Expression of the 27,000 mol. wt heat shock protein following kainic acid-induced status epilepticus in the rat

Neuroscience

Volumn 75, Issue 3, 1996, Pages 849-856

  Plumier, J C L ^a   Armstrong, J N ^a,b   Landry, J ^c   Babity, J M ^a,b   Robertson, H A ^b   Currie, R W ^a  

^a DALHOUSIE UNIVERSITY   (Canada)

^b DALHOUSIE UNIVERSITY   (Canada)

^c LAVAL UNIVERSITY   (Canada)

Author keywords

astrogliosis; epilepsy; heat shock; hippocampus; piriform cortex; reactive astrocytes

Indexed keywords

HEAT SHOCK PROTEIN; KAINIC ACID;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; ASTROCYTE; CONTROLLED STUDY; EPILEPSY; GLIOSIS; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; MALE; NONHUMAN; PRIORITY JOURNAL; PYRIFORM CORTEX; RAT;

EID: 0030561264     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/0306-4522(96)00317-X     Document Type: Article

References (36)

1. 1. Armstrong J. N., Plumier J.-C. L., Robertson H. A. and Currie R. W. (1996) The inducible 70,000 mol. wt heat shock protein is expressed in the degenerating dentate hilus and piriform cortex after systemic administration of kainic acid in the rat. Neuroscience (in press).
2. 2. Arrigo A.-P. and Landry J. (1994) Expression and function of the low-molecular-weight heat shock proteins. In The Biology of Heat Shock Proteins and Molecular Chaperones (eds Morimoto R. I., Tissières A. and Georgopoulos C.), pp. 335-373. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
3. 3. Baorto M. D., Mellado W. and Shelanski M. L. (1992) Astrocyte process growth induction by actin breakdown. J. Cell BM. 117, 357-367.
4. 4. Ben-Ari Y. (1985) Limbic seizure and brain damage produced by kainic acid: mechanisms and relevance to human temporal lobe epilepsy. Neuroscience 14, 375-103.
5. 5. Brown I. R., Rush S. J. and Ivy G. O. (1989) Induction of a heat shock gene at the site of tissue injury in the rat brain. Neuron 2, 1559-1564.
6. 6. Currie R. W. and White F. P. (1981) Trauma-induced protein in rat tissues: a physiological role for a "heat shock" protein? Science 214, 72-73.
7. 7. Dusart I., Marty S. and Peschanski M. (1991) Glial changes following an excitotoxic lesion in the CNS. II. Astrocytes. Neuroscience 45, 541-549.
8. 8. Fernaud-Epinosa I., Nieto-Sampedro M. and Bovolenta P. (1993) Differential activation of microglia and astrocytes in aniso-and isomorphic gliotic tissue. Glia 8, 227-291.
9. 9. Gass P., Prior P. and Kiessling M. (1995) Correlation between seizure intensity and stress protein expression after limbic epilepsy in the rat brain. Neuroscience 65, 27-36.
10. 10. Goldman J. E. and Abramson B. (1990) Cyclic AMP-induced shape changes of astrocytes are accompanied by rapid depolymerization of actin. Brain Res. 528, 189-196.
11. 11. Goldman J. E. and Chiu F. (1984) Dibutyril cyclic AMP causes intermediate filament accumulation and actin reorganization in astrocytes. Brain Res. 306, 85-95.
12. 12. Gonzalez M. F., Lowenstein D., Fernyak S., Hisanaga K., Simon R. and Sharp F. R. (1991) Induction of heat shock protein 72-like immunoreactivity in the hippocampal formation following transient global ischemia. Brain Res. Bull. 26, 241-250.
13. 13. Gonzalez M. F., Shiraishi K., Kisanaga K., Sagar S. M., Mandabach M. and Sharp F. R. (1989) Heat shock proteins as markers of neural injury. Molec. Brain Res. 6, 93-100.
14. 14. Head M. W., Corbin E. and Goldman J. E. (1993) Overexpression and abnormal modification of the stress proteins αB-crystallin and HSP27 in Alexander disease. Am. J. Pathol. 143, 1743-1753.
15. 15. Head M. W., Corbin E. and Goldman J. E. (1993) Coordinate and independent regulation of αB-crystallin and HSP27 expression in response to physiological stress. J. Cell Physiol. 159, 41-50.
16. 16. Iwaki T., Iwaki A., Tateishi J., Sakaki Y. and Goldman J. E. (1993) αB-Crystallin and 27-kD heat shock protein are regulated by stress conditions in the central nervous system and accumulate in Rosenthal fibers. Am. J. Pathol. 143, 487-495.
17. 17. Jørgensen M. B., Finsen B. R., Jensen M. B., Castellano B., Diemer N. H. and Zimmer J. (1993) Microglial and astroglial reactions to ischemic and kainic acid-induced lesions of the adult rat hippocampus. Expl Neurol. 120, 70-88.
18. 18. Kato H., Liu Y., Kogure K. and Kato K. (1994) Induction of 27-kDa heat shock protein following cerebral ischemia in a model of ischemic tolerance. Brain Res. 634, 235-244.
19. 19. Landry J., Chrétien P., Lambert H., Hickey E. and Weber L. A. (1989) Heat shock resistance conferred by expression of the human HSP27 gene in rodent cells. J. Cell Biol. 109, 7-15.
20. 20. Lavoie J. N., Gingras-Breton G., Tanguay R. M. and Landry J. (1993) Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J. biol. Chem. 268, 3420-3429.
21. 21. Lavoie J. N., Hickey E., Weber L. A. and Landry J. (1993) Modulation of actin microfilament dynamics and fluid phase pinocytosis by phosphorylation of heat shock protein 27. J. biol. Chem. 268, 24210-24214.
22. 22. Lavoie J. N., Lambert H., Hickey E., Weber L. A. and Landry J. (1995) Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Molec. cell Biol. 15, 505-516.
23. 23. Lowenstein D. H., Simon R. P. and Sharp F. R. (1990) The pattern of 72-kDa heat shock protein-like immunoreactivity in the rat brain following fluorothyl-induced status epilepticus. Brain Res. 531, 173-182.
24. 24. Mehlen P., Préville X., Chareyron P., Briolay J., Klementz R. and Arrigo A.-P. (1995) Constitutive expression of human HSP27, Drosophila HSP27, or human alpha B-crystallin confer resistance to TNF-and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts. J. Immunol. 154, 363-374.
25. 25. Miron T., Vancompernolle K., Vandekerckhove J., Wilchek M. and Geiger B. (1991) A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein. J. Cell Biol. 114, 255-261.
26. 26. Miron T., Wilchek M. and Geiger B. (1988) Characterization of an inhibitor of actin polymerization in vinculin-rich fraction of turkey gizzard smooth muscle. Eur. J. Biochem. 178, 543-553.
27. 27. O'Farrell P. H. (1975) High resolution two-dimensional electrophoresis of proteins. J. biol. Chem. 250, 4007-4021.
28. 28. Plumier J.-C. L., Ross B. M., Currie R. W., Angelidis C. E., Kazlaris H., Kollias G. and Pagoulatos G. N. (1995) Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery. J. clin. Invest. 95, 1854-1860.
29. i. Glia 13, 101-112.
30. 30. Renkawek K., Bosman G. J. and De Jong W. W. (1994) Expression of small heat-shock protein hsp27 in reactive gliosis in Alzheimer disease and other types of dementia. Acta neuropath., Berlin 87, 511-519.
31. 31. Schmidt-Kastner R. and Ingvar M. (1994) Loss of immunoreactivity for glial fibrillary acidic protein (GFAP) in astrocytes as a marker for profound tissue damage in substantia nigra and basal cortical areas after status epilepticus induced by pilocarpine in rat. Glia 12, 165-172.
32. 32. Sharp F. R., Lowenstein D., Simon R. and Hisanaga K. (1991) Heat shock protein hsp72 induction in cortical and striatal astrocytes and neurons following infarction. J. cerebr. Blood Flow Metab. 11, 621-627.
33. 33. Simon R. P., Cho H., Gwinn R. and Lowenstein D. H. (1991) The temporal profile of 72-kDa heat-shock protein expression following global ischemia. J. Neurosci. 11, 881-889.
34. 34. Sloviter R. S. and Lowenstein D. H. (1992) Heat shock protein expression in vulnerable cells of the rat hippocampus as an indicator of excitation-induced neuronal stress. J. Neurosci. 12, 3004-3009.
35. 35. Towbin H., Staeheln T. and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. natn. Acad. Sci. U.S.A. 76, 4350-4354.
36. 36. Vass K., Berger M. L., Nowak T. S. Jr., Welch W. J. and Lassmann H. (1989) Induction of stress protein HSP70 in nerve cells after status epilepticus in the rat. Neurosci. Lett. 100, 259-264.