Stimulation of poly(ADP-ribose) synthesis by free radicals in C3H10T1/2 cells: relationship with NAD metabolism and DNA breakage

1990 ◽  
Vol 68 (3) ◽  
pp. 602-608 ◽  
Author(s):  
Dominique Lautier ◽  
Danièle Poirier ◽  
Annie Boudreau ◽  
Moulay A. Alaoui Jamali ◽  
André Castonguay ◽  
...  

We have studied the effect of H2O2 and O2− produced by xanthine and xanthine oxidase on NAD catabolism, poly(ADP-ribose) synthesis, and production of DNA single-strand breaks in C3H10T1/2 cells. The results show a correlation between the induction of DNA single-strand breaks, the decrease of NAD pool, and the accumulation of polymer. New techniques, based on affinity chromatography and reversed-phase high pressure liquid chromatography, have allowed an accurate determination of polymer contents and showed a 20-fold stimulation of polymer biosynthesis induced by active oxygen species. Inhibition experiments performed with 3-aminobenzamide have shown that the decrease in NAD levels after exposure of cells to active oxygen species was caused by stimulation of poly(ADP-ribosyl)ation and of another cellular process.Key words: poly(ADP-ribose), free radicals, C3H10T1/2 cells, DNA breakage, NAD catabolism.

1988 ◽  
Vol 8 (5) ◽  
pp. 485-492 ◽  
Author(s):  
Imrana Naseem ◽  
Maqbool Ahmad ◽  
S. M. Hadi

Superoxide anion (O2.-) was photogenerated upon illumination of riboflavin in fluorescent light. The rate of O2.- formation was stimulated by double stranded DNA but not by denatured DNA or RNA. Depurinated DNA, which was predominantly depleted in guanine residues, did not exhibit the stimulatory effect, indicating an interaction of riboflavin, or active oxygen species derived from it, with guanine bases. Also, the stimulation of O2.- photogeneration was not observed with ethidium bromide but was seen with proflavin-intercalated DNA. Since ethidium bromide intercalates preferentially between purines and pyrimidines, and proflavin prefers dA-dT rich sites, these results were interpreted to suggest that the interaction of riboflavin with DNA is mainly with GC or CG base pairs.


2005 ◽  
Vol 28 (6) ◽  
pp. 998-1003 ◽  
Author(s):  
Kiyomi Kikugawa ◽  
Natsuki Oikawa ◽  
Azusa Miyazawa ◽  
Ken-ichi Shindo ◽  
Tetsuta Kato

1999 ◽  
Vol 110 (3) ◽  
pp. 129-136 ◽  
Author(s):  
Flávio J.S. Dantas ◽  
Milton O. Moraes ◽  
José C.P. de Mattos ◽  
Roberto J.A.C. Bezerra ◽  
Elizeu F. Carvalho ◽  
...  

2000 ◽  
Vol 21 (7) ◽  
pp. 1329-1334
Author(s):  
Tadahide Izumi ◽  
Tapas K. Hazra ◽  
Istvan Boldogh ◽  
Alan E. Tomkinson ◽  
Min S. Park ◽  
...  

2000 ◽  
Vol 21 (7) ◽  
pp. 1329-1334 ◽  
Author(s):  
Tadahide Izumi ◽  
Tapas K. Hazra ◽  
Istvan Boldogh ◽  
Alan E. Tomkinson ◽  
Min S. Park ◽  
...  

1976 ◽  
Vol 158 (1) ◽  
pp. 109-117 ◽  
Author(s):  
A J Paine

1. The photochemical generation of excited states of oxygen in liver cell culture by the mild ilumination of culture medium containing riboflavin, results in stimulation of benzo[a]pyrene 3-mono-oxygenase, a cytochrome P-450-linked mono-oxygenase. 2. The same large increase in mono-oxygenase activity was found when medium containing riboflavin was illuminated in the absence of cells and then stored in the dark for 24h before contact with the cells. From this it may be inferred that stimulation is due to the formation of a stable inducer in the culture medium. Further experiments indicate that the stable inducer is due to the photo-oxidation of an amino acid. 3. Evidence that singlet oxygen is responsible for initiating the stimulation of the mono-oxygenase is based on the use of molecules that scavenge particular active oxygen species. Of all the scavengers tested, only those that scavenge single oxygen inhibited the stimulation. 4. A hypothesis is developed to relate the stimulation of the mono-oxygenase by singlet oxygen in cultured cells to the regulation of the cytochrome P-450 enzyme system in vivo. It is suggested that single oxygen generation within cells may be a common factor linking the many structurally diverse inducers of the enzyme system.


Sign in / Sign up

Export Citation Format

Share Document