Poly(Adenosine Diphosphate Ribose) Glycohydrolase and Poly(Adenosine Diphosphate Ribose)
نویسندگان
چکیده
Green, S. & Bodansky, 0. (1965) J. Biol. Chem. 240,25742579 Haines, M. E., Johnston, I. R., Mathias, A. P. & Ridge, D. (1969) Biochem. J . 115, 881-887 Kashnig, D. M. 19 Kasper, C. B. (1969) J. Biol. Clzem. 244, 3786-3792 Mamaril, F. P., Dobrjansky, A. & Green, S. (1970) Cancer Res. 30, 352-356 Mizuno, N. S., Stoops, C. E. & Sinha, A. A. (1971) Nature (London) New Biol. 229,22-24 Siebert, G. & Humphrey, G. B. (1965) Aduan. Eniymol. Relat. Subj. Biochem. 27, 239-288 Skidmore, J. R. & Trams, E. G . (1970) Biochint. Biophys. Acta 219, 93-103 Solao, P. B. & Shalt, S. (1971) Exp. Cell Res. 69, 295-300 Swanson, M. A. (1955) Methods Enzymol. 2, 541-542 Zatman, L. J., Kaplan, N. 0. & Colowick, S. P. (1953) J . Biol. Chetn. 200, 197-212
منابع مشابه
Mechanism of alteration of poly(adenosine diphosphate-ribose) metabolism by hyperthermia.
The effects of hyperthermia on adenine nucleotide metabolism including NAD and poly(ADP-ribose) have been studied in confluent cultures of C3H10T1/2 cells. Cells replated immediately following hyperthermic treatment showed only 9% survival relative to controls while after a 24-h recovery period at 37 degrees C survival was 87% of control. Hyperthermic treatment caused no detectable effect on to...
متن کاملStructures of the Human Poly (ADP-Ribose) Glycohydrolase Catalytic Domain Confirm Catalytic Mechanism and Explain Inhibition by ADP-HPD Derivatives
Poly(ADP-ribose) glycohydrolase (PARG) is the only enzyme known to catalyse hydrolysis of the O-glycosidic linkages of ADP-ribose polymers, thereby reversing the effects of poly(ADP-ribose) polymerases. PARG deficiency leads to cell death whilst PARG depletion causes sensitisation to certain DNA damaging agents, implicating PARG as a potential therapeutic target in several disease areas. Effort...
متن کاملEffect of hyperthermia on poly(adenosine diphosphate-ribose) glycohydrolase.
The effects of supranormal temperature on the activity of poly(ADP-ribose) glycohydrolase were studied by assaying the enzyme in cell extracts derived from cells subjected to hyperthermia and comparing with extracts that were heated in vitro. The enzyme activity was reduced by both hyperthermic treatment of cells and by heating of cell extracts; however greater reductions were observed when int...
متن کاملPreferential degradation of protein-bound (ADP-ribose)n by nuclear poly(ADP-ribose) glycohydrolase from human placenta.
Poly(ADP-ribose) glycohydrolase, extensively purified to homogeneity from nuclei of human placenta, is composed of a single polypeptide with a molecular mass of 71,000 daltons on sodium dodecyl sulfate-polyacrylamide gel. Judging from its physico-chemical and catalytic properties, the enzyme is similar to the nuclear glycohydrolase (glycohydrolase I), but not to the cytoplasmic glycohydrolase (...
متن کاملSynthesis and degradation of poly(ADP-ribose) in plants.
Poly(ADP-ribosylation) is a post-translational modification of proteins involved in a wide range of molecular and cellular processes in mammalian system. The main enzymes responsible for this modification are the poly(ADP-ribose) polymerases that catalyze the transfer of ADP-ribose moieties from NAD + to target protein acceptors, producing long and branched ADP-ribose polymers. The poly(ADP-rib...
متن کاملEffect of 1-methyl-1-nitrosourea on poly(adenosine diphosphate-ribose) polymerase activity at the nucleosomal level.
The stimulation of poly(adenosine diphosphate ribose) [poly(ADP-ribose)] polymerase activity at the nuclear level after damage of HeLa cells by 1-methyl-1-nitrosourea has been previously reported. We have observed a similar activation of the enzyme after treatment of cells with MNU at the nucleosomal level of chromatin (greater than 1N). This stimulation of enzyme activity did not occur through...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2009