Ultracytochemical localization of particulate guanylate cyclase in rat adrenal gland exposed to stimulation by porcine brain natriuretic peptide

Rambotti, Maria Grazia; Ercolani, Piergiacomo; Spreca, A

doi:10.1007/bf00159503

Cited by 11 publications

(3 citation statements)

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“…Recently we detected the presence of rANF and pBNP GC capable of stimulating on intracellular membranes in rat adrenal gland (Rambotti et aL, 1993) and in rat neurohypophysis (Rambotti et al, 1994). A fraction of particulate GC was previously seen on various subcellular membranes (for a review see Tremblay et al, 1988), and intracellular ANF binding sites were detected in some subcellular structures (e.g.…”

Section: Discussionmentioning

confidence: 89%

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Ultracytochemical localization of particulate guanylate cyclase after stimulation with natriuretic peptides in lamb olfactory mucosa

Spreca

Rambotti

1994

Histochem J

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The ultracytochemical localization of particulate guanylate cyclase has been studied in lamb olfactory mucosa after activation with rat atrial natriuretic factor (rANF), porcine brain natriuretic peptide (pBNP), porcine C-type natriuretic peptide (pCNP) or rat brain natriuretic peptide (rBNP). Particulate guanylate cyclase is the receptor for these peptides and recently two subtypes of the cyclase have been identified. These isoforms are stimulated differently by ANF, BNP and CNP. Under our experimental conditions, rANF, pCNP and pBNP were strong activators of particulate guanylate cyclase in lamb olfactory mucosa, as demonstrated by the presence of reaction product. Samples incubated in basal conditions without rANF, pCNP or pBNP, or samples incubated in presence of rBNP did not reveal any cyclase activity. The rANF-stimulated cyclase activity was localized in the apical portion of olfactory epithelium. pCNP-stimulated guanylate cyclase was detected to the lamina propria in association with secretory cells of Bowman's glands and with cells in close relation with Bowman's glands (elongated cells and myoepithelial cells). The cyclase activity stimulated by pBNP was limited to cells of Bowman's glands. The present data indicate that ANF and CNP are recognized by different receptors and that BNP and CNP bind to the same receptor.

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Section: Discussionmentioning

confidence: 89%

“…Recently, we have carried out analogous studies on membrane-bound GC activity stimulated by ANF and BNP in several rat organs such as kidney, lung and adrenal gland (Rambotti et al, 1990;Rambotti et al, 1993), in rabbit platelets (Spreca et aI., 1991) and in neurohypophysis (Rambotti et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Ultracytochemical localization of particulate guanylate cyclase after stimulation with natriuretic peptides in lamb olfactory mucosa

Spreca

Rambotti

1994

Histochem J

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“…In fact, it has been shown that acetylcholine (Rodriguez-Pascual et al 1994 and the preganglionic transmitter NPY, present in some ganglion neurons (Schalling et al 1988) as well as in chromaffin cells (Allen et al 1983;Lundberg et al 1983), cause a rapid, transient increase in medullary cGMP levels (Soares-Lemos et al 1997). It may be mentioned that Rambotti et al (1993) have shown that brain natriuretic peptide activates particulate GC, but not the sGC in the adrenal gland, mainly in zona glomerulosa and fasciculata in cortex and in the adrenaline cells of the medulla.…”

Section: Discussionmentioning

confidence: 98%

The distribution of cGMP in the adrenal gland in the rat, guinea pig and mouse after stimulation with sodium nitroprusside

Holmberg

Steinbusch

Vente

et al. 1998

Cell and Tissue Research

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Nitric oxide (NO) acts as an intercellular messenger molecule in the nervous system. In the adrenal gland sympathetic preganglionic fibers innervating the medulla, as well as intrinsic neural ganglion cells, contain nitric oxide synthase (NOS). Nitric oxide stimulates the soluble enzyme guanylate cyclase forming cyclic GMP (cGMP). Using sodium nitroprusside (SNP) as nitric oxide donor we have studied the putative target cells for nitric oxide in the rat adrenal gland, both in vivo and in vitro. The guinea pig and a few mouse adrenal glands were studied after SNP perfusion for comparison. Our results show that after vascular perfusion with a high concentration (3 mM) of SNP both noradrenaline and adrenaline chromaffin cells express cGMP-like immunoreactivity in all three species. After incubation of rat adrenal slices with SNP primarily the noradrenaline chromaffin cells are cGMP-positive. In contrast, detectable levels of cGMP-like immunoreactivity were not found in neuronal ganglion cells. In the adrenal cortex cGMP-like immunoreactivity was seen in blood vessel walls, in small cells with processes forming a reticular network, at least partly presumably representing endothelial cells, as well as in some presumable nerve terminals. These findings support the view that chromaffin cells, especially the noradrenergic ones and blood vessels, are targets for nitric oxide in the adrenal gland.

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Ultracytochemistry as a tool for the study of the cellular and subcellular localization of membrane-bound guanylate cyclase (GC) activity. Applicability to both receptor-activated and receptor-independent GC activity

et al. 2002

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Ultracytochemical localization of particulate guanylate cyclase in rat adrenal gland exposed to stimulation by porcine brain natriuretic peptide

Cited by 11 publications

References 57 publications

Ultracytochemical localization of particulate guanylate cyclase after stimulation with natriuretic peptides in lamb olfactory mucosa

Ultracytochemical localization of particulate guanylate cyclase after stimulation with natriuretic peptides in lamb olfactory mucosa

The distribution of cGMP in the adrenal gland in the rat, guinea pig and mouse after stimulation with sodium nitroprusside

Ultracytochemistry as a tool for the study of the cellular and subcellular localization of membrane-bound guanylate cyclase (GC) activity. Applicability to both receptor-activated and receptor-independent GC activity

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