Differential toxicity of protease inhibitors in cultures of cerebellar granule neurons

Experimental Neurology

Volumn 153, Issue 2, 1998, Pages 335-341

  Monti, Barbara ^a   Sparapani, Mauro ^a   Contestabile, Antonio ^a  

^a UNIVERSITY OF BOLOGNA   (Italy)

Author keywords

Apoptosis; Calpains; Caspases; Cerebellar granule neurons; In vitro cultures; Leupeptin; Protease inhibitors

Indexed keywords

CALPAIN; PROTEINASE INHIBITOR;

ANIMAL CELL; APOPTOSIS; ARTICLE; BRAIN DEVELOPMENT; CALCIUM CELL LEVEL; CELL CULTURE; CELL DEATH; CELL STIMULATION; ENZYME INHIBITION; GRANULE CELL; NEUROBLASTOMA CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN SYNTHESIS REGULATION; PROTEINASE INHIBITION; RAT; TOXICITY TESTING;

EID: 0032192009     PISSN: 00144886     EISSN: None     Source Type: Journal    
DOI: 10.1006/exnr.1998.6858     Document Type: Article

References (33)

1. Bartus R. T., Elliot P. J., Hayward N. J., Dean R. L., Harbeson S., Straub J. A., Li Z., Powers J. C. Calpain as a novel target for treating acute neurodegenerative disorders. Neurol. Res. 17:1995;249-258.
2. Cataldo A. M., Nixon R. A. Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc. Natl. Acad. Sci. USA. 87:1990;3861-3865.
3. Contestabile A., Virgili M., Ciani E., Facchinetti F. Intrastriatal leupeptin, but not calpain inhibitor I results in neurodegeneration. Neurodegeneration. 3:1994;91-93.
4. Du Y., Dodel R. C., Bales K. R., Jemmerson R., Hamilton-Byrd E., Paul S. M. Involvement of a caspase-3-like cysteine protease in 1-methyl-4-phenylpyridinium-mediated apoptosis of cultured cerebellar granule neurons. J. Neurochem. 69:1997;1382-1388.
5. Eldadah B. A., YaKovlev A. G., Faden A. I. The role of CED-3-related cysteine proteases in apoptosis of cerebellar granule cells. J. Neurosci. 17:1997;6105-6113.
6. Faddis B. F., Hasbani M. J., Goldberg M. P. Calpain activation contributes to dendritic remodeling after brief axcitotoxic injuryin vitro. J. Neurosci. 17:1997;951-959.
7. Gallo V., Kingsbury A., Balazs R., Jorgensen O. S. The role of depolarization in the survival and differentiation of cerebellar granule cells in culture. J. Neurosci. 7:1987;2203-2213.
8. Gavrieli Y., Sherman Y., Ben-Sasson S. A. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 119:1992;493-501.
9. Hartley A., Stone J. M., Heron C., Cooper J. M., Scapira A. H. V. Complex I inhibitors induce dose-dependent apoptosis in PC12 cells: Relevance to Parkinson's disease. J. Neurochem. 63:1994;1987-1990.
10. Jones K. H., Senft J. A. An improved method to determine cell viability by simultaneous staining with fluorescein diacetate-propidium iodide. J. Histochem. Cytochem. 33:1985;77-79.
11. Jordan J., Galindo M. F., Miller R. J. Role of calpain- and Interleukin-1β-converting enzyme-like proteases in the β-amyloid-induced death of rat hippocampal neurons in culture. J. Neurochem. 68:1997;1612-1621.
12. Kampfl A., Posmantur R., Nixon R., Grynspan F., Zhao X., Liu S. J., Newcomb J. K., Clifton G. L., Hayes R. L. Calpain activation and calpain-mediated cytoskeletal proteolysis following traumatic brain injury. J. Neurochem. 67:1996;1575-1583.
13. Kampfl A., Zhao X., Whitson J. S., Posmantur R., Dixon C. E., Yang K., Clifton G. L., Hayes R. L. Calpain inhibitors protect against depolarization-induced neurofilament protein loss of septo-hippocampal neurons in culture. Eur. J. Neurosci. 8:1996;344-352.
14. Kikuchi H., Imajoh-Ohmi S. Activation and possible involvement of calpain, a calcium-activated cysteine protease, in down-regulation of apoptosis of human monoblast U937 cells. Cell Death Differ. 2:1995;195-199.
15. Koh J. Y., Choi D. W. Quantitative determination of glutamate mediated cortical neuronal injury in cell culture by lactate dehydrogenase efflux assay. J. Neurosci. Methods. 20:1987;83-90.
16. 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;2002-2009.
17. Lynch G., Baudry M. The biochemistry of memory: A new and specific hypothesis. Science. 224:1984;1057-1063.
18. Milligan C. E., Prevette D., Yaginuma H., Homma S., Cardwell C., Fritz L. C., Tomaselli K. J., Oppenhaim R. W., Schwartz L. M. Peptide inhibitors of the ICE protease family arrest programmed cell death of motoneuronsin vivoin vitro. Neuron. 15:1995;385-393.
19. Nath R., Kadee J. R., McGinnis K., Nadimpalli R., Stafford D., Wang K. K. W. Effects of ICE-like protease and calpain inhibitors on neuronal apoptosis. Neuroreport. 8:1996;249-255.
20. Portera-Cailliau C., Hedreen J. C., Price D. L., Koliatsos V. E. Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models. J. Neurosci. 15:1995;3775-3787.
21. Rabizadeh S., Gralla E. B., Borchelt D. R., Gwinn R., Valentine J. S., Sisodia S., Wong P., Lee M., Hahn H., Bredesen D. E. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: Studies in yeast end neural cells. Proc. Natl. Acad. Sci. USA. 92:1995;3024-3028.
22. Raff M. C., Barres B. A., Burne J. F., Coles H. S., Ishizaki Y., Jacobson M. D. Programmed cell death and the control of cell survival: Lessons from the nervous system. Science. 262:1993;695-700.
23. Saido T. C., Sorimachi H., Suzuki K. Calpain: New perspectives in molecular diversity and physiological-pathological involvement. FASEB J. 8:1994;814-822.
24. Saito K., Elce J. S., Hamos J. E., Nixon R. A. Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neural degeneration. Proc. Natl. Acad. Sci. USA. 90:1993;2628-2632.
25. Schwartz L. M., Milligan C. E. Cold thoughts of death: The role of ICE proteases in neuronal cell death. Trends Neurosci. 19:1996;555-562.
26. Shinohara K., Tomioka M., Nakano H., Toné S., Ito H., Kawashima S S. Apoptosis induction resulting from proteosome inhibition. Biochem. J. 317:1996;385-388.
27. Schulz J. B., Weller M., Klockgether T. Potassium deprivation-induced apoptosis of cerebellar granule neurons: A sequential requirement for new mRNA and protein synthesis, ICE-like protease activity, and reactive oxygen species. J. Neurosci. 16:1996;4696-4706.
28. Sparapani M., Dall'Olio R., Gandolfi O., Ciani E., Contestabile A. Neurotoxicity of polyamines and pharmacological neuroprotection in cultures of rat cerebellar granule cells. Exp. neurol. 148:1997;157-166.
29. Steller H. Mechanisms and genes of cellular suicide. Science. 267:1995;1445-1449.
30. Squier M. K. T., Miller A. C. K., Malkinson A. M., Cohen J. J. Calpain activation in apoptosis. J. Cell. Physiol. 159:1994;229-237.
31. Taylor J., Gatchalian C. L., Keen G., Rubin L. L. Apoptosis in cerebellar granule neurons: Involvement of interleukin-1β-converting enzyme-like proteases. J. Neurochem. 68:1997;1598-1605.
32. Wang K. K., Yuen P. W. Calpain inhibition: An overview of its therapeutic potential. Trends Phrmacol. Sci. 15:1994;412-419.
33. Wood K. A., Dipasquale B., Joule R. J. In situ. Neuron. 11:1993;621-632.