor did not stimulate oocyte maturation (Noh and Han, 1998).…”

Section: Introductionmentioning

confidence: 99%

“…However, others found that inhibition of PKA activity using H-89 or PKI injection failed to stimulate oocyte maturation (Noh and Han, 1998). Furthermore, induction of a drop in cAMP levels through stimulation of exogenously expressed Gi-coupled serotonin receptor did not stimulate oocyte maturation (Noh and Han, 1998).…”

Section: Introductionmentioning

confidence: 99%

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Xenopus oocyte prophase I meiotic arrest is released independently from a decrease in cAMP levels or PKA activity

et al. 2016

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Vertebrate oocytes arrest at prophase of meiosis I as a result of high levels of cyclic adenosine monophosphate (cAMP) and protein kinase A (PKA) activity. In Xenopus, progesterone is believed to release meiotic arrest by inhibiting adenylate cyclase, lowering cAMP levels and repressing PKA. However, the exact timing and extent of the cAMP decrease is unclear, with conflicting reports in the literature. Using various in vivo reporters for cAMP and PKA at the single-cell level in real time, we fail to detect any significant changes in cAMP or PKA in response to progesterone. More interestingly, there was no correlation between the levels of PKA inhibition and the release of meiotic arrest. Furthermore, we devised conditions whereby meiotic arrest could be released in the presence of sustained high levels of cAMP. Consistently, lowering endogenous cAMP levels by >65% for prolonged time periods failed to induce spontaneous maturation. These results argue that the release of oocyte meiotic arrest in Xenopus is independent of a reduction in either cAMP levels or PKA activity, but rather proceeds through a parallel cAMP/PKAindependent pathway.

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Section: Introductionsupporting

confidence: 86%

Section: Introductionsupporting

confidence: 77%

Section: Pka Anchoring To Akap Is Not Essential For Releasing Meioticmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Xenopus oocyte prophase I meiotic arrest is released independently from a decrease in cAMP levels or PKA activity

et al. 2016

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Different signaling pathway between sphingosine-1-phosphate and lysophosphatidic acid inXenopus oocytes: Functional coupling of the sphingosine-1-phosphate receptor to PLC-xβ inXenopus oocytes

et al. 1998

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In Xenopus oocytes, both sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA) activate Ca2+-dependent oscillatory Cl- currents by acting through membrane-bound receptors. External application of 50 microM S1P elicited a long-lasting oscillatory current that continued over 30 min from the beginning of oscillation, with 300 nA (n = 11) as a usual maximum peak of current, whereas 1-microM LPA treatment showed only transiently oscillating but more vigorous current responses, with 2,800 nA (n = 18) as a maximum peak amplitude. Both phospholipid-induced Ca2+-dependent Cl- currents were observed in the absence of extracellular Ca2+, were blocked by intracellular injection of the Ca2+ chelator, EGTA, and could not be elicited by treatment with thapsigargin, an inhibitor of endoplasmic reticulum (ER) Ca2+ ATPase. Intracellular Ca2+ release appeared to be from inositol 1,4,5-trisphosphate (IP3)-sensitive Ca2+ store, because Cl- currents were blocked by heparin injection. Pretreatment with the aminosteroid, U-73122, an inhibitor of G protein-mediated phospholipase C (PLC) activation, to oocytes inhibited the current responses evoked both by S1P and LPA. However, when they were injected with 10 ng of antisense oligonucleotide (AS-ODN) against Xenopus phospholipase C (PLC-xbeta), oocytes could not respond to S1P application, whereas they responded normally to LPA, indicating that the S1P signaling pathway goes through PLC-xbeta, whereas LPA signaling goes through another unknown PLC. To determine the types of G proteins involved, we introduced AS-ODNs against four types of G-protein alpha subunits that were identified in Xenopus laevis; G(q)alpha, G11alpha, G0alpha, and G(i1)alpha. Among AS-ODNs against the G alphas tested, AS-G(q)alpha and AS-G(i1)alpha to S1P and AS-G(q)alpha and AS-G11alpha to LPA specifically reduced current responses, respectively, to about 20-30% of controls. These results demonstrate that LPA and S1P, although they have similar structural features, release intracellular Ca2+ from the IP3-sensitive pool, use different components in their signal transduction pathways in Xenopus oocytes.

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Co‐operation of G_sα and G_βγ in maintaining G₂ arrest in xenopus oocytes

Sheng

Montplaisir

2004

Journal Cellular Physiology

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Progesterone-induced oocyte maturation is thought to involve the inhibition of an oocyte adenylyl cyclase and reduction of intracellular cAMP. Our previous studies demonstrated that injection of inhibitors of G protein betagamma complex induces hormone-independent oocyte maturation. In contrast, over-expression of Xenopus Gbeta1 (xGbeta1), alone or together with bovine Ggamma2, elevates oocyte cAMP and inhibits progesterone-induced oocyte maturation. To further investigate the mechanism of Gbetagamma-induced oocyte maturation, we generated a mutant xGbeta1, substituting Asp-228 for Gly (D228G). An equivalent mutation in the mammalian Gbeta1 results in the loss of its ability to activate adenylyl cyclases. Indeed, co-injection of xGbeta1D228G with Ggamma2 failed to increase oocyte cAMP or inhibit progesterone-induced oocyte maturation. To directly demonstrate that oocytes contained a Gbetagamma-regulated adenylyl cyclase, we analyzed cAMP formation in vitro by using oocyte membrane preparations. Purified brain Gbetagamma complexes significantly activated membrane-bound adenylyl cyclase activities. Multiple adenylyl cyclase isoforms were identified in frog oocytes by PCR using degenerate primers corresponding to highly conserved catalytic amino acid sequences. Among these we identified a partial Xenopus adenylyl cyclase 7 (xAC7) that was 65% identical in amino acid sequence to human AC7. A dominant-negative mutant of xAC7 induced hormone-independent oocyte maturation and accelerated progesterone-induced oocyte maturation. Theses findings suggest that xAC7 is a major component of the G2 arrest mechanism in Xenopus oocytes.

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Inhibition of the adenylyl cyclase and activation of the phosphatidylinositol pathway in oocytes through expression of serotonin receptors does not induce oocyte maturation

Cited by 21 publications

References 48 publications

Xenopus oocyte prophase I meiotic arrest is released independently from a decrease in cAMP levels or PKA activity

Xenopus oocyte prophase I meiotic arrest is released independently from a decrease in cAMP levels or PKA activity

Different signaling pathway between sphingosine-1-phosphate and lysophosphatidic acid inXenopus oocytes: Functional coupling of the sphingosine-1-phosphate receptor to PLC-xβ inXenopus oocytes

Co‐operation of G_sα and G_βγ in maintaining G₂ arrest in xenopus oocytes

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Inhibition of the adenylyl cyclase and activation of the phosphatidylinositol pathway in oocytes through expression of serotonin receptors does not induce oocyte maturation

Cited by 21 publications

References 48 publications

Xenopus oocyte prophase I meiotic arrest is released independently from a decrease in cAMP levels or PKA activity

Xenopus oocyte prophase I meiotic arrest is released independently from a decrease in cAMP levels or PKA activity

Different signaling pathway between sphingosine-1-phosphate and lysophosphatidic acid inXenopus oocytes: Functional coupling of the sphingosine-1-phosphate receptor to PLC-xβ inXenopus oocytes

Co‐operation of Gsα and Gβγ in maintaining G2 arrest in xenopus oocytes

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Co‐operation of G_sα and G_βγ in maintaining G₂ arrest in xenopus oocytes