Autoradiographic visualization of the natriuretic peptide receptor-B in rat tissues

Konrad, Edyta M.; Thibault, Gaétan; Schiffrin, Ernesto L.

doi:10.1016/0167-0115(92)90539-7

Cited by 35 publications

(15 citation statements)

References 29 publications

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“…This protein seemed to be specific for pituitary cells, and its concentration in nuclear extract coincided with the efficiency of the CNP promoter function (GH3 > GH1 > AtT20/D16V-F2 > RASMC and FR). The molecular weight of 70,000 apparently differs from those of SP-1 (95,000 to 105,000 [16]), AP-2 (52,000 [24]), and Pit-1 (33,000 [2] (20,43), it is possible that CNP may act locally in the anterior pituitary as an autocrine or paracrine regulator. Our observation that the CNP promoter functioned more effectively in GH3 cells than in GH1 cells provides another speculation that CNP might have significant physiological roles in somatomammotrophs, proposed progenitor cells of somatotrophs and lactotrophs (4)-in their differentiation process, for example.…”

Section: Resultsmentioning

confidence: 99%

“…While ANP and BNP are mainly cardiac hormones (27), CNP is localized in the brain and very little is detected in other peripheral tissues, including the heart (19,28,42). A receptor specific for CNP has been designated the ANP-B (or GC-B) receptor (18) and has been shown to exist in the brain and pituitary gland (20,43). Therefore, it is possible that CNP functions in a manner distinct from ANP and BNP, as a neuromodulator, for example.…”

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confidence: 99%

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Cell-type-specific function of the C-type natriuretic peptide gene promoter in rat anterior pituitary-derived cultured cell lines.

1993

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The promoter function of the human C-type natriuretic peptide (CNP) (23,38), and then was identified in rat and human brains (19,28). CNP shares considerable sequence homology with ANP and BNP, especially within the 17-residue ring portion formed by a disulfide bond between two cysteine residues. According to the cloned cDNA and genes for CNP from various species (17,19,28,40,41), the structure of CNP is highly conserved among species, and rat, porcine, and human CNP-22 are actually identical. CNP seems to exert pharmacological actions similar to those of ANP and BNP, including natriuretic, diuretic, and vasorelaxant effects (40), albeit with lesser potency. Although the vasorelaxant activity of CNP in the isolated rat aorta is 16-fold lower than that of ANP, CNP is a more effective stimulator of cyclic GMP generation in cultured vascular smooth muscle cells (8) and may be a more potent growth inhibitor of these cells than ANP is (9). While ANP and BNP are mainly cardiac hormones (27), CNP is localized in the brain and very little is detected in other peripheral tissues, including the heart (19, 28, 42). A receptor specific for CNP has been designated the ANP-B (or GC-B) receptor (18) and has been shown to exist in the brain and pituitary gland (20, 43). Therefore, it is possible that CNP functions in a manner distinct from ANP and BNP, as a neuromodulator, for example. As a matter of fact, CNP is suggested to have some actions on the rat central nervous system (12,13,31

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Cell-type-specific function of the C-type natriuretic peptide gene promoter in rat anterior pituitary-derived cultured cell lines.

1993

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“…Many previous studies have established the presence of the CNP and its receptor, GC-B, in rat, mouse, and sheep pituitaries (Komatsu et al 1991, Konrad et al 1992, Minamino et al 1993, Yandle et al 1993, McArdle et al 1994, Herman et al 1996, Thompson et al 2009), yet the expression of GC-B in human pituitary tissue has not been reported. We show for the first time that NPR2 expression is found in normal human fetal pituitary samples, ranging from 12 to 20 weeks of gestation, suggesting that natriuretic peptide signaling is required during pituitary development in humans.…”

Section: Discussionmentioning

confidence: 99%

Expression of guanylyl cyclase-B (GC-B/NPR2) receptors in normal human fetal pituitaries and human pituitary adenomas implicates a role for C-type natriuretic peptide

Thompson¹,

Chand²,

King³

et al. 2012

Endocrine-Related Cancer

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C-type natriuretic peptide (CNP/Nppc) is expressed at high levels in the anterior pituitary of rats and mice and activates guanylyl cyclase B receptors (GC-B/Npr2) to regulate hormone secretion. Mutations in NPR2/Npr2 can cause achondroplasia, GH deficiency, and female infertility, yet the normal expression profile within the anterior pituitary remains to be established in humans. The current study examined the expression profile and transcriptional regulation of NPR2 and GC-B protein in normal human fetal pituitaries, normal adult pituitaries, and human pituitary adenomas using RT-PCR and immunohistochemistry. Transcriptional regulation of human NPR2 promoter constructs was characterized in anterior pituitary cell lines of gonadotroph, somatolactotroph, and corticotroph origin. NPR2 was detected in all human fetal and adult pituitary samples regardless of age or sex, as well as in all adenoma samples examined regardless of tumor origin. GC-B immunoreactivity was variable in normal pituitary, gonadotrophinomas, and somatotrophinomas. Maximal transcriptional regulation of the NPR2 promoter mapped to a region within K214 bp upstream of the start site in all anterior pituitary cell lines examined. Electrophoretic mobility shift assays revealed that this region contains Sp1/Sp3 response elements. These data are the first to show NPR2 expression in normal human fetal and adult pituitaries and adenomatous pituitary tissue and suggest a role for these receptors in both pituitary development and oncogenesis, introducing a new target to manipulate these processes in pituitary adenomas.

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“…Immunoreactive CNP and CNP-specific ANP-B receptor as well as ANP-specific ANP-A receptor has been detected in anterior pituitary glands [5,15,161. To investigate whether CNP has any biological effect(s) on pituitary-derived cell lines, we first examined the response of those cells to CNP by monitoring the intracellular cGMP level which should increase if guanylate-cyclase-coupled ANP receptor exists on the cell surface.…”

Section: Response Of Pituitary-derived Cells To Cnp and Anpmentioning

confidence: 99%

C‐type natriuretic peptide stimulates secretion of growth hormone from rat‐pituitary‐derived GH3 cells via a cyclic‐GMP‐mediated pathway

Shimekake

Ohta

Nagata

1994

European Journal of Biochemistry

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Although C-type natriuretic peptide (CNP) has been shown to exist at the highest concentration in the anterior pituitary in rat tissues, its physiological role(s) there is (are) not clear. In this study, we report a novel function of CNP examined with anterior pituitary-derived cell lines, GH3 and AtT20/D16v-F2. Both CNP and atrial natriuretic peptide (ANP) increased cellular cGMP levels in both cell lines in dose-dependent manners. CNP, but not ANP, stimulated growth hormone (GH) release from GH3 cells. In contrast, neither ANP nor CNP had any significant effect on the corticotropin release from AtT20/D16v-F2 cells. An activator for cGMP-dependent protein kinase (cGK), dibutyryl cGMP, mimicked the stimulation of GH release from GH3 cells by CNP. Constitutive GH release from GH3 cells was greatly diminished in the presence of inhibitors for CAMP-dependent protein kinase, while stimulative GH release by CNP was not affected. However, inhibitors which can block cGK almost completely diminished the stimulative effect of CNP. An inhibitor for protein kinase C did not show any effect on either constitutive or CNP-stimulative GH release. Our observations indicate that the stimulation of GH release from GH3 cells by CNP is mediated mainly by the cGK signal-transduction pathway, not by CAMP-dependent protein kinase or protein kinase C, through a CNP-specific receptor (possibly ANP-B receptor). Thus, CNP may act as a local modulator in the anterior pituitary.C-type natriuretic peptide (CNP) is the third member of the mammalian natriuretic peptide family discovered following atrial natriuretic peptide (ANP) [l] and brain natriuretic peptide (BNP) [2]. CNP was first isolated from porcine brain [3, 41, then identified in rat and human brains [5, 61. CNP possesses sequence similarity to ANP and BNP. According to the cloned cDNA and genes for CNP from various species [5-91, its structure is highly conserved among species and, actually, rat, porcine and human CNP-22, the smaller molecular form with 22 amino acid residues, are identical. CNP has been shown to exert pharmacological actions similar to ANP and BNP, for example, natriuretic, diuretic and vasorelaxant effects [lo, l l ] , albeit with a lesser Correspondence to K. Nagata, Shionogi Research Laboratories, Shionogi & Co., Ltd., 5-12-4 Sagisu, Fukushima-ku, Osaka, Japan 553Abbreviations. CNP, C-type natriuretic peptide ; ANP, atrial natriuretic peptide; BNP, brain natriuretic peptide; GH, growth hormone ; ACTH, corticotropin ; PRL, prolactin ; cGK, cGMP-dependent protein kinase; cAK, CAMP-dependent protein kinase ; PKC, protein kinase C ; db-CAMP, N6,2'-O-dibutyryladenosine 3':5'-cyclic monophosphate (sodium salt) ; db-cGMP, iV,2'-O-dibutyrylguanosine 3':5'-cyclic monophosphate (sodium salt); H-85, N-[2-(N-formyl-p-chlorocinnamylamino)ethyl]-5-isoquinolinesulfona~de; H-88, N-(2-cinnamylaminoethyl)-5-isoquinolinesulfonamide ; H-89, N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide; KT-5720, (SR, 9S, 11S)-( -)-9-hydroxy-9-hexyloxycarbonyl-8-methy1-2,3,9,10-tetrah...

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Autoradiographic visualization of the natriuretic peptide receptor-B in rat tissues

Cited by 35 publications

References 29 publications

Cell-type-specific function of the C-type natriuretic peptide gene promoter in rat anterior pituitary-derived cultured cell lines.

Cell-type-specific function of the C-type natriuretic peptide gene promoter in rat anterior pituitary-derived cultured cell lines.

Expression of guanylyl cyclase-B (GC-B/NPR2) receptors in normal human fetal pituitaries and human pituitary adenomas implicates a role for C-type natriuretic peptide

C‐type natriuretic peptide stimulates secretion of growth hormone from rat‐pituitary‐derived GH3 cells via a cyclic‐GMP‐mediated pathway

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