Changes in Nitric Oxide Synthase Activity in the Ovary of Gonadotropin Treated Rats. The Role of Nitric Oxide during Ovulation.

Nakamura, Yasuhiko; Kashida, Shiro; Nakata, Masahiko; Takiguchi, Shuji; Yamagata, Yuriko; Takayama, Hisako; Sugino, Norihiro; Katô, Hiroshi

doi:10.1507/endocrj.46.529

Cited by 34 publications

(21 citation statements)

References 44 publications

(42 reference statements)

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“…The increased amount of protein in the nucleus and cytoplasm in partially meiotically competent oocytes may be related to the acquisition of meiotic competence and the requirement of nitric oxide synthesis. Our results confirmed that eNOS is a frequently expressed isoform in mammalian oocytes (Van Voorhis et al, 1994;Jablonka-Shariff and Olson, 1997;Nishikimi et al, 2001;Mitchell et al, 2004) and is also abundant in the somatic compartments of the ovary (Zackrisson et al, 1996;Jablonka-Shariff and Olson, 1997;Jablonka-Shariff et al, 1999;Nakamura et al, 1999;Yamagata et al, 2002;Mitchell et al, 2004). The expression and distribution of eNOS in porcine oocytes do not deviate from this pattern Takesue et al, 2003).…”

Section: Discussionsupporting

confidence: 82%

“…However, works that concentrate on NOS isoform expression and localization contribute to its clarification. eNOS and iNOS isoforms were detected in fullygrown rat oocytes (Van Voorhis et al, 1994Zackrisson et al, 1996;Jablonka-Shariff and Olson, 1997;Jablonka-Shariff et al, 1999;Nakamura et al, 1999;Yamagata et al, 2002;Tao et al, 2004) and in mouse oocytes (Nishikimi et al, 2001;Mitchell et al, 2004). The nNOS isoform was not detected in oocytes.…”

mentioning

confidence: 91%

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Expression and localization of nitric oxide synthase isoforms during porcine oocyte growth and acquisition of meiotic competence

Eva¹,

Sedmı́ková²,

Petr³

et al. 2009

CZECH J ANIM SCI

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The intensive development of biotechnologies such as in vitro embryo production and cloning by nuclear transfer requires a great number of oocytes with fully-developed meiotic competence.During in vitro culture these oocytes are able to reach the stage of second meiotic metaphase and complete their meiotic maturation. However, the number of these oocytes in the ovary is limited. ABSTRACT: Reproduction biotechnologies depend on the use of fully meiotically competent oocytes. Growing oocytes without full meiotic competence are an interesting potential source due to their quantity, but the mechanisms regulating the processes of acquisition of meiotic competence have not been clarified to date. Nitric oxide synthase (NOS) and its product, nitric oxide (NO), may possibly play a role. Understanding the precise NO regulatory mechanism is therefore important for the development of in vitro growth methods. The objective of this work was to detect changes in the expression of NOS isoforms and their mRNA expression and changes in the intracellular localization of separate NOS isoforms during the growth period of the porcine oocyte, and also to determine whether these changes are related to the process of meiotic competence acquisition. mRNA for all NOS isoforms was already detected in oocytes at the beginning of their growth and was present in them until they completed their growth period. mRNA for iNOS and eNOS was also observed in granulosa and cumulus cells from these oocytes. But nNOS mRNA was not demonstrated in these types of cells. Pig oocytes and their surrounding cells contained all NOS proteins. Their amounts increased and localization changed with the acquisition of meiotic competence. nNOS was localized mainly in the cortex in meiotically incompetent oocytes, while meiotically competent oocytes contained nNOS in the nucleus as well. iNOS protein was distributed in the cytoplasm and nucleus in all oocytes, and meiotically incompetent oocytes contained iNOS in the nucleolus as well. eNOS protein was distributed in oocytes in the form of fine granules with a strong fluorescence signal. Protein was concentrated in the nuclear area in meiotically incompetent oocytes and also in the periphery in oocytes with partially and fully-developed meiotic competence. All these findings indicate that NOS isoforms may significantly influence the acquisition of meiotic competence in porcine oocytes.

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Section: Discussionsupporting

confidence: 82%

mentioning

confidence: 91%

Expression and localization of nitric oxide synthase isoforms during porcine oocyte growth and acquisition of meiotic competence

Eva¹,

Sedmı́ková²,

Petr³

et al. 2009

CZECH J ANIM SCI

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“…This effect is mediated largely by -receptors, the major receptor activated by ␤-endorphin, as naltrexone, a relatively specific -receptor antagonist, inhibited the action of ␤-endorphin on NOS activity. Recent studies indicate that NO is involved directly in the ovulatory process (Shukovski and Tsafriri, 1994;Bonello et al, 1996;Jablonka-Shariff and Olson, 1998;Drazen et al, 1999;Jablonka-Shariff et al, 1999;Mitsube et al, 1999;Nakamura et al, 1999). Faletti et al (1999a) reported that NO is involved in ovulation in the rats by stimulating the production of prostaglandins.…”

Section: Discussionmentioning

confidence: 99%

Interaction among beta-endorphin, nitric oxide and prostaglandins during ovulation in rats

Faletti¹,

Mohn

Farina

et al. 2003

Reproduction

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The aim of this study was to investigate the relationship between ␤-endorphin and nitric oxide (NO) during the ovulatory process in rats. Immature rats were treated with equine chorionic gonadotrophin-hCG to induce ovulation. An intrabursal injection of ␤-endorphin stimulated nitric oxide synthase (NOS) activity. This effect was completely reversed when naltrexone was co-injected with ␤-endorphin. The stimulatory action of ␤-endorphin on NOS activity was studied to determine whether it was exerted via prostaglandins. Treatment with prostaglandin E 2 (PGE 2 ) completely reversed the ␤-endorphin-induced stimulation of NOS activity. Moreover, intrabursal injection of meloxicam, an inhibitor of cyclooxygenase 2, increased NOS activity, but this effect was not altered by co-injection with ␤-endorphin. The presence of both endothelial NOS (eNOS) and inducible NOS (iNOS) in the ovary at 10 h after hCG treatment was studied by western blot analysis. Local administration of ␤-endorphin inhibited the expression of eNOS protein, whereas expression of iNOS protein was not detectable. Ovarian ␤-endorphin content was diminished at 10 h after hCG injection. Treatment with prostaglandin synthesis inhibitors in vivo augmented the ovarian ␤-endorphin content. In conclusion, these results indicate that ␤-endorphin stimulates the activity of ovarian NOS indirectly by inhibiting prostaglandin production.

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“…It has been reported that iNOS or eNOS could be detected in porcine or mouse follicles, granulosa cells, cumulus cells and oocytes (Hattori et al 2001, Takesue et al 2003, Mitchell et al 2004. Expression of eNOS increases after the luteinizing hormone surge or human chorionic gonadotropin (hCG) injection (Van Voorhis et al 1995, Jablonka-Shariff & Olson 1998, Nakamura et al 1999, and eNOS-derived NO stimulates the ovulatory process (Shukovski & Tsafriri 1994, Powers et al 1995, Bonello et al 1996, Hesla et al 1997, Yamauchi et al 1997, Jablonka-Shariff & Olson 1998, Jablonka-Shariff et al 1999. The reports about changes in iNOS expression during this process are controversial (Matsumi et al 1998), and the role of iNOS-derived NO is unclear.…”

Section: Introductionmentioning

confidence: 99%

Inducible nitric oxide synthase-derived nitric oxide regulates germinal vesicle breakdown and first polar body emission in the mouse oocyte

Huo

Liang²,

Yu³

et al. 2005

Reproduction

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The present study investigated the subcellular localization of inducible nitric oxide synthase (iNOS) during mouse oocyte meiotic maturation and fertilization using confocal microscopy, and further studied the roles of iNOS-derived NO in oocyte maturation by using an iNOS-specific inhibitor aminoguanidine (AG) and iNOS antibody microinjection. In germinal vesiclestage oocytes, iNOS immunoreactivity was mainly localized in the germinal vesicle. Shortly after germinal vesicle breakdown, the iNOS immunoreactivity accumulated around the condensed chromosomes. At metaphase I and metaphase II, with the organization of chromosomes to the equatorial plate, iNOS immunoreactivity was concentrated around the aligned chromosomes, putatively the position of the metaphase spindle. The accumulation of iNOS immunoreactivity could not be detected at anaphase I and anaphase II. However, at telophase I and telophase II, the staining of iNOS was concentrated in the region between the separating chromosomes/chromatids. Furthermore, the staining of iNOS also accumulated in the male and female pronuclei in fertilized eggs. Germinal vesicle breakdown and the first polar body emission of the oocytes were significantly blocked by the iNOS-specific inhibitor AG in a dose-dependent manner. The germinal vesicle breakdown in oocytes injected with iNOS antibody was also inhibited. We found that the phosphorylation of mitogen-activated protein kinase in oocytes after germinal vesicle breakdown was inhibited by AG treatment. The control oocytes extruded a normal first polar body, while the AG-treated oocytes exhibited an elongated protrusion or no elongated protrusion. The results of confocal microscopy showed that the AG-treated oocytes were arrested at anaphase I -telophase I. Our results suggest that the iNOSderived NO pathway plays important roles in mouse oocyte meiotic maturation, especially in germinal vesicle breakdown and the anaphase -telophase transition.

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Changes in Nitric Oxide Synthase Activity in the Ovary of Gonadotropin Treated Rats. The Role of Nitric Oxide during Ovulation.

Cited by 34 publications

References 44 publications

Expression and localization of nitric oxide synthase isoforms during porcine oocyte growth and acquisition of meiotic competence

Expression and localization of nitric oxide synthase isoforms during porcine oocyte growth and acquisition of meiotic competence

Interaction among beta-endorphin, nitric oxide and prostaglandins during ovulation in rats

Inducible nitric oxide synthase-derived nitric oxide regulates germinal vesicle breakdown and first polar body emission in the mouse oocyte

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