Cell density modulates the decrease of cytosolic free Ca2+ induced by atrial natriuretic hormone, <i>S</i>-nitroso-<i>N</i>-acetylpenicillamine and 8-bromo cyclic GMP in cultured rat mesangial cells

Lermioglu, Ferzan; Goyal, Jawahar Lal; Hassid, Aviv

doi:10.1042/bj2740323

Cited by 17 publications

(11 citation statements)

References 24 publications

(31 reference statements)

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“…S-Nitroso-N-acetylpenicillamine rapidly releases nitric oxide in aqueous solution at 37" in concentrations sufficient to stimulate intracellular guanylate cyclase (Field et al 1978;Wood & Ignarro 1987;Lermioglu et al 1991). S-Nitroso-N-acetylpenicillamine (1 .O mM) had no affect on basal rates of glycogenolysis in isolated rat hepatocytes ( Table 1).…”

Section: Resultsmentioning

confidence: 99%

Inhibition of Glucagon‐Stimulated Glycogenolysis by S‐Nitroso‐N‐acetylpenicillamine*

Brass

Vetter

1993

Pharmacology & Toxicology

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Rat liver is known to contain both a nitric oxide-stimulated guanylate cyclase and a cGMP-stimulated cAMP-phosphodiesterase. To evaluate the possible function of this system, the effect of the nitric oxide generating compound S-nitroso-N-acetylpenicillamine on glycogenolysis was evaluated in isolated rat hepatocytes. S-nitroso-N-acetylpenicillamine (1.0 mM) inhibited glucagon-stimulated glycogenolysis by 15%, but had no effect on basal rates of glycogenolysis. Inhibition of hepatocyte glycogenolysis by S-nitroso-N-acetylpenicillamine was associated with accumulation of cGMP (1.5 pmol/2.0 x 10(6) cells/2 min.). Exogenous 8-Br-cGMP (1.0 mM) inhibited hepatocyte glucagon-stimulated glycogenolysis by a magnitude similar to that observed with S-nitroso-N-acetylpenicillamine. S-nitroso-N-acetylpenicillamine had no effect on phenylephrine-stimulated glycogenolysis, but inhibited 8-bromo-cAMP-stimulated glycogenolysis by 15%. These observations suggest that S-nitroso-N-acetylpenicillamine inhibits cAMP-mediated stimulation of glycogenolysis at a site distal to adenylate cyclase. In summary, hepatocyte glucagon-stimulated glycogenolysis was inhibited to a small, but significant, degree by S-nitroso-N-acetylpenicillamine. This inhibition is consistent with a nitric oxide mediated stimulation of guanylate cyclase and consequent stimulation of cAMP-phosphodiesterase activity. Nitric oxide may contribute to altered carbohydrate homeostasis under pathophysiologic conditions.

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Section: Resultsmentioning

confidence: 99%

Inhibition of Glucagon‐Stimulated Glycogenolysis by S‐Nitroso‐N‐acetylpenicillamine*

Brass

Vetter

1993

Pharmacology & Toxicology

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“…Many studies exist that examine the regulation of calcium transport by natriuretic peptides 12 . All knowledge about regulation of [Ca 2+ ] i by ANP, however, concentrates on the ‘classical’ target cells of natriuretic peptides, such as cardiac and vascular myocytes, 13 , 14 endothelial cells 15 and mesangial cells 16 . To our knowledge, no studies exist on the influence of ANP on the Ca 2+ status of macrophages.…”

Section: Discussionmentioning

confidence: 99%

Elevation of intracellular calcium levels contributes to the inhibition of nitric oxide production by atrial natriuretic peptide

Kiemer¹,

Vollmar²

2001

Immunol Cell Biol

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Atrial natriuretic peptide (ANP) attenuates LPS‐induced inducible nitric oxide synthase (iNOS) expression in murine macrophages by destabilizing iNOS mRNA. Because elevated intracellular free Ca2+ levels [Ca2+]i reduce iNOS mRNA stability, the aim of the present study was to determine whether inhibition of iNOS by ANP is due to alterations in intracellular calcium. As determined by fluorescence photometry, ANP (10–7 and 10–6 mol/L) was shown to elevate intracellular calcium levels in bone marrow‐derived macrophages. This effect seemed to be mediated via the guanylate cyclase‐coupled A receptor, because dibutyryl‐cGMP mimicked and the A‐receptor antagonist HS‐142‐1 partially abrogated the effect of ANP. Because the Ca2+ increase was also observed in Ca2+‐free buffer, it is suggested that the liberation of intracellular calcium pools contributes to the elevation of [Ca2+]i by ANP. The B‐receptor ligand C‐type natriuretic peptide (CNP), which does not alter iNOS expression, had no effect on [Ca2+]i. The Ca2+‐ionophore 4‐Br‐A23187 and thapsigargin, a compound known to liberate Ca2+ from intracellular stores, were further demonstrated to reduce LPS‐induced NO production in macrophages (Griess assay), confirming a functional link for elevated [Ca2+]i and iNOS inhibition. These effects were abrogated by coincubation with extra‐ as well as intracellular Ca2+ chelators (EGTA, 1,2‐bis(o‐aminophenoxy)ethane‐N,N,N′,N′‐tetraacetic acid (BAPTA)). The inhibitory effect of ANP on NO production was also abrogated by Ca2+ chelation. These findings support a causal relationship between reduced iNOS induction and elevation of [Ca2+]i. Taken together, the data indicate that intracellular Ca2+ elevation by ANP is involved in the inhibition of LPS‐induced nitric oxide production in macrophages.

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“…The variable levels of phospho-ERK and JNK were likely due to the rapidly fluctuating levels of intracellular cGMP, a phenomenon that is known to occur in cultured cells (61). During the growth phase of RASMC in the presence of serum, the intracellular levels of cGMP are some 10 -100-fold greater when compared with cells approaching confluence (62). 3 These high levels of cGMP activate PKG I␣ during growth, thus accounting for the higher basal activity of ERK and JNK and in the stably transfected cell lines.…”

Section: Discussionmentioning

confidence: 99%

Activation of Mitogen-activated Protein Kinase Pathways by Cyclic GMP and Cyclic GMP-dependent Protein Kinase in Contractile Vascular Smooth Muscle Cells

Komalavilas

Shah

et al. 1999

Journal of Biological Chemistry

136

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Vascular smooth muscle cells (VSMC) exist in either a contractile or a synthetic phenotype in vitro and in vivo.The molecular mechanisms regulating phenotypic modulation are unknown. Previous studies have suggested that the serine/threonine protein kinase mediator of nitric oxide (NO) and cyclic GMP (cGMP) signaling, the cGMP-dependent protein kinase (PKG) promotes modulation to the contractile phenotype in cultured rat aortic smooth muscle cells (RASMC). Because of the potential importance of the mitogen-activated protein kinase (MAP kinase) pathways in VSMC proliferation and phenotypic modulation, the effects of PKG expression in PKG-deficient and PKG-expressing adult RASMC on MAP kinases were examined. In PKG-expressing adult RASMC, 8-para-chlorophenylthio-cGMP activated extracellular signal-regulated kinases (ERK1/2) and c-Jun N-terminal kinase (JNK). The major effect of PKG activation was increased activation by MAP kinase kinase (MEK). The cAMP analog, 8-Br-cAMP inhibited ERK1/2 activation in PKG-deficient and PKG-expressing RASMC but had no effect on JNK activity. The effects of PKG on ERK and JNK activity were additive with those of platelet-derived growth factor (PDGF), suggesting that PKG activates MEK through a pathway not used by PDGF. The stimulatory effects of cGMP on ERK and JNK activation were also observed in low-passaged, contractile RASMC still expressing endogenous PKG, suggesting that the effects of PKG expression were not artifacts of cell transfections. These results suggest that in contractile adult RASMC, NO-cGMP signaling increases MAP kinase activity. Increased activation of these MAP kinase pathways may be one mechanism by which cGMP and PKG activation mediate c-fos induction and increased proliferation of contractile adult RASMC. Vascular smooth muscle cell (VSMC)1 proliferation and migration are associated with several vascular diseases such as atherosclerosis and restenosis following vascular injury (1-5). VSMC from several species when cultured in vitro undergo a change in phenotype from a contractile state to a synthetic state similar to the changes that occur with VSMC in vivo in response to vascular injury (6 -8). Several lines of evidence suggest that nitric oxide (NO) inhibits VSMC proliferation (9 -13), suggesting that signal transduction pathways regulated by NO may be important in VSMC phenotypic modulation. NO stimulates the production of cyclic GMP (14), which, in turn, regulates several functions of VSMC such as smooth muscle relaxation (15). The major receptor protein for cGMP in VSMC is cGMP-dependent protein kinase (PKG), a serine/ threonine kinase that catalyzes the phosphorylation of important proteins that regulate intracellular Ca 2ϩ levels and relaxation of vascular smooth muscle (16). Our laboratory has recently demonstrated that PKG also plays a major role in the regulation of the phenotype and morphology of VSMC (17, 18).The expression of PKG is highly variable in VSMC. When adult rat aortic SMC are subcultured in vitro, PKG expression is reduced to nearly un...

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Cell density modulates the decrease of cytosolic free Ca2+ induced by atrial natriuretic hormone, S-nitroso-N-acetylpenicillamine and 8-bromo cyclic GMP in cultured rat mesangial cells

Cited by 17 publications

References 24 publications

Inhibition of Glucagon‐Stimulated Glycogenolysis by S‐Nitroso‐N‐acetylpenicillamine*

Inhibition of Glucagon‐Stimulated Glycogenolysis by S‐Nitroso‐N‐acetylpenicillamine*

Elevation of intracellular calcium levels contributes to the inhibition of nitric oxide production by atrial natriuretic peptide

Activation of Mitogen-activated Protein Kinase Pathways by Cyclic GMP and Cyclic GMP-dependent Protein Kinase in Contractile Vascular Smooth Muscle Cells

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