Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation.

Vedia, L Molina y; McDonald, BJ; Reep, Bryan R.; Brüne, Bernhard; Silvio, Mauricio Di; Billiar, Timothy R.; Lapetina, Eduardo G.

doi:10.1016/s0021-9258(19)73985-4

Cited by 363 publications

(29 citation statements)

References 35 publications

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“…For demonstration of S-nitrosylation, bacterially expressed CPP-32 wild-type p17 subunit (p17 wt) and Cys 163-mutated p17 subunit (p17 mt) were purified as described above and p17 subunits were renaturated by dialysis in 10 mM Tris/HCl, pH 7.5, overnight (18). Then, 0.5 mg protein was incubated in 30 mM Tris/HCl, pH 7.5, with NO released nonenzymatically by NaNO 2 or sodium nitroprusside (SNP) (19,20) for the time indicated and again was dialysed overnight. S-nitrosylation was determined spectrophotometrically at 335 nm using an extinction coefficient of 3,869 mol Ϫ 1 ϫ cm Ϫ 1 (19,20), titration of SH-groups was carried out with excess of 5,5Јdithiobis(2-nitroben-zoate) (DTNB) at 412 nm with an extinction coefficient of 13,600 mol Ϫ1 ϫ cm Ϫ1 (19).…”

Section: Methodsmentioning

confidence: 99%

Suppression of Apoptosis by Nitric Oxide via Inhibition of Interleukin-1β–converting Enzyme (ICE)-like and Cysteine Protease Protein (CPP)-32–like Proteases

Dimmeler

Haendeler

Nehls

et al. 1997

The Journal of Experimental Medicine

788

511

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Physiological levels of shear stress alter the genetic programm of cultured endothelial cells and are associated with reduced cellular turnover rates and formation of atherosclerotic lesions in vivo. To test the hypothesis that shear stress (15 dynes/cm2) interferes with programmed cell death, apoptosis was induced in human umbilical venous cells (HUVEC) by tumor necrosis factor-α (TNF-α). Apoptosis was quantified by ELISA specific for histone-associated DNA-fragments and confirmed by demonstrating the specific pattern of internucleosomal DNA-fragmentation. TNF-α (300 U/ml) mediated increase of DNA-fragmentation was completely abrogated by shear stress (446 ± 121% versus 57 ± 11%, P <0.05). This anti-apoptotic activity of shear stress decreased after pharmacological inhibition of endogenous nitric oxide (NO)-synthase by NG-monomethyl-l-arginine and was completely reproduced by exogenous NO-donors.The activation of interleukin-1β–converting enzyme (ICE)-like and cysteine protease protein (CPP)-32-like cysteine proteases was required to mediate TNF-α–induced apoptosis of HUVEC. Endothelial-derived nitric oxide (NO) as well as exogenous NO donors inhibited TNF-α–induced cysteine protease activation. Inhibition of CPP-32 enzyme activity was due to specific S-nitrosylation of Cys 163, a functionally essential amino acid conserved among ICE/CPP-32–like proteases. Thus, we propose that shear stress-mediated NO formation interferes with cell death signal transduction and may contribute to endothelial cell integrity by inhibition of apoptosis.

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Section: Methodsmentioning

confidence: 99%

Suppression of Apoptosis by Nitric Oxide via Inhibition of Interleukin-1β–converting Enzyme (ICE)-like and Cysteine Protease Protein (CPP)-32–like Proteases

Dimmeler

Haendeler

Nehls

et al. 1997

The Journal of Experimental Medicine

788

511

View full text Add to dashboard Cite

show abstract

“…NO has several cytotoxic effects, including reactions with proteins and nucleic acids. The main targets of NO in proteins are the SH group (Molina y Vedia et al, 1992) and Fe of active sites (Hibbs et al, 1988), especially Fe 2 ϩ (Kim et al, 1995) in heme. In the nucleus, NO has been shown to cause mutations of genes (Routledge et al, 1994;Juedes and Wogan, 1996), and inhibition of DNA repair enzymes (Kwon et al, 1991;Lepoivre et al, 1991), and to mediate DNA strand breaks (Nguyen et al, 1992;Fehsel et al, 1993).…”

mentioning

confidence: 99%

Arginase II Downregulates Nitric Oxide (NO) Production and Prevents NO-mediated Apoptosis in Murine Macrophage-derived RAW 264.7 Cells

Gotoh

Mori

1999

The Journal of Cell Biology

179

119

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Excess nitric oxide (NO) induces apoptosis of some cell types, including macrophages. As NO is synthesized by NO synthase (NOS) from arginine, a common substrate of arginase, these two enzymes compete for arginine. There are two known isoforms of arginase, types I and II. Using murine macrophage-like RAW 264.7 cells, we asked if the induction of arginase II would downregulate NO production and hence prevent apoptosis. When cells were exposed to lipopolysaccharide (LPS) and interferon-γ (IFN-γ), the inducible form of NOS (iNOS) was induced, production of NO was elevated, and apoptosis followed. When dexamethasone and cAMP were further added, both iNOS and arginase II were induced, NO production was much decreased, and apoptosis was prevented. When the cells were transfected with an arginase II expression plasmid and treated with LPS/IFN-γ, some cells were rescued from apoptosis. An arginase I expression plasmid was also effective. On the other hand, transfection with the arginase II plasmid did not prevent apoptosis when a NO donor SNAP or a high concentration (12 mM) of arginine was added. These results indicate that arginase II prevents NO-dependent apoptosis of RAW 264.7 cells by depleting intracellular arginine and by decreasing NO production.

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“…GAPDH can also be inactivated in cases of deep oxidation of the catalytic cysteines by ROS to sulfinic (-SO 2 ) and sulfonic acids (-SO 3 ) [28,29], S-nitrosylation by NO donors [30][31][32], and S-glutathionylation [32]. A ROS source in RBC can arise in the reaction of MG with amino acids [13,33], auto-oxidation of glucose [33], and auto-oxidation of oxyHb [34].…”

Section: Glyceraldehyde-3-phosphate Dehydrogenasementioning

confidence: 99%

“…Starting with 1968, studies into the glycated Hb accelerated dramatically. That year Samuel Rahbar reported that the proportion of the glycated Hb increased in RBCs in patients with diabetes [30,114], and in 1969 he published a detailed study of HbA1c in patients with diabetes [115]. In 1975 several reactions leading to HbA1c formation were described [116].…”

Section: Glycated Hemoglobinmentioning

confidence: 99%

Carbonyl Stress in Red Blood Cells and Hemoglobin

2021

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The paper overviews the peculiarities of carbonyl stress in nucleus-free mammal red blood cells (RBCs). Some functional features of RBCs make them exceptionally susceptible to reactive carbonyl compounds (RCC) from both blood plasma and the intracellular environment. In the first case, these compounds arise from the increased concentrations of glucose or ketone bodies in blood plasma, and in the second—from a misbalance in the glycolysis regulation. RBCs are normally exposed to RCC—methylglyoxal (MG), triglycerides—in blood plasma of diabetes patients. MG modifies lipoproteins and membrane proteins of RBCs and endothelial cells both on its own and with reactive oxygen species (ROS). Together, these phenomena may lead to arterial hypertension, atherosclerosis, hemolytic anemia, vascular occlusion, local ischemia, and hypercoagulation phenotype formation. ROS, reactive nitrogen species (RNS), and RCC might also damage hemoglobin (Hb), the most common protein in the RBC cytoplasm. It was Hb with which non-enzymatic glycation was first shown in living systems under physiological conditions. Glycated HbA1c is used as a very reliable and useful diagnostic marker. Studying the impacts of MG, ROS, and RNS on the physiological state of RBCs and Hb is of undisputed importance for basic and applied science.

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Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation.

Cited by 363 publications

References 35 publications

Suppression of Apoptosis by Nitric Oxide via Inhibition of Interleukin-1β–converting Enzyme (ICE)-like and Cysteine Protease Protein (CPP)-32–like Proteases

Suppression of Apoptosis by Nitric Oxide via Inhibition of Interleukin-1β–converting Enzyme (ICE)-like and Cysteine Protease Protein (CPP)-32–like Proteases

Arginase II Downregulates Nitric Oxide (NO) Production and Prevents NO-mediated Apoptosis in Murine Macrophage-derived RAW 264.7 Cells

Carbonyl Stress in Red Blood Cells and Hemoglobin

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