Inhibition of apoptosis: potential clinical targets

Bibliography

• KERR JF, WYLLIE AH, CURRIE AR: Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer (1972) 26:239–257.
   PubMed Web of Science ®Google Scholar
• STEWART BW: Mechanisms of apoptosis: integration of genetic, biochemical, and cellular indicators. J. Natl. Cancer Inst. (1994) 86:1286–1296.
   PubMed Web of Science ®Google Scholar
• SCHWARTZMAN RA, CIDLOWSKI JA: Apoptosis: the biochemistry and molecular biology of programmed cell death. Endocr. Rev. (1993) 14:133–151.
   PubMed Web of Science ®Google Scholar
• EARNSHAW WC: Nuclear changes in apoptosis. Curr. Opin. Cell Biol. (1995) 7:337–343.
   PubMed Web of Science ®Google Scholar
• BERGAMASCHI G, ROSTI V, DANOVA M, LUCOTTI C, CAZZOLA M: Apoptosis: biological and clinical aspects. Haematologica (1994) 79:86–93.
   PubMed Web of Science ®Google Scholar
• STEWART BW: Mechanisms of apoptosis: integration of genetic, biochemical, and cellular indicators. J. Natl. Cancer Inst. (1994) 86:1286–1296.
   PubMed Web of Science ®Google Scholar
• BRIGHT J, KHAR A: Apoptosis: programmed cell death in health and disease. Biosci. Rep. (1994) 14:67–82.
   PubMed Web of Science ®Google Scholar
• YUAN J, HORVITZ HR: The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death. Dev. Biol. (1990) 138:33–41.
   PubMed Web of Science ®Google Scholar
• •Paper on the C. elegans genes that form the basis of our understanding of the human system.
   Google Scholar
• BARINAGA M: Cell suicide: by ICE, not fire [news; comment]. Science (1994) 263:754–756.
   PubMed Web of Science ®Google Scholar
• NICHOLSON DW, THORNBERRY NA: Caspases: killer proteases. Trends. Biochem. Sci. (1997) 22:299–306.
   PubMed Web of Science ®Google Scholar
• ••Excellent current review of the caspase field.
   Google Scholar
• LIP, NIJHAWAN D, BUNDIHARDJO I, et al.: Cytochrome c and dATP-dependent formation of Apaf- 1/caspase 9 complex initiates an apoptotic protease cascade. Cell (1997) 91:479–489.
   PubMed Web of Science ®Google Scholar
• ••This paper makes a strong case for caspase 9 playing a role in connecting mitochondrialdysfunction to caspase activation.
   Google Scholar
• KRAMMER PH, BEHRMANN I, DANIEL P, DHEIN J, DEBATIN KM: Regulation of apoptosis in the immune system. Curr. Opin. Immunol. (1994) 6:279–289.
   PubMed Web of Science ®Google Scholar
• BARR PJ, TOMEI LD: Apoptosis and its role in human disease. BioTechnology (1994) 12:487–493.
   PubMed Web of Science ®Google Scholar
• KERR JF, WINTERFORD CM, HARMON BV: Apoptosis. Its significance in cancer and cancer therapy. Cancer (1994) 73:2013–2026.
   PubMed Web of Science ®Google Scholar
• THOMPSON CB: Apoptosis in the pathogenesis and treatment of disease. Science (1995) 267:1456–1462.
   PubMed Web of Science ®Google Scholar
• •Good perspective on apoptosis and disease.
   Google Scholar
• CHIARUGI V, MAGNELLI L, CINELLI M: Complex interplay among apoptosis factors: RB,p53, E2F, TGF-beta, cell cycle inhibitors and the bc1-2 gene family. Pharmacol. Res. (1997) 35:257–261.
   PubMed Web of Science ®Google Scholar
• KROEMER G: The proto-oncogene Bc1-2 and its role in regulating apoptosis. Nature Med. (1997) 3:614–620.
   PubMed Web of Science ®Google Scholar
• ANDERSON GP: Bc1-2 related proteins, apoptosis and disease. Trends Pharmacol. Sci. (1997) 18:51.
   PubMed Web of Science ®Google Scholar
• LAVIN MF, WAITERS D, SONG Q: Role of protein kinase activity in apoptosis. Experientia (1996) 52:979–994.
   PubMedGoogle Scholar
• COHEN GM: Caspases: the executioners of apoptosis. Biochem. J. (1997) 326:1–16.
   PubMed Web of Science ®Google Scholar
• NEVE RL, ROBAKIS NK: Alzheimer's disease: a re-examination of the amyloid hypothesis. Trends Neurosci. (1998) 21:15–19.
   PubMed Web of Science ®Google Scholar
• YUAN J: Transducing signals of life and death. Curr. Opin. Cell Biol. (1997) 9:247–251.
   PubMed Web of Science ®Google Scholar
• DIXIT VM: Role of ICE-proteases in apoptosis. Adv. Exp. Med. Biol. (1996) 406:113–117.
   PubMedGoogle Scholar
• SALVESEN GS, DIXIT VM: Caspases: intracellular signaling by proteolysis. Cell (1997) 91:443–446.
   PubMed Web of Science ®Google Scholar
• •Good review of caspase signalling.
   Google Scholar
• YUAN J, SHAHAM S, LEDOUX S, ELLIS HM, HORVITZ HR: The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-113-converting enzyme. Cell (1993) 75:641–652.
   PubMed Web of Science ®Google Scholar
• PARK DS, STEFANIS L, YAN CYI, FARINELLI SE, GREENE LA: Ordering the cell death pathway. Differential effects of BCL-2, an interleukin- 1-converting enzyme family protease inhibitor, and other survival agents on JNK activation in serum/nerve growth factor-deprived PC12 cells. J. Biol. Chem. (1996) 271:21898–21905.
   PubMed Web of Science ®Google Scholar
• CHINNAIYAN AM, ORTH K, O'ROURKE K, et al.: Molecular ordering of the cell death pathway. Bc1-2 and Bc1-; function upstream of the CED-3-like apoptotic proteases. J. Biol. Chem. (1996) 271:4573–4576.
   PubMed Web of Science ®Google Scholar
• VILLA P, KAUFMANN SH, EARNSHAW WC: Caspases and caspase inhibitors. Trends Biochem. Sci. (1997) 22:388–393.
   PubMed Web of Science ®Google Scholar
• KUIDA K, ZHENG TS, NA S, et al.: Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature (1996) 384:368–372.
   PubMed Web of Science ®Google Scholar
• THATTE U, DAHANUKAR S: Apoptosis: clinical relevance and pharmacological manipulation. Drugs (1997) 54:511–532.
   PubMed Web of Science ®Google Scholar
• BLANCO FJ, OCHS RL, SCHWARZ H, LOTZ M: Chondrocyte apoptosis induced by nitric oxide. Am. J. Pathol. (1995) 146:75–85.
   PubMed Web of Science ®Google Scholar
• Adolphe M (Ed.), CRC Press, Boca Raton (1992):295–319.
   Google Scholar
• MALEMUD CJ, PAPAY RS, HERING TM, et al.: Phenotypic modulation of newly synthesized proteoglycans in human cartilage and chondrocytes. Osteoarthritis Cartilage (1995) 3:227–238.
   PubMed Web of Science ®Google Scholar
• ERLACHER L, MAIER R, ULLRICH R, et al.: Differential expression of the protooncogene bc1-2 in normal and osteoarthritic human articular cartilage. J. Rheumatol. (1995) 22:926–931.
   PubMed Web of Science ®Google Scholar
• JOHNSON EM, Jr.: Possible role of neuronal apoptosis in Alzheimer's disease. Neurobiol. Aging (1994) 15 (Suppl. 2) :S187–S189.
   Google Scholar
• DRAGUNOW M, FAULL RLM, LAWLOR P, et al.: In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. Neuroreport (1995) 6:1053–1057.
   PubMed Web of Science ®Google Scholar
• COTMAN CW, ANDERSON AJ: A potential role for apoptosis in neurodegeneration and Alzheimer's disease. Mol. Neurobiol. (1995) 10:19–45.
   PubMed Web of Science ®Google Scholar
• STEFANIS L, BURKE RE, GREENE LA: Apoptosis in neurodegenerative disorders. Curr. Opin. Neurol. (1997) 10:299–305.
   PubMed Web of Science ®Google Scholar
• NI B, WU X, DU Y et al.: Cloning and expression of a rat brain interleukin- lbeta-converting enzyme (ICE)-related protease (IRP) and its possible role in apoptosis of cultured cerebellar granule neurons. J. Neurosci. (1997) 17:1561–1569.
   PubMed Web of Science ®Google Scholar
• ARMSTRONG RC, AJA TJ, HOANG KD, et al.: Activation of the CED3/ICE-related protease CPP32 in cerebellar granule neurons undergoing apoptosis but not necrosis. J. Neurosci. (1997) 17:553–562.
   PubMed Web of Science ®Google Scholar
• TROY CM, STEFANIS L, GREENE LA, SHELANSKI ML: Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) downregulation, in sympathetic neurons and PC12 cells. J. Neurosci. (1997) 17:1911–1918.
   PubMed Web of Science ®Google Scholar
• DAVIDSON FF, STELLER H: Blocking apoptosis prevents blindness in Drosophila retinal degeneration mutants. Nature (1998) 391:587–591.
   PubMed Web of Science ®Google Scholar
• ••Recent paper providing evidence that blocking apoptosis can allow recovery of function.
   Google Scholar
• ISLAM N, AFTABUDDIN M, MORIWAKI A, HORI Y: Detection of DNA damage inducedby apoptosis in the rat brain following incomplete ischemia. Neurosci. Lett. (1995) 188:159–162.
   PubMed Web of Science ®Google Scholar
• LODDICK SA, MACKENZIE A, ROTHWELL NJ: An ICE inhibitor, z-VAD-DCB attenuates ischaemic brain damage in the rat. Neuroreport (1996) 7:1465–1468.
   PubMed Web of Science ®Google Scholar
• HARA H, FRIEDLANDER RM, GAGLIARDINI V, et al.: Inhibition of interleukin lbeta converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage. Proc. Natl. Acad. Sci. USA (1997) 94:2007–2012.
   PubMed Web of Science ®Google Scholar
• YAKOVLEV AG, KNOBLACH SM, FAN L, et al.: Activation of CPP32-like caspases contributes to neuronal apoptosis and neurological dysfunction after traumatic brain injury. J. Neurosci. (1997) 17:7415–7424.
   PubMed Web of Science ®Google Scholar
• HARA H, FINK K, ENDRES M, et al.: Attenuation of transient focal cerebral ischemic injury in transgenic mice expressing a mutant ICE inhibitory protein. J. Cereb. Blood Flow Metab. (1997) 17:370–375.
   PubMed Web of Science ®Google Scholar
• FRIEDLANDER RM, GAGLIARDINI V, HARA H, et al.: Expression of a dominant negative mutant of interleukin-1 beta converting enzyme in transgenic mice prevents neuronal cell death induced by trophic factor withdrawal and ischemic brain injury. J. Exp. Med. (1997) 185:933–940.
   PubMed Web of Science ®Google Scholar
• LODDICK SA, WONG ML, BONGIORNO PB, et al.: Endogenous interleukin-1 receptor antagonist is neuroprotective. Biochem. Biophys. Res. Commun. (1997) 234:211–215.
   PubMed Web of Science ®Google Scholar
• ASAHI M, HOSHIMARU M, UEMURAY et al.: Expression of interleukin-1 beta converting enzyme gene family and bc1-2 gene family in the rat brain following permanent occlusion of the middle cerebral artery. J. Cereb. Blood Flow Metab. (1997) 17:11–18.
   PubMed Web of Science ®Google Scholar
• KRAMS SM, EGAWA H, QUINN MB, et al.: Apoptosis as a mechanism of cell death in liver allograft rejection. Transplantation (1995) 59:621–625.
   PubMed Web of Science ®Google Scholar
• HIRAMATSU N, HAYASHI N, KATAYAMA K, et al.: Immunohistochemical detection of FAS antigen in liver tissue of patients with chronic hepatitis C. Hepatology (1994) 19:1354–1359.
   PubMed Web of Science ®Google Scholar
• RAY SD, KAMENDULIS LM, GURULE MW, YORKIN RD, CORCORAN GB: Ca' antagonists inhibit DNA fragmentation and toxic cell death induced by acetaminophen. FASEB J. (1993) 7:453–463.
   PubMed Web of Science ®Google Scholar
• BARONI GS, MARUCCI L, BENEDETTI A, et al.: Chronic ethanol feeding increases apoptosis and cell proliferation in rat liver. J. Hepatol. (1994) 20:508–513.
   PubMed Web of Science ®Google Scholar
• LEIST M, GANTNER F, BOHLINGER I, et al.: Tumor necrosis factor-induced hepatocyte apoptosis precedes liver failure in experimental murine shock models. Am. J. Pathol. (1995) 146:1220–1234.
   PubMed Web of Science ®Google Scholar
• OGASAWARA J, WATANABE FUKUNAGA R, ADACHI M, et al.: Lethal effect of the anti-Fas antibody in mice. Nature (1993) 364:806–809.
   PubMed Web of Science ®Google Scholar
• RODRIGUEZ I, MATSUURA K, ODY C, NAGATA S, VASSALLI P: Systemic injection of a tripeptide inhibits the intracellular activation of CPP32-like proteases in vivo and fully protects mice against Fas-mediated fulminant liver destruction and death. J. Exp. Med. (1996) 184:2067–2072.
   PubMed Web of Science ®Google Scholar
• ROUQUET N, PAGES JC, MOLINA T, BRIAND P, JOULIN V: ICE inhibitor YVADcmk is a potent therapeutic agent against in vivo liver apoptosis. Curr. Biol. (1996) 6:1192–1195.
   PubMed Web of Science ®Google Scholar
• LACRONIQUE V, MIGNON A, FABRE M, et al.: Bc1-2 protects from lethal hepatic apoptosis induced by an anti-Fas antibody in mice. Nature Med. (1996) 2:80–86.
   PubMed Web of Science ®Google Scholar
• RODRIGUEZ I, MATSUURA K, KHATIB K, et al.: A bc1-2 transgene expressed in hepatocytes protects mice from fulminant liver destruction but not from rapid death induced by anti-Fas antibody injection. J. Exp. Med. (1996) 183:1031–1036.
   PubMed Web of Science ®Google Scholar
• KUNSTLE G, LEIST M, UHLIG S, et al.: ICE-protease inhibitors block murine liver injury and apoptosis caused by CD95 or by TNF-a. Immunol. Lett. (1997) 55:5–10.
   PubMed Web of Science ®Google Scholar