Regulation of human neutrophil guanylate cyclase by metal ions, free radicals and the muscarinic cholinergic receptor

Lad, Pramod M.; Glovsky, M. Michael; Richards, John H.; Smiley, Paula A.; Backstrom, B.

doi:10.1016/0161-5890(85)90138-5

Cited by 21 publications

(4 citation statements)

References 17 publications

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“…MPP + itself has been shown to increase free radicals, as well as to disrupt calcium homeostasis (Gerlach et al, 1991;Chiueh et al, 1994;Packer et al, 1996). Furthermore, carbachol increases reactive oxygen species production (unpublished data; Lad et al, 1985;Arroyo et al, 1990;Arroyo and Forray, 1991). Therefore, deficiencies in mitochondrial calcium sequestration and regulation could have profound effects on cellular ability to respond to physiologic stimuli.…”

Section: Physiological and Clinical Significancementioning

confidence: 99%

Altered Calcium Homeostasis in Cells Transformed by Mitochondria from Individuals with Parkinson's Disease

Sheehan

Swerdlow

Parker

et al. 1997

Journal of Neurochemistry

148

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Parkinson's disease may be linked to defects in mitochondrial function. Mitochondrially transformed cells (cybrids) were created from Parkinson's disease patients or disease-free controls. Parkinson's disease cybrids had 26% less complex I activity, but maintained comparable basal calcium and energy levels. Parkinson's disease cybrids recovered from a carbachol-induced increase in cytosolic calcium 53% more slowly than controls even with lanthanum and thapsigargin blockade. Inhibition of complex I with the Parkinson's disease-inducing metabolite 1 -methyl-4-phenylpyridinium (MPP~)similarly reduced the rate of recovery after carbachol. This MPP~-induced reduction in recovery rates was much more pronounced in control cybrids than in Parkinson's disease cybrids. Parkinson's disease cybrids had less carbonyl cyanide m-chlorophenylhydrazone-releasable calcium. Bypassing complex I with succinate partially restored Parkinson's disease cybrid, and MPP~suppressed control cybrid recovery rates. The subtle alteration in calcium homeostasis of Parkinson's disease cybrids may reflect an increased susceptibility to cell death under circumstances not ordinarily toxic. Key Words: Parkinson's disease-Mitochondria-Calcium.

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Section: Physiological and Clinical Significancementioning

confidence: 99%

Altered Calcium Homeostasis in Cells Transformed by Mitochondria from Individuals with Parkinson's Disease

Sheehan

Swerdlow

Parker

et al. 1997

Journal of Neurochemistry

148

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“…Pyruvate kinase [30] (PK), also known as adenosine triphosphate pyruvate 2-O phosphotransferase, is one of the three rate-limiting enzymes that regulate glycolysis. While metal ions such as K, Na, Mg, Cu, Zn, and Fe can act as agonists of the enzyme [31][32][33], Nowak et al [34] showed that potassium ion is an agonist of pyruvate kinase, which increases pyruvate kinase activity, accelerates the production of pyruvate, and then quickly converts it into L-valine. In thiamine metabolism, tyrosine produced through tyrosine metabolism and pyruvate produced through glycolysis are used to produce aminoacetic acid and, finally, thiamine.…”

Section: Combined Analysis Of Differential Metabolites and Differenti...mentioning

confidence: 99%

Serum Metabolomics and Ionomics Analysis of Hoof-Deformed Cows Based on LC-MS/MS and ICP-OES/MS

Deng

Yue

Zhang

et al. 2023

Animals

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In order to explore the metabolic and ionic changes of hoof-deformed cows, the serum samples of 10 healthy cows (group C) and 10 hoof-deformed cows (group T) were analyzed by LC-MS/MS and ICP-OES/MS. The pathway enrichment of differential metabolites was analyzed by screening and identifying differential metabolites and ions and using a bioinformatics method. The integration of metabolomics and ionics was analyzed with ggplot2 software in R language, and verified by MRM target metabolomics. The results showed that 127 metabolites were screened by metabolomics, of which 81 were up-regulated (p < 0.05) and 46 were down-regulated (p < 0.05). The results of ICP-OES/MS showed that 13 kinds of ions such as K, Li, and Pb in serum of dairy cows were up-regulated, while 18 kinds of ions such as Al, Cu and Sb were down-regulated. The integrated analysis of metabolomics and ionics found that potassium ions were positively correlated with L-tyrosine, L-proline, thiamine and L-valine. Sodium ions were positively correlated with L-valine and negatively correlated with α-D-glucose. The results of high-throughput target metabolomics showed that the contents of L-proline, L-phenylalanine and L-tryptophan in serum of dairy cows increased significantly, which was consistent with the results of non-target metabolomics. In a word, the metabolism and ion changes in dairy cows with hoof deformation were revealed by metabolomics and ionics.

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“…All data are expressed as mean Ϯ S.E.M. Downloaded from (Lad et al, 1985;Pryzwansky et al, 1990). However, whether YC-1 can activate sGC in human neutrophils is still unknown.…”

Section: Role Of Camp/pka In Yc-1-induced Inhibition Of Omentioning

confidence: 99%

“…The clinical potential of cAMP-elevating agents as inhibitors of neutrophil activities is supported by the suppression of endotoxin-induced acute lung injury in mice by the PDE4 inhibitor rolipram (Miotla et al, 1998), and the anti-inflammatory activity of the second-generation PDE4 inhibitor Ariflo (SB 207499), in experimental asthma in guinea pigs (Underwood et al, 1998). Neutrophils have been reported to contain sGC and PKG (Lad et al, 1985;Pryzwansky et al, 1990). Despite this fact, the physiological role of cGMP in regulating neutrophil function remains poorly understood.…”

mentioning

confidence: 99%

Soluble Guanylyl Cyclase Activator YC-1 Inhibits Human Neutrophil Functions through a cGMP-Independent but cAMP-Dependent Pathway

Hwang

Hung²,

Kao³

et al. 2003

Mol Pharmacol

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3-(5Ј-Hydroxymethyl-2Ј-furyl)-1-benzyl indazole (YC-1), a novel type of soluble guanylyl cyclase (sGC) activator, is useful in investigating the signaling of cGMP and may provide a new approach for treating cardiovascular diseases. Herein, YC-1 was demonstrated to inhibit the generation of superoxide anion (O 2 . ) and the release of ␤-glucuronidase release, to diminish the membrane-associated p47 phox and to accelerate resequestration of cytosolic calcium in formyl-L-methionyl-L-leucyl-L-phenylalanine-activated human neutrophils. YC-1 not only directly promoted sGC activity and cGMP formation but also dramatically potentiated sodium nitroprusside-induced sGC activity and cGMP formation in human neutrophils. However, the synergistic increase in the amount of cGMP was inconsistent with its cellular response. Moreover, neither an sGC inhibitor nor protein kinase G inhibitors reversed the inhibitory effect of YC-1. Interestingly, YC-1 also increased the cAMP concentration and protein kinase (PK)A activity. The inhibitory effect of YC-1 was significantly enhanced by prostaglandin (PG)E 1 and isoproterenol, and almost abolished by PKA inhibitors. These results show that cAMP, but not cGMP, mediates the YC-1-induced inhibition of human neutrophils. YC-1 increased the PGE 1 -and forskolin-induced but not 3-isobutyl-1-methylxanthine-produced cAMP formation, suggesting inhibition of phosphodiesterase. These findings thus reveal novel mechanismmediated anti-inflammatory properties of YC-1 in human neutrophils, which can influence the progression of cardiovascular disease. cAMP, but not cGMP, plays an important role in the regulation of respiratory burst and degranulation in human neutrophils.

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Regulation of human neutrophil guanylate cyclase by metal ions, free radicals and the muscarinic cholinergic receptor

Cited by 21 publications

References 17 publications

Altered Calcium Homeostasis in Cells Transformed by Mitochondria from Individuals with Parkinson's Disease

Altered Calcium Homeostasis in Cells Transformed by Mitochondria from Individuals with Parkinson's Disease

Serum Metabolomics and Ionomics Analysis of Hoof-Deformed Cows Based on LC-MS/MS and ICP-OES/MS

Soluble Guanylyl Cyclase Activator YC-1 Inhibits Human Neutrophil Functions through a cGMP-Independent but cAMP-Dependent Pathway

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