Thermoprotection of synaptic transmission in aDrosophilaheat shock factor mutant is accompanied by increased expression of Hsp83 and DnaJ-1
Autor: | Scott J. Neal, Anthony K.-C. So, J. Timothy Westwood, Robert M. Tanguay, Harold L. Atwood, Shanker Karunanithi, Adrienne Best |
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Rok vydání: | 2006 |
Předmět: |
endocrine system
Hot Temperature Physiology Acclimatization Mutant Biology Neurotransmission Synaptic Transmission Neuromuscular junction Heat Shock Transcription Factors Heat shock protein Genetics medicine Animals Drosophila Proteins RNA Messenger Heat-Shock Proteins Oligonucleotide Array Sequence Analysis Gene Expression Profiling Reproducibility of Results HSP40 Heat-Shock Proteins Molecular biology Up-Regulation Cell biology Hsp70 DNA-Binding Proteins Heat shock factor Drosophila melanogaster medicine.anatomical_structure Larva Shock (circulatory) Mutation Hypot medicine.symptom Heat-Shock Response Transcription Factors |
Zdroj: | Physiological Genomics. 25:493-501 |
ISSN: | 1531-2267 1094-8341 |
Popis: | In Drosophila larvae, acquired synaptic thermotolerance after heat shock has previously been shown to correlate with the induction of heat shock proteins (Hsps) including HSP70. We tested the hypothesis that synaptic thermotolerance would be significantly diminished in a temperature-sensitive strain ( Drosophila heat shock factor mutant hsf4), which has been reported not to be able to produce inducible Hsps in response to heat shock. Contrary to our hypothesis, considerable thermoprotection was still observed at hsf4larval synapses after heat shock. To investigate the cause of this thermoprotection, we conducted DNA microarray experiments to identify heat-induced transcript changes in these organisms. Transcripts of the hsp83, dnaJ-1 ( hsp40), and glutathione- S-transferase gstE1 genes were significantly upregulated in hsf4larvae after heat shock. In addition, increases in the levels of Hsp83 and DnaJ-1 proteins but not in the inducible form of Hsp70 were detected by Western blot analysis. The mode of heat shock administration differentially affected the relative transcript and translational changes for these chaperones. These results indicate that the compensatory upregulation of constitutively expressed Hsps, in the absence of the synthesis of the major inducible Hsp, Hsp70, could still provide substantial thermoprotection to both synapses and the whole organism. |
Databáze: | OpenAIRE |
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