Inhibition of poly(ADP-ribose) polymerase rescues human T lymphocytes from methylmercury-induced apoptosis

Toxicology and Applied Pharmacology

Volumn 152, Issue 2, 1998, Pages 397-405

  Guo, Tai Liang ^a   Miller, Mark A ^a   Datar, Sugandha ^a   Shapiro, Irving M ^a   Shenker, Bruce J ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

3 AMINOBENZAMIDE; FLAVOPROTEIN; METHYLMERCURY; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PYRIDINE NUCLEOTIDE; REACTIVE OXYGEN METABOLITE;

APOPTOSIS; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; HUMAN; HUMAN CELL; MEMBRANE POTENTIAL; MERCURIALISM; MITOCHONDRIAL MEMBRANE; MONONUCLEAR CELL; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; T LYMPHOCYTE;

EID: 0032191357     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1006/taap.1998.8526     Document Type: Article

References (45)

1. Althaus F. R., Richter C. ADP-ribosylation of proteins. Enzymology and biological significance. Mol. Biol. Biochem. Biophys. 37:1987;1-237.
2. An S., Knox K. A. Ligation of CD40 rescues Ramos-Burkitt lymphoma B cells from calcium ionophore- and antigen receptor-triggered apoptosis by inhibiting activation of the cysteine protease CPP32/Yama and cleavage of its substrate PARP. FEBS Lett. 386:1996;115-122.
3. Ashour H., Abdel-Rahman M., Khodair A. The mechanism of methyl mercury toxicity in isolated rat hepatocytes. Toxicol. Lett. 69:1993;87-96.
4. Atchison W. D., Hare M. F. Mechanisms of methylmercury-induced neurotoxicity. FASEB J. 8:1994;622-629.
5. Castedo M., Macho A., Zamzami N., Hirsch T., Marchetti P., Uriel J., Kroemer G. in vivo. Eur. J. Immunol. 25:1995;3277-3284.
6. Chance B., Schoener B., Oshino R., Itshak F., Nakase Y. Oxidation-reduction ratio studies of mitochondria in freeze-trapped samples. NADH and flavoprotein fluorescence signals. J. Biol. Chem. 254:1979;4764-4771.
7. Clarkson T. W. The toxicology of mercury. Crit. Rev. Clin. Lab. Sci. 34:1997;369-403.
8. Contrino J., Marucha P., Ribaudo R., Ference R., Bigazzi P. E., Kreutzer D. L. Effects of mercury on human polymorphonuclear leukocyte function in vitro. Am. J. Pathol. 132:1988;110-118.
9. 22. Exp. Cell Res. 221:1995;462-469.
10. De Flora S., Bennicelli C., Bagnasco M. Genotoxicity of mercury compounds. A review. Mutat. Res. 317:1994;57-79.
11. De Murcia G., de Murcia J. M. Poly(ADP-ribose) polymerase: A molecular nick-sensor. Trends Biochem. Sci. 19:1994;172-176.
12. i. J. Physiol. 450:1992;33-61.
13. Ellis R. E., Yuan J. Y., Horvitz H. R. Mechanisms and functions of cell death. Annu. Rev. Cell Biol. 7:1991;663-698.
14. Eng J., Lynch R. M., Balaban R. S. Nicotinamide adenine dinucleotide fluorescence spectroscopy and imaging of isolated cardiac myocytes. Biophys. J. 55:1989;621-630.
15. Fearnhead H. O., Dinsdale D., Cohen G. M. An interleukin-1 beta-converting enzyme-like protease is a common mediator of apoptosis in thymocytes. FEBS Lett. 375:1995;283-288.
16. Fowler B. A. The nephropathology of metals. Toxicology of Metal. 1996;CRC Press, Boca Raton. p. 721-729.
17. Franceschi C. Cell proliferation, cell death and aging. Aging. 1:1989;3-15.
18. Franchi E., Loprieno G., Ballardin M., Petrozzi L., Migliore L. Cytogenetic monitoring of fishermen with environmental mercury exposure. Mutat. Res. 320:1994;23-29.
19. Gold R., Schmied M., Giegerich G., Breitschopf H., Hartung H. P., Toyka K. V., Lassmann H. Differentiation between cellular apoptosis and necrosis by the combined use ofin situ. Lab. Invest. 71:1994;219-225.
20. Gorczyca W., Bigman K., Mittelman A., Ahmed T., Gong J., Melamed M. R., Darzynkiewicz Z. Induction of DNA strand breaks associated with apoptosis during treatment of leukemias. Leukemia. 7:1993;659-670.
21. Gu Y., Sarnecki C., Aldape R. A., Livingston D. J., Su M. S. Cleavage of poly(ADP-ribose) polymerase by interleukin-1 beta converting enzyme and its homologs TX and Nedd-2. J. Biol. Chem. 270:1995;18715-18718.
22. Harada M. Minamata disease: Methylmercury poisoning in Japan caused by environmental pollution. Crit. Rev. Toxicol. 25:1995;1-24.
23. Kaufmann S. H., Desnoyers S., Ottaviano Y., Davidson N. E., Poirier G. G. Specific proteolytic cleavage of poly(ADP-ribose) polymerase: An early marker of chemotherapy-induced apoptosis. Cancer Res. 53:1993;3976-3985.
24. Koropatnick J., Zalups R. K. Effect of non-toxic mercury, zinc or cadmium pretreatment on the capacity of human monocytes to undergo lipopolysaccharide-induced activation. Br. J. Pharmacol. 120:1997;797-806.
25. Kunz D., Luley C., Winkler K., Lins H., Kunz W. S. Flow cytometric detection of mitochondrial dysfunction in subpopulations of human mononuclear cells. Anal. Biochem. 246:1997;218-224.
26. Langworth S., Elinder C. G., Sundqvist K. G. Minor effects of low exposure to inorganic mercury on the human immune system. Scand. J. Work Environ. Health. 19:1993;405-413.
27. Malamud D., Dietrich S. A., Shapiro I. M. Low levels of mercury inhibit the respiratory burst in human polymorphonuclear leukocytes. Biochem. Biophys. Res. Commun. 128:1985;1145-1151.
28. McGowan A. J., Fernandes R. S., Samali A., Cotter T. G. Anti-oxidants and apoptosis. Biochem. Soc. Trans. 24:1996;229-233.
29. Nosseri C., Coppola S., Ghibelli L. Possible involvement of poly(ADP-ribosyl) polymerase in triggering stress-induced apoptosis. Exp. Cell Res. 212:1994;367-373.
30. O I., Shenker B. J., Shapiro I. M. Mercuric compounds inhibit human monocytes function by inducing apoptosis: Evidence for formation of reactive oxygen species, development of mitochondrial permeability transition and loss of reductive reserve. Toxicology. 124:1997;211-224.
31. Pollard K. M., Hultman P. Effects of mercury on the immune system. Metal Ions Biol. Syst. 34:1997;421-440.
32. Schmid I., Uittenbogaart C. H., Giorgi J. V. Sensitive method for measuring apoptosis and cell surface phenotype in human thymocytes by flow cytometry. Cytometry. 15:1994;12-20.
33. Schraufstatter I. U., Hinshaw D. B., Hyslop P. A., Spragg R. G., Cochrane C. G. Oxidant injury of cells. DNA strand-breaks activate polyadenosine diphosphate-ribose polymerase and lead to depletion of nicotinamide adenine dinucleotide. J. Clin. Invest. 77:1986;1312-1320.
34. Shah G. M., Kaufmann S. H., Poirier G. G. Detection of poly(ADP-ribose) polymerase and its apoptosis-specific fragment by a nonisotopic activity-Western blot technique. Anal. Biochem. 232:1995;251-254.
35. Shenker B. J., Berthold P., Decker S., Mayro J., Rooney C., Vitale L., Shapiro I. M. Immunotoxic effects of mercuric compounds on human lymphocytes and monocytes. II. Alterations in cell viability. Immunopharmacol. Immunotoxicol. 14:1992;555-577.
36. Shenker B. J., Datar S., Mansfield K., Shapiro I. M. Induction of apoptosis in human T-cells by organomercuric compounds: A flow cytometric analysis. Toxicol. Appl. Pharmacol. 143:1997;397-406.
37. Shenker B. J., Guo T. L., Shapiro I. M. Low level mercury exposure causes human T-cells to undergo apoptosis: Evidence of mitochondrial dysfunction. Environ. Res. 77:1998;149-159.
38. Shenker B. J., Vitale L., King C. Induction of human T cells that coexpress CD4 and CD8 by an immunomodulatory protein produced byActinobacillus. Cell. Immunol. 164:1995;36-46.
39. Steffensen I. L., Mesna O. J., Andruchow E., Namork E., Hylland K., Andersen R. A. Cytotoxicity and accumulation of Hg, Ag, Cd, Cu, Pb and Zn in human peripheral T and B lymphocytes and monocytesin vitro. Gen. Pharmacol. 25:1994;1621-1633.
40. Szabó C., Saunders C., O'Connor M., Salzman A. L. Peroxynitrite causes energy depletion and increases permeability via activation of poly (ADP-ribose) synthetase in pulmonary epithelial cells. Am. J. Resp. Cell Mol. Biol. 16:1997;105-109.
41. Tanaka Y., Yoshihara K., Tohno Y., Kojima K., Kameoka M., Kamiya T. Inhibition and down-regulation of poly(ADP-ribose) polymerase results in a marked resistance of HL-60 cells to various apoptosis-inducers. Cell. Mol. Biol. 41:1995;771-781.
42. Tewari M., Quan L. T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D. R., Poirier G. G., Salvesen G. S., Dixit V. M. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
43. Thiemermann C., Bowes J., Myint F. P., Vane J. R. Inhibition of the activity of poly(ADP ribose) synthetase reduces ischemia-reperfusion injury in the heart and skeletal muscle. Proc. Natl. Acad. Sci. USA. 94:1997;679-683.
44. Wyllie A. H., Kerr J. F., Currie A. R. Cell death: The significance of apoptosis. Int. Rev. Cytol. 68:1980;251-306.
45. Zamzami N., Hirsch T., Dallaporta B., Petit P. X., Kroemer G. Mitochondrial implication in accidental and programmed cell death: Apoptosis and necrosis. J. Bioenerg. Biomembr. 29:1997;185-193.