Nitroprusside stimulates the cysteine‐specific mono(ADP‐ribosylation) of glyceraldehyde‐3‐phosphate dehydrogenase from human erythrocytes

Kots, Alexander Y.; Skurat, Alexander V.; Sergienko, Edward A.; Bulargina, T. V.; Severin, E. S.

doi:10.1016/0014-5793(92)80153-8

Cited by 92 publications

(60 citation statements)

References 16 publications

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“…NO has been reported to inactivate mitochondrial complexes I and IV (48) and also glyceraldehyde 3-phosphate dehydrogenase (49,50), both of which are key enzymes responsible for ATP production in the cell. NO also has been reported recently to decrease ATP content of the cells (51), and it would be interesting to investigate whether this could result in the decrease in cyclin D1 synthesis observed in our study.…”

Section: Discussionmentioning

confidence: 99%

Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1

Pervin

Singh

Chaudhuri

2001

Proc. Natl. Acad. Sci. U.S.A.

160

115

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DETA-NONOate, a nitric oxide (NO) donor, induced cytostasis in the human breast cancer cells MDA-MB-231, and the cells were arrested in the G 1 phase of the cell cycle. This cytostatic effect of the NO donor was associated with the down-regulation of cyclin D1 and hypophosphorylation of the retinoblastoma protein. No changes in the levels of cyclin E or the catalytic partners of these cyclins, CDK2, CDK4, or CDK6, were observed. This NO-induced cytostasis and decrease in cyclin D1 was reversible for up to 48 h of DETA-NONOate (1 mM) treatment. DETA-NONOate (1 mM) produced a steady-state concentration of 0.5 M of NO over a 24-h period. Synchronized population of the cells exposed to DETANONOate remained arrested at the G 1 phase of the cell cycle whereas untreated control cells progressed through the cell cycle after serum stimulation. The cells arrested at the G 1 phase after exposure to the NO donor had low cyclin D1 levels compared with the control cells. The levels of cyclin E and CDK4, however, were similar to the control cells. The decline in cyclin D1 protein preceded the decrease of its mRNA. This decline of cyclin D1 was due to a decrease in its synthesis induced by the NO donor and not due to an increase in its degradation. We conclude that down-regulation of cyclin D1 protein by DETA-NONOate played an important role in the cytostasis and arrest of these tumor cells in the G 1 phase of the cell cycle.A ctivated macrophages produce large amounts of nitric oxide (NO), which induces cytostasis and cytotoxicity to tumor cells both in vitro and in vivo (1-8). Macrophages also play a significant role in host resistance to tumors (7-9). Tumor cells cocultured with activated macrophages rapidly develop cytostasis, which precedes the cytotoxic effects (5, 10).It has been reported that NO-induced early cytostasis begins with a rapid and reversible inhibition of ribonucleotide reductase (RR) (10). However, the possibility of targets other than RR being involved in the NO-induced long-lasting cytostasis was suggested by other investigators (10). Hydroxyurea, a specific inhibitor of RR (10), decreased thymidine incorporation in cultured cells and, after its removal, the thymidine incorporation rapidly returned to control values. The rate of recovery was much faster after withdrawal of hydroxyurea when compared with the rate of recovery observed in cells that initially were exposed either to activated macrophages or to a NO donor and then kept in a NO-free environment. On this basis, it was suggested that targets other than RR may be responsible for producing long-lasting cytostasis in target cells exposed to NO (5,10,11). This long-lasting cytostasis, therefore, would be associated with metabolic alterations in target cells, producing long-lasting growth inhibition and requiring a longer time for these cells to resume their normal rate of proliferation.Because the precise mechanism(s) by which NO induces this long-lasting cytostasis is not completely known, the present work was undertaken to assess this mechanism(s)...

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Section: Discussionmentioning

confidence: 99%

Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1

Pervin

Singh

Chaudhuri

2001

Proc. Natl. Acad. Sci. U.S.A.

160

115

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“…However, in CEC from inflamed IBD mucosa, the loss of IAMlabeling capacity and inhibition of GAPDH activity did not recover despite incubation for 16 h in complete media under nonoxidative conditions (see Methods), suggesting that the occurrence of other reactions contribute to the oxidation of the reduced thiol. Direct oxidation by NO leads to the formation of irreversible oxidation conjugates that cannot be re-reduced by cytoplasmic constituents (34)(35)(36). Initially, NO reacts with the GAPDH active-site thiol to form a reversible nitrosothiol.…”

Section: Discussionmentioning

confidence: 99%

Evidence of oxidant-induced injury to epithelial cells during inflammatory bowel disease.

et al. 1996

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Evidence of in vivo oxidant-induced injury in inflammatory bowel disease (IBD) is largely indirect. Colon epithelial crypt cells (CEC) from paired specimens of histologically normal and inflamed bowel from IBD patients with active disease were examined for altered protein thiol redox status as an indicator of oxidative damage. When CEC preparations from 22 IBD patients were labeled with the reducedthiol-specific probe [14 C]-iodoacetamide (IAM), there was decreased labeling of a number of proteins indicating oxidation of thiol groups in CEC from inflamed mucosa compared to paired normal mucosa, especially the loss of thiol labeling of a 37-kD protein which was almost completely lost. The loss of reduced protein thiol status for the 37-kD band was paralleled by loss of epithelial cell glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) enzyme activity, an enzyme known to contain an essential reduced cysteine (Cys 149 ) at the active site. The identity of the 37-kD protein as GADPH monomer was confirmed by NH 2 -terminal amino acid sequence analysis.To examine whether this type of in vivo injury could be attributed to biologically relevant oxidants produced by inflammatory cells, CEC prepared from normal mucosa were exposed to H 2 O 2 , OCl

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“…Brune & Lapetina (1989) NO AND SYNAPTIC FUNCTION 161 demonstrated that sodium nitroprusside induced the ADP-ribosylation of a 39-kD protein in platelets. Later studies have identified this 39-kD protein as glyceraldehyde 3' phosphate dehydrogenase (GAPDH) , Kots et al 1992, Zhang & Snyder 1992 and have indicated that NO promotes the auto-ADP-ribosylation of GAPDH, rather than activating a distinct ADP-ribosyltransferase. NO first stimulates the S-nitrosylation of a cysteine residue adjacent to the NAD-binding site in the catalytic region of GAPDH (Molina y Vedia et al 1992).…”

Section: No Effectorsmentioning

confidence: 99%

Nitric Oxide and Synaptic Function

Schuman

Madison²

1994

Annu. Rev. Neurosci.

752

273

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Nitroprusside stimulates the cysteine‐specific mono(ADP‐ribosylation) of glyceraldehyde‐3‐phosphate dehydrogenase from human erythrocytes

Cited by 92 publications

References 16 publications

Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1

Nitric oxide-induced cytostasis and cell cycle arrest of a human breast cancer cell line (MDA-MB-231): Potential role of cyclin D1

Evidence of oxidant-induced injury to epithelial cells during inflammatory bowel disease.

Nitric Oxide and Synaptic Function

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