Abstract
The pathophysiology of febrile convulsion, the most common childhood neurologic disease, remains unclear. In this study, we investigated what role a heat shock protein plays in this disease. We enrolled eight boys and two girls with febrile convulsion and 10 age‐matched healthy controls. We did a biosynthetic evaluation of both groups by separating lymphocytes and measuring the expression of heat shock protein 72 before and after heat shock treatment. Before the treatment, both groups were found to have small amounts of constitutive heat shock protein 72. Afterwards, its expression increased in both groups, and no statistical difference was found between the increases in the two groups. In addition, there was no obvious difference in the susceptibility to produce heat shock proteins. However, the febrile convulsion group was found to have a significant decrease in phosphorylation of heat shock protein 72. These results suggest the possible involvement of post‐translational modification of heat shock proteins, most likely phosphorylation, in the pathogenesis of febrile convulsion.
Keywords: febrile convulsion, heat shock protein, phosphorylation
Full Text
The Full Text of this article is available as a PDF (466.5 KB).
References
- 1. Kaplan RE. Febrile seizures. When is treatment justified?. Postgrad Med. 1987; 82: 63–66 –, 69–71. [DOI] [PubMed] [Google Scholar]
- 2. Nelson KB, Ellenberg JH, eds. Febrile Seizure. New York, NY: Raven Press. 1981, 301–306. [Google Scholar]
- 3. Lee P, Jones KV. Urinary tract infection in febrile convulsions. Arch Dis Child. 1991; 66: 1291–1295. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 4. Lewis HM, Parry JV, Parry RP, et al. Role of viruses in febrile convulsions. Arch Dis Child. 1979; 54: 869–876. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 5. Helminen M, Vesikari T. Increased interleukin‐1 (IL‐1) production from LPS‐stimulated peripheral blood monocytes in children with febrile convulsions. Acta Pediatr Scand. 1990; 79: 810–816. [DOI] [PubMed] [Google Scholar]
- 6. Schmiegelow K, Johnsen AH, Ebbesen F, Sorensen O. Gamma‐ aminobutyric acid concentration in lumbar cerebrospinal fluid from patients with febrile convulsions and controls. Acta Pediatr Scand. 1990; 79: 1092–1098. [DOI] [PubMed] [Google Scholar]
- 7. Koyama A, Matsui T, Sugisawa T. Febrile convulsions in northern Japan: A quantitative and qualitative analysis of EEG and clinical findings. Acta Neurol Scand. 1991; 83: 411–417. [DOI] [PubMed] [Google Scholar]
- 8. Welch WJ, Suhan JP. Morphological study of the mammalian stress response: characterization of changes in cytoplasmic organelles, cytoskeleton, and nucleoli and the modulation of plasma membrane sodium‐potassium ATPase activity. J Cell Biol. 1985; 101: 1198–1211. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 9. Burdon RH, Cutmore DMM. Human heat shock gene expression and the modulation of plasma membrane sodium‐ potassium ATPase activity. FBES Lett. 1982; 140: 45–48. [DOI] [PubMed] [Google Scholar]
- 10. Lewis MJ, Pelham HRB. Involvement of ATP in the nuclear and nucleolar function of the 70 kd shock protein. EMBO J. 1985; 4: 3137–3143. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 11. Ritossa F. A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia. 1962; 18: 571–573. [Google Scholar]
- 12. Ashburner M, Bonner JJ. The induction of gene activity in drosophila by heat shock. Cell. 1979; 17: 241–254. [DOI] [PubMed] [Google Scholar]
- 13. Wang G, Zhang J, Moskophidis D, Mivechi NF. Targeted disruption of the heat shock transcription factor (hsf)‐2 gene results in increased embryonic lethality, neuronal defects, and reduced spermatogenesis. Genesis. 2003; 36: 48–61. [DOI] [PubMed] [Google Scholar]
- 14. Fukuyama Y, Kagawa K, Tanaka K. A genetic study of febrile convulsions. Eur Neurol. 1979; 18: 166–182. [DOI] [PubMed] [Google Scholar]
- 15. Krapfenbauer K, Berger M, Lubec G, Fountoulakis M. Changes in the brain protein levels following administration of kainic acid. Electrophoresis. 2001; 22: 2086–2091. [DOI] [PubMed] [Google Scholar]
- 16. White DJ, Carlson D, Ordway GA, Horton JW. Protective role of heat stress in burn trauma. Crit Care Med. 2004; 32: 1338–1345. [DOI] [PubMed] [Google Scholar]
- 17. Lai Y, Kochanek PM, Adelson PD, et al. Induction of the stress response after inflicted and non‐inflicted traumatic brain injury in infants and children. J Neurotrauma. 2004; 21: 229–237. [DOI] [PubMed] [Google Scholar]
- 18. Yang SL, Jing SH, Yang RC, et al. The effect of hyperthermic treatment on the recovery of EEG after interruption of respiration in rats. Exp Brain Res. 1994; 99: 431–434. [DOI] [PubMed] [Google Scholar]
- 19. Nover L. Heat Shock Response. Florida: CRC Press. 1991. [Google Scholar]
- 20. Parnham MJ, Feige U. Structural and functional properties of heat shock proteins in inflammation and immunity. Agents Actions. 1992; 35: 34–36. [DOI] [PubMed] [Google Scholar]
- 21. Barbe MF, Tyeli M, Gower DJ, Welch WJ. Hyperthermia protects against light damage in the rat retina. Science. 1988; 241: 1817–1820. [DOI] [PubMed] [Google Scholar]
- 22. Chopp M, Chen H, Ho KL, et al. Transient hyperthermia protects against subsequent forebrain ischemic cell damage in the rat. Neurology. 1989; 39: 1396–1398. [DOI] [PubMed] [Google Scholar]
- 23. Krueger‐Naug AM, Hopkins DA, Armstrong JN, et al. Hyperthermic induction of the 27 kDa heat shock protein (Hsp27) in neuroglia and neurons of the rat central nervous system. J Comp Neurol. 2000; 428: 495–510. [DOI] [PubMed] [Google Scholar]
- 24. Lavoie JN, Lambert H, Landry J, et al. Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation‐induced changes in the oligomeric structure of heat shock protein 27. Mol and Cell Biol. 1995; 15: 505–516. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 25. Schafer C, Clapp P, Williams JA, et al. Hsp 27 expression regulates CCK‐induced changes of the actin cytoskeleton in CHO‐CCK‐A cells. Am J Physiol. 1999; 277: C1032–C1043. [DOI] [PubMed] [Google Scholar]