Abstract
A study involving markers of subcellular and submitochondrial fractions, gradient centrifugation, latency measurements and extraction with digitonin, demonstrates the association of a specific ADP-ribose pyrophosphatase with rat liver mitochondria and its localization in the matrix space. The enzyme hydrolyses ADP-ribose to AMP, with a Km of 2-3 microM. The results support the occurrence of a specific turnover pathway for free ADP-ribose and its relevance in mitochondria.
Full text
PDF



Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Bischoff E., Tran-Thi T. A., Decker K. F. Nucleotide pyrophosphatase of rat liver. A comparative study on the enzymes solubilized and purified from plasma membrane and endoplasmic reticulum. Eur J Biochem. 1975 Feb 21;51(2):353–361. doi: 10.1111/j.1432-1033.1975.tb03935.x. [DOI] [PubMed] [Google Scholar]
- Boyer C. S., Moore G. A., Moldéus P. Submitochondrial localization of the NAD+ glycohydrolase. Implications for the role of pyridine nucleotide hydrolysis in mitochondrial calcium fluxes. J Biol Chem. 1993 Feb 25;268(6):4016–4020. [PubMed] [Google Scholar]
- Cameselle J. C., Costas M. J., Günther Sillero M. A., Sillero A. Two low Km hydrolytic activities on dinucleoside 5',5"'-P1,P4-tetraphosphates in rat liver. Characterization as the specific dinucleoside tetraphosphatase and a phosphodiesterase I-like enzyme. J Biol Chem. 1984 Mar 10;259(5):2879–2885. [PubMed] [Google Scholar]
- Costas M. J., Cameselle J. C., Sillero A. Mitochondrial location of rat liver dinucleoside triphosphatase. J Biol Chem. 1986 Feb 15;261(5):2064–2067. [PubMed] [Google Scholar]
- Desmarais Y., Ménard L., Lagueux J., Poirier G. G. Enzymological properties of poly(ADP-ribose)polymerase: characterization of automodification sites and NADase activity. Biochim Biophys Acta. 1991 Jun 24;1078(2):179–186. doi: 10.1016/0167-4838(91)99007-f. [DOI] [PubMed] [Google Scholar]
- Fleischer S., Kervina M. Subcellular fractionation of rat liver. Methods Enzymol. 1974;31:6–41. doi: 10.1016/0076-6879(74)31005-1. [DOI] [PubMed] [Google Scholar]
- Frei B., Richter C. Mono(ADP-ribosylation) in rat liver mitochondria. Biochemistry. 1988 Jan 26;27(2):529–535. doi: 10.1021/bi00402a004. [DOI] [PubMed] [Google Scholar]
- Galione A. Ca(2+)-induced Ca2+ release and its modulation by cyclic ADP-ribose. Trends Pharmacol Sci. 1992 Aug;13(8):304–306. doi: 10.1016/0165-6147(92)90096-o. [DOI] [PubMed] [Google Scholar]
- Guida L., Zocchi E., Franco L., Benatti U., De Flora A. Presence and turnover of adenosine diphosphate ribose in human erythrocytes. Biochem Biophys Res Commun. 1992 Oct 15;188(1):402–408. doi: 10.1016/0006-291x(92)92399-i. [DOI] [PubMed] [Google Scholar]
- Hilz H., Koch R., Fanick W., Klapproth K., Adamietz P. Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides. Proc Natl Acad Sci U S A. 1984 Jul;81(13):3929–3933. doi: 10.1073/pnas.81.13.3929. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kawaichi M., Ueda K., Hayaishi O. Multiple autopoly(ADP-ribosyl)ation of rat liver poly(ADP-ribose) synthetase. Mode of modification and properties of automodified synthetase. J Biol Chem. 1981 Sep 25;256(18):9483–9489. [PubMed] [Google Scholar]
- Kim H., Jacobson E. L., Jacobson M. K. Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases. Science. 1993 Sep 3;261(5126):1330–1333. doi: 10.1126/science.8395705. [DOI] [PubMed] [Google Scholar]
- Kirsten E., Bauer P. I., Kun E. Cellular regulation of ADP-ribosylation of proteins. IV. Conversion of poly(ADP-ribose) polymerase activity to NAD-glycohydrolase during retinoic acid-induced differentiation of HL60 cells. Exp Cell Res. 1991 May;194(1):1–8. doi: 10.1016/0014-4827(91)90122-b. [DOI] [PubMed] [Google Scholar]
- Kun E., Chang A. C., Sharma M. L., Ferro A. M., Nitecki D. Covalent modification of proteins by metabolites of NAD+. Proc Natl Acad Sci U S A. 1976 Sep;73(9):3131–3135. doi: 10.1073/pnas.73.9.3131. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kun E., Zimber P. H., Chang A. C., Puschendorf B., Grunicke H. Macromolecular enzymatic product of NAD+ in liver mitochondria. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1436–1440. doi: 10.1073/pnas.72.4.1436. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lötscher H. R., Winterhalter K. H., Carafoli E., Richter C. Hydroperoxide-induced loss of pyridine nucleotides and release of calcium from rat liver mitochondria. J Biol Chem. 1980 Oct 10;255(19):9325–9330. [PubMed] [Google Scholar]
- Maruta H., Inageda K., Aoki T., Nishina H., Tanuma S. Characterization of two forms of poly(ADP-ribose) glycohydrolase in guinea pig liver. Biochemistry. 1991 Jun 18;30(24):5907–5912. doi: 10.1021/bi00238a014. [DOI] [PubMed] [Google Scholar]
- Masmoudi A., Mandel P. ADP-ribosyl transferase and NAD glycohydrolase activities in rat liver mitochondria. Biochemistry. 1987 Apr 7;26(7):1965–1969. doi: 10.1021/bi00381a027. [DOI] [PubMed] [Google Scholar]
- Matlib M. A., O'Brien P. J. Compartmentation of enzymes in the rat liver mitochondrial matrix. Arch Biochem Biophys. 1975 Mar;167(1):193–202. doi: 10.1016/0003-9861(75)90456-7. [DOI] [PubMed] [Google Scholar]
- Miró A., Costas M. J., García-Díaz M., Hernández M. T., Cameselle J. C. A specific, low Km ADP-ribose pyrophosphatase from rat liver. FEBS Lett. 1989 Feb 13;244(1):123–126. doi: 10.1016/0014-5793(89)81176-7. [DOI] [PubMed] [Google Scholar]
- Miró A., Hernández M. T., Costas M. J., Cameselle J. C. Enzyme saturation and inhibition kinetics studied from multiple progress curves recorded spectrophotometrically from single reaction mixtures for ADP-ribose pyrophosphatase. J Biochem Biophys Methods. 1991 Feb-Mar;22(2):177–184. doi: 10.1016/0165-022x(91)90031-q. [DOI] [PubMed] [Google Scholar]
- Miwa M., Sugimura T. Splitting of the ribose-ribose linkage of poly(adenosine diphosphate-robose) by a calf thymus extract. J Biol Chem. 1971 Oct 25;246(20):6362–6364. [PubMed] [Google Scholar]
- Parry D. M., Pedersen P. L. Intracellular localization and properties of particulate hexokinase in the Novikoff ascites tumor. Evidence for an outer mitochondrial membrane location. J Biol Chem. 1983 Sep 25;258(18):10904–10912. [PubMed] [Google Scholar]
- Richter C., Schlegel J., Schweizer M. Prooxidant-induced Ca2+ release from liver mitochondria. Specific versus nonspecific pathways. Ann N Y Acad Sci. 1992 Nov 21;663:262–268. doi: 10.1111/j.1749-6632.1992.tb38669.x. [DOI] [PubMed] [Google Scholar]
- Schnaitman C., Erwin V. G., Greenawalt J. W. The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol. 1967 Mar;32(3):719–735. doi: 10.1083/jcb.32.3.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tanuma S., Endo H. Identification in human erythrocytes of mono(ADP-ribosyl) protein hydrolase that cleaves a mono(ADP-ribosyl) Gi linkage. FEBS Lett. 1990 Feb 26;261(2):381–384. doi: 10.1016/0014-5793(90)80597-c. [DOI] [PubMed] [Google Scholar]
- Tanuma S., Endo H. Purification and characterization of an (ADP-ribose)n glycohydrolase from human erythrocytes. Eur J Biochem. 1990 Jul 20;191(1):57–63. doi: 10.1111/j.1432-1033.1990.tb19093.x. [DOI] [PubMed] [Google Scholar]
- Ueda K., Oka J., Naruniya S., Miyakawa N., Hayaishi O. Poly ADP-ribose glycohydrolase from rat liver nuclei, a novel enzyme degrading the polymer. Biochem Biophys Res Commun. 1972 Jan 31;46(2):516–523. doi: 10.1016/s0006-291x(72)80169-4. [DOI] [PubMed] [Google Scholar]
- Weis M., Kass G. E., Orrenius S., Moldéus P. N-acetyl-p-benzoquinone imine induces Ca2+ release from mitochondria by stimulating pyridine nucleotide hydrolysis. J Biol Chem. 1992 Jan 15;267(2):804–809. [PubMed] [Google Scholar]
