Nitric Oxide Synthase and cGMP in the Anterior Pituitary Gland: Effect of a GnRH Antagonist and Nitric Oxide Donors

Yamada, Kaoru; Xu, Zhi‐Qing David; Zhang, Xu; Gustafsson, Lars E.; Hulting, Anna‐Lena; Vente, Jan de; Steinbusch, Harry W.; Hökfelt, Tomas

doi:10.1159/000127175

Cited by 30 publications

(19 citation statements)

References 20 publications

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“…Using a direct in situ immunodetection technique to reveal cGMP-producing cells in response to NO donors in rat pituitary slices, Yamada et al (66) identified essentially gonadotrophs, suggesting that these cells primarily contained a functionally reactive sGC, or enough sGC to produce detectable levels of cGMP under these conditions. Surprisingly, in such studies no cGMP response to NO donors could be detected in folliculo-stellate cells (66). The same was recently observed by the McArdle's group (67) using a folliculostellate cell line (TtT-GF) and classical cGMP assay.…”

Section: Discussionmentioning

confidence: 99%

Pituitary Adenylate Cyclase-activating Polypeptide Stimulates Nitric-oxide Synthase Type I Expression and Potentiates the cGMP Response to Gonadotropin-releasing Hormone of Rat Pituitary Gonadotrophs

Garrel

Lozach²,

Bachir³

et al. 2002

Journal of Biological Chemistry

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Nitric-oxide synthase type I (NOS I) is expressed primarily in gonadotrophs and in folliculo-stellate cells of the anterior pituitary. In gonadotrophs, the expression and the activity of NOS I are stimulated by gonadotropin-releasing hormone (GnRH) under both experimental and physiological conditions. In the present study, we show that pituitary adenylate cyclase-activating polypeptide (PACAP) is twice as potent as GnRH at increasing NOS I levels in cultured rat anterior pituitary cells. The action of PACAP is detectable after 4 -6 h and maximal at 24 h, this effect is mimicked by 8-bromocAMP and cholera toxin and suppressed by H89 suggesting a mediation through the cAMP pathway. Surprisingly, NADPH diaphorase staining revealed that these changes occurred in gonadotrophs exclusively although PACAP and cAMP, in contrast to GnRH, have the potential to target several types of pituitary cells including folliculo-stellate cells. There was no measurable alteration in NOS I mRNA levels after cAMP or PACAP induction. PACAP also stimulated cGMP synthesis, which was maximal within 15 min and independent of cAMP, however, only part resulted from NOS I/soluble guanylate cyclase activation implying that in contrast to GnRH, PACAP has a dual mechanism in cGMP production. Interestingly, induction of NOS I by PACAP markedly enhanced the capacity of gonadotrophs to produce cGMP in response to GnRH. The fact that PACAP may act on gonadotrophs to alter NOS I levels, generate cGMP, and potentiate the cGMP response to GnRH, suggests that cGMP could play important cellular functions.

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Section: Discussionmentioning

confidence: 99%

Pituitary Adenylate Cyclase-activating Polypeptide Stimulates Nitric-oxide Synthase Type I Expression and Potentiates the cGMP Response to Gonadotropin-releasing Hormone of Rat Pituitary Gonadotrophs

Garrel

Lozach²,

Bachir³

et al. 2002

Journal of Biological Chemistry

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“…Sections were processed for immunocytochemistry as described (de Vente et al, 1996a,b;Yamada et al, 1997). Antisera used were a polyclonal sheep anticGMP (Tanaka et al, 1997; diluted 1:4000), a polyclonal rabbit anti-cGMP (de Vente et al, 1996a,b; diluted 1:300) and a polyclonal sheep anti-bNOS (kindly provided by Dr P.C.…”

Section: Bnos-and Cgmp-immunohistochemistry On Cryo-sectionsmentioning

confidence: 99%

“…Dilutions of the sera were made in filtered TBS supplemented with 0.3% Triton X-100. The specificity of these antisera in staining mammalian tissues has been largely demonstrated (de Vente et al, 1996a,b;Herbison et al, 1996;Tanaka et al, 1997;Yamada et al, 1997). In the single cGMP-immunostaining procedure, secondary antisera used were the CY3-labeled goat anti-rabbit IgG (Jackson; diluted 1:800) or the FITC-labeled rabbit anti-sheep (Calbiochem, La Jolla, CA; diluted 1:150), depending on the host species of the primary antiserum.…”

Section: Bnos-and Cgmp-immunohistochemistry On Cryo-sectionsmentioning

confidence: 99%

Nitric oxide synthase and background adaptation in Xenopus laevis

Allaerts

Ubink

Vente

et al. 1997

Journal of Chemical Neuroanatomy

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Adaptation of the skin colour to the background light condition in the amphibian Xenopus lae6is is achieved by migration of pigment granules in the skin melanophores, a process regulated by h-MSH secretion from melanotrope cells in the pituitary pars intermedia (PI). h-MSH secretion in turn, is regulated by various stimulatory and inhibitory messengers synthesized in brain nuclei, especially the hypothalamic suprachiasmatic and magnocellular nuclei and the locus coeruleus in the hindbrain.In the present study, the roles in background adaptation of nitric oxide (NO) and NO synthase (NOS) enzyme activity were evaluated. In situ, using both immunohistochemistry with anti-human brain NOS (bNOS) serum in paraffin-embedded material and using nicotinamide adenine dinucleotide phosphate-diaphorase (NADPH-d) histochemistry in cryo-sections, we showed NOS in neurons in the optic tectum and in the locus coeruleus. NADPH-d reactivity was also found in neurons in the lateral amygdala, the ventral hypothalamic nucleus and in fibers in the median eminence. Using a Western blot stained with an anti-human bNOS serum, we demonstrated a 150 kDa band in Xenopus hindbrain lysates, which is similar to the NOS protein present in the rat anterior pituitary, but which was not detectable in the lysates from both the neurointermediate and distal lobes in Xenopus. No differences in histochemical staining pattern or on Western blotting were observed between animals adapted to a black or a white background.Paraffin sections of the endocrine PI and pars distalis did not reveal bNOS-like immunoreactivity. NADPH-d reactivity was observed in the endothelia of this gland. However, using a new procedure of thin cryo-sections of pituitary neurointermediate lobes, we observed bNOS-immunoreactive fibers as well as cyclic 3%,5% guanosine monophosphate (cGMP)-accumulating fibers in the PI.The PI may be regulated by NOergic neurons from higher brain centers. The possibility that NOergic neurons in the locus coeruleus are involved in the innervation of the PI needs further investigation. The latter neurons are probably not noradrenergic because double labeling studies show no co-localization of NADPH-d reactivity and tyrosine hydroxylase immunoreactivity in locus coeruleus neurons. © 1997 Elsevier Science B.V.

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“…cGMP mediates NO effects on prolactin release (11). Although evidence for cGMP production in lactotrophs has not been obtained to date (33), our results indicate that this cyclic nucleotide participates in the regulation of prolactin release.…”

Section: Discussionmentioning

confidence: 47%

Role of phosphodiesterase and protein kinase G on nitric oxide-induced inhibition of prolactin release from the rat anterior pituitary

Velardez

Laurentiis²,

Diaz³

et al. 2000

European Journal of Endocrinology

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Objective: In order to determine the mechanism by which nitric oxide (NO) inhibits prolactin release, we investigated the participation of cGMP-dependent cAMP-phosphodiesterases (PDEs) and protein kinase G (PKG) in this effect of NO. Methods: Anterior pituitary glands of male rats were incubated with inhibitors of PDE and PKG with or without sodium nitroprusside (NP). Prolactin release, and cAMP and cGMP concentrations were determined by RIA. Results and conclusions: The inhibitory effect of NP (0.5 mmol/l) on prolactin release and cAMP concentration was blocked by EHNA (10 ±4 mol/l) and HL-725 (10 ±4 mol/l), inhibitors of cGMPstimulated cAMP-PDE (PDE2). 8-Br-cGMP (10 ±4 and 10 ±3 mol/l), which mimics cGMP as a mediator of NP effects on prolactin release, also decreased cAMP concentration. Zaprinast (10 ±4 mol/l), a selective inhibitor of speci®c cGMP-PDE (PDE5), potentiated the NP effect on cAMP concentration. thio]-cGMP triethylamine (Rp-8-cGMP, 10 ±7 ±10 ±6 mol/l), an inhibitor of PKG, reversed the effect of NP on prolactin release. The present study suggests that several mechanisms are involved in the inhibitory effect of NO on prolactin release. The activation of PDE2 by cGMP may mediate the inhibitory effect of NO on cAMP concentration and therefore on prolactin release. NO-activated PKG may also be participating in the inhibitory effect of NO on prolactin release.

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Nitric Oxide Synthase and cGMP in the Anterior Pituitary Gland: Effect of a GnRH Antagonist and Nitric Oxide Donors

Cited by 30 publications

References 20 publications

Pituitary Adenylate Cyclase-activating Polypeptide Stimulates Nitric-oxide Synthase Type I Expression and Potentiates the cGMP Response to Gonadotropin-releasing Hormone of Rat Pituitary Gonadotrophs

Pituitary Adenylate Cyclase-activating Polypeptide Stimulates Nitric-oxide Synthase Type I Expression and Potentiates the cGMP Response to Gonadotropin-releasing Hormone of Rat Pituitary Gonadotrophs

Nitric oxide synthase and background adaptation in Xenopus laevis

Role of phosphodiesterase and protein kinase G on nitric oxide-induced inhibition of prolactin release from the rat anterior pituitary

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