A purine nucleoside phosphorylase (PNP) inhibitor induces apoptosis via caspase-3-like protease activity in MOLT-4 T cells

Immunopharmacology

Volumn 37, Issue 2-3, 1997, Pages 231-244

  Posmantur, Rand ^a   Wang, Kevin K W ^a   Nath, Rathna ^a   Gilbertsen, Richard B ^a  

^a PFIZER INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; NUCLEOSIDE PHOSPHORYLASE; PURINE NUCLEOSIDE;

APOPTOSIS; ARTICLE; AUTOSOMAL RECESSIVE DISORDER; CELL DEATH; DNA SYNTHESIS INHIBITION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE; FLUOROMETRY; HUMAN; HUMAN CELL; NECROSIS; PRIORITY JOURNAL; PURINE METABOLISM; T LYMPHOCYTE ACTIVATION;

APOPTOSIS; CASPASE 3; CASPASES; CELL LINE; CELL SURVIVAL; CHROMATIN; CYSTEINE ENDOPEPTIDASES; DEOXYGUANOSINE; DNA; ENZYME INHIBITORS; GUANINE; HUMANS; L-LACTATE DEHYDROGENASE; PROTEASE INHIBITORS; PROTEINS; PURINE-NUCLEOSIDE PHOSPHORYLASE; SPECTRIN; T-LYMPHOCYTES; THYMIDINE;

EID: 0030862201     PISSN: 01623109     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0162-3109(97)00052-0     Document Type: Article

References (64)

1. Alexianu M.E., Mohammed A.H., Smith R.G., Colom L.V., Appel S.H. Apoptotic cell death of a hybrid motor neuron cell line induced by immunoglobulin from patients with amyotrophic lateral sclerosis. J. Neurochem. 63:1994;2365-2368.
2. Alnemri E.S., Livingston D.J., Nicholson D.W., Salvesen G., Thornberry N.A., Wong W.W., Yuan J. Human ICE/CED-3 protease nomenclature. Cell. 87:1996;171.
3. Arora A.S., de Groen P.C., Croall D.E., Emori Y., Gores G.J. Hepatocellular carcinoma cells resist necrosis during anoxia by preventing phospholipase-mediated calpain activation. J. Cell. Physiol. 167:1996;434-442.
4. Boehncke W.H., Gilbertsen R.B., Hemmer J., Sterry W. Evidence for a pathway independent from 2′-deoxyguanosine and reversible by IL-2 by which purine nucleoside phosphorylase inhibitors block T-cell proliferation. Scand. J. Immunol. 39:1994;327-332.
5. Carson D.A., Carrera C.J. Immunodeficiency secondary to adenosine deaminase deficiency and purine nucleoside phosphorylation deficiency (review). Semin. Hematol. 27:1990;260-269.
6. Cerretti P.G., Kozlosky C.J., Mosley B., Nelson N., Ness K.V., Greenstreet T.A., March C.J., Kronheim S.R., Druck T., Cannizzaro L.A., Huebner K., Black R.A. Molecular cloning of the interleukin-1 beta converting enzyme. Science. 256:1992;97-101.
7. Chen J., Zhu R.L., Nakayama M., Kawaguchi K., Jin K., Stetler R.A., Simon R.P., Graham S.H. Expression of the apoptosis-effector gene, Bax, is up-regulated in vulnerable hippocampal CA1 neurons following global ischemia. J. Neurochem. 67:1996;64-71.
8. Chow S.C., Weis M., Kass G.E., Holmstrom T.H., Eriksson J.E., Orrenius S. Involvement of multiple proteases during fas-mediated apoptosis in T-lymphocytes. FEBS Lett. 364:1995;134-138.
9. Darmon A.J., Ehrman N., Caputo A., Fujinaga J., Bleackley R.C. The cytotoxic T cell proteinase granzyme B does not activate interleukin-1-beta-converting enzyme. J. Biol. Chem. 269:1994;32043-32050.
10. Datta R., Banach D., Kojima H., Talanian R.V., Alnemri E.S., Wong W.W., Kufe D.W. Activation of the CPP32 protease in apoptosis induced by 1-beta-D-arabinofuranosylcytosine. Blood. 88:1996;1936-1943.
11. 1 aspartate-based peptide α-((2,6-dichlorobenzoyl)oxy)methyl keytones as potent time dependent inhibitors of interleukin-1β-converting enzyme. J. Med. Chem. 37:1994;563-564.
12. Edelstein C.L., Ling H., Schrier R.W. The nature of renal cell injury. Kidney Int. 51:1997;1341-1351.
13. Falcieri E., Martelli A.M., Bareggi R., Cataldi A., Cocco L. The protein kinase inhibitor staurosporine induces morphological changes typical of apoptosis in MOLT-4 cells without concomitant DNA fragmentation. Biochem. Biophys. Res. Commun. 193:1993;19-25.
14. Gavrieli Y., Sherman Y., Ben-Sasson S. Identification of programmed cell death. Early synthesis and DNA degradation. J. Biol. Cell. 119:1992;493-501.
15. Fraser A., Evan G. A licence to kill. Cell. 85:1996;781-784.
16. Gilbertsen, R.B., Sircar, S., 1991. Enzyme cascades: Purine metabolism and immunosuppression. In: Hansch, C., Sammes, P.G., Taylor, J.B. (Eds.), Comprehensive Medicinal Chemistry, vol. 2. Pergamon Press, Oxford, pp. 443-480.
17. Gilbertsen R.B., Dong M.K., Kossarek L.M., Sircar J.C., Kostlan C.R., Conroy M.C. Selective in vitro inhibition of human MOLT-4 T lymphoblast by novel purine nucleoside phosphorylase inhibitor, CI-972. Biochem. Biophys. Res. Commun. 178:1991;1351-1358.
18. Gilbertsen R.B., Josyula U., Sircar J.C., Dong M.K., Wu W.S., Wilburn D.J., Conroy M.C. Comparative in vitro and in vivo activities of two 9-deazaguanine analog inhibitors of purine nucleoside phosphorylase, CI-972 and PD 141955. Biochem. Pharmacol. 44:1992;996-999.
19. Gilbertsen R.B., Dong M.K., Josyula U., Sircar J.C., Wilburn D.J., Conroy M.C. Activities of two 9-deazaguanine analogue inhibitors of purine nucleoside phosphorylase, CI-972 and PD 141955, in vitro and in vivo. Ann. NY Acad. Sci. 685:1993;248-251.
20. Gschwind M., Martin J.R., Moreau J.L., Huber G. beta APP cognitive function versus beta-amyloid induced cell death. Ann. NY Acad. Sci. 777:1996;293-296.
21. Jagadeesh G., Shailaja B., Moses L., Kumari C.K., Anjaneyulu A., Anandaraj M.P. Important of monitoring calcium and calcium related properties in carrier detection for Duchenne muscular dystrophy. Indian J. Med. 99:1994;283-288.
22. Jenne D.E., Tschopp J. Granzymes: A family of serine proteases in granules of cytolytic T Lymphocytes. Curr. Top. Microbiol. Immunol. 140:1988;33-34.
23. Kappler J.W., Roehm N., Marrack P. T-cell tolerance by clonal elimination in the thymus. Cell. 49:1987;273.
24. Kazmers I.S., Mitchell B.S., Dadonna P.E., Wotring L.L., Townsend L.B., Kelley W.N. Inhibition of purine nucleoside phosphorylase by 8-aminoguanosine: Selective toxicity of T-lymphoblast. Science. 214:1981;1137-1139.
25. 2+-dependent neutral protease, in the destructive thrombocytopenia of the Wiskott-Aldrich syndrome. Br. J. Haematol. 87:1994;773-781.
26. Kerr, J.F.R., Harmon, B.V., 1991. Definition and incidence of apoptosis: An historical perspective. In: Tomei, L.D., Cope, F.O. (Eds.), Apoptosis: The Molecular Basis of Cell Death. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, p. 5.
27. Kredich, N.M., Hershfield, M.S. 1989. Immunodeficiency disease caused by adenosine deaminase deficiency and purine nucleoside phosphorylase deficiency. In: Stanbury, J.A. (Ed.), The Metabolic Basis of Inherited Disease. McGraw-Hill Information Services, New York, 6th ed., pp. 1045-1075.
28. Lazebnik Y.A., Kaufman S.H., Desnoyers S., Poirier G.G., Earnshaw W.C. Cleavage of poly (ADP-ribose) polymerase by a proteinase with properties like ICE. Nature. 371:1994;346-347.
29. Linnik M.D., Zobrist R.H., Hatfield M.D. Evidence supporting a role for programmed cell death in focal cerebral ischemia in rats. Stroke. 24:1993;2002-2008.
30. Martin D.W., Gelfand E.W. Biochemistry of diseases of immunodevelopment. Annu. Rev. Biochem. 50:1981;845-877.
31. Martin S.J., O'Brien G.A., Nishioka W.K., McGahon A.J., Mahboubia T., Saido T.C., Green D. Proteolysis of fodrin during apoptosis. J. Biol. Chem. 270:1995;6425-6428.
32. Marx J. Mutant enzyme provides new insights into the cause of ALS. Science. 5248:1996;446-447.
33. Merken M., Grynspan F., Nixon R.A. Differential sensitivity to proteolysis by brain calpain of adult human tau and PHF-tau. FEBS Lett. 368:1995;10-14.
34. Muzio, M., Salvesen, G.S., Dixit, V.M., 1997. FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J. Biol. Chem. 272, 2952-2956.
35. Nath R., Raser K.J., Stafford D., Hajimohammadreza I., Posner A., Allen H., Talanian R., Yuen P.Y., Gilbertsen R.B., Wang K.W. Non-erythoid α-spectrin breakdown by calpain and interleukin 1B-converting enzyme like proteases in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis. Biochem. J. 319:1996;683-690.
36. Nath R., Raser K.J., McGinnis K., Nadimpalli R., Stafford D., Wang K.K. Effects of ICE-like protease and calpain inhibitors on neuronal apoptosis. Neuroreport. 8:1996;249-255.
37. Nicholson D.W., Ambereen A.N., Thornberry N.A., Vallancourt J.P.et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature. 376:1995;37-43.
38. Nixon R.A., Saito K.I., Grynspan F., Griffin W.R., Katayama S., Honda T., Mohan P.S., Shea T.B., Beermann M. Calpain activated neutral protease (calpain) system in aging and Alzheimer's disease. Ann. NY Acad. Sci. 747:1994;77-91.
39. Orth K., O'Rourke K., Salvesen G.S., Dixit V.M. Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases. J. Biol. Chem. 271:1996;20977-20980.
40. Parks, E., Stoeckler, J.D., Cambor, C., Savarese, T.M., Crabtree, G.W., Chu, S.H., 1981. Purine nucleoside phosphorylase and 5′ methyladenosine phosphorylase: Targets of chemotherapy. In: Sartorelli, A., Lazo, J.S., Bertini, J.R. (Eds.), Molecular actions and targets for cancer chemotherapeutic agent. Academic Press, New York, pp. 229-252.
41. Posmantur R., Kampfl A., Siman R., liu S.J., Zhao X., Clifton G.L., Hayes R.L. A calpain inhibitor attenuates cortical cytoskeletal protein loss after experimental traumatic brain injury in the rat. Neuroscience. 77:1997;875-888.
42. Roberts-Lewis J.M., Savage M.J., Marcy V.R., Pinsker L.R., Siman R. Immunolocalization of calpain 1 mediated spectrin degradation to vulnerable neurons in ischemic gerbil brain. J. Neurosci. 14:1994;3934-3944.
43. Salvesen G.S., Dixit V.M. Yama/CPP32, a mammalian homolog of CED-3, is a CrmA-inhabitable protease that cleaves the death substrate poly (ADP-ribose) polymerase. Cell. 81:1995;801-809.
44. Satou T., Cummings B.J., Cotman C.W. Immunoreactivity for BCl-2 protein with neurons in the Alzheimer's disease brain increases with disease severity. Brain. Res. 697:1995;35-43.
45. Schlegel J., Peters I., Orrenius S., Miller D., Thornberry N.A., Yamin T.T., Nicholson D.W. CPP32/Apopain is a key interleukin-1 beta converting enzyme-like protease involved in fas-mediated apoptosis. J. Biol. Chem. 271:1996;1841-1844.
46. Seiffert D. Hydrolysis of platelet vitronectin by calpain. J. Biol. Chem. 271:1996;11170-11176.
47. Sidi Y., Mitchell B.S. 2′-deoxyguanosine toxicity for B and mature T lymphoid cell lines is mediated by guanine ribonucleotide accumulation. J. Clin. Invest. 74:1984;1640-1648.
48. Sircar J.C., Gilbertsen R.B. Purine nucleoside phosphorylase (PNP) inhibitors: Potentially selective immunosuppressive agents. Drugs Future. 13:1988;653-668.
49. Spencer M.J., Croall D.E., Tidball J.G. Calpains are activated in necrotic fibers from mdx dystrophic mice. J. Biol. Chem. 279:1995;10909-10914.
50. Squier K.T., Cohen J.J. Calpain, an upstream regulator of thymocyte apoptosis. J. Immunol. 158:1997;3690-3697.
51. Stoeckler J.D., Cambir C., Kuhns V., Chu S.H., Parks R.E. Inhibitors of purine nucleoside phosphorylase C(8) and C(5) substitutions. Biochem. Pharmacol. 31:1982;163-171.
52. Talanian, R.V., Quinlan, C., Trautz, S., Hackett, M.C., Mankovich, J.A., Banach, D., Ghayur, T., Brady, K.D., Wong, W.W., 1997. Substrate specificities of caspase family proteases. J. Biol. Chem. 272, 9677-9682.
53. Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Bedler D.R., Poirier S.S., Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456.
54. Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456.
55. Thornberry N.A., Herbert G.B., Calaycay J.R., Chapman K.T., Howard A.D., Kostura M.J., Miller D.K., Molineaux S.M., Weidner J.R., Aunins J.et al. A novel heterodimeric cysteine protease is required for interleukin-1B processing in monocytes. Nature. 356:1992;768-774.
56. Troost D., Aten J., Morsink F., de-long J.M. Apoptosis in ALS is not restricted to motor neurons: Bcl-2 expression increased in post-central cortex, adjacent to the affected motor cortex. J. Neurol. Sci. 129:1995;79-80.
57. Vanags D.M., Porn-Ares M.I., Coppola S., Burgess D.H., Orrenius S. Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis. J. Biol. Chem. 271:1996;31075-31081.
58. Vaux D.L., Strasser A. The molecular biology of apoptosis. Proc. Natl. Acad. Sci. USA. 93:1996;2239-2244.
59. 2+ binding protein ALG-2 and Alzheimer's disease gene ALG-3. Science. 271(5248):1996;521-525.
60. von Boehmer H. Positive selection of lymphocytes. Cell. 76:1994;219.
61. Wang K.K.W., Yuen P.W. Calpain inhibition: An overview of its therapeutic potential. Trends Pharmacol. Sci. 15:1994;412-419.
62. Wang K.K.W., Nath R., Posner A., Raser K.et al. An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective. Proc. Natl. Acad. Sci. USA. 93:1996;6686-6692.
63. Yamatsuji T., Matsui T., Okamoto T., Komatsuzaki K.et al. G-protein-mediated neuronal DNA fragmentation induced by familial Alzheimer's disease-associated mutants of APP. Science. 272:1996;1349-1352.
64. Yuen P., Wang K.W. Therapeutic potential of calpain inhibitors in neurodegenerative disorders. Exp. Opin. Invest. Drug. 5(10):1996;1-14.