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Enhancement of presynaptic performance in transgenic Drosophila overexpressing heat shock protein Hsp70
Author(s) -
Karunanithi Shanker,
Barclay Jeffrey W.,
Brown Ian R.,
Robertson R. Meldrum,
Atwood Harold L.
Publication year - 2002
Publication title -
synapse
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.809
H-Index - 106
eISSN - 1098-2396
pISSN - 0887-4476
DOI - 10.1002/syn.10048
Subject(s) - hsp70 , microbiology and biotechnology , postsynaptic potential , synapse , shock (circulatory) , drosophila (subgenus) , heat shock protein , neurotransmission , transgene , biophysics , biology , neuroscience , chemistry , biochemistry , gene , medicine , receptor
Prior heat shock confers protection to Drosophila synapses during subsequent heat stress by stabilizing quantal size and reducing the decline of quantal emission at individual synaptic boutons. The major heat shock protein Hsp70, which is strongly induced by high temperatures in Drosophila, may be responsible for this synaptic protection. To test this hypothesis, we investigated synaptic protection and stabilization at larval neuromuscular junctions of transgenic Drosophila which produce more than the normal amount of Hsp70 in response to heat shock. Overexpression of Hsp70 coincides with enhanced protection of presynaptic performance, assayed by measuring mean quantal content and percentage success of transmission. Quantal size was not selectively altered, indicating no effects of overexpression on postsynaptic performance. Thus, presynaptic mechanisms can be protected by manipulating levels of Hsp70, which would provide stability to neural circuits otherwise susceptible to heat stress. Synapse 44:8–14, 2002. © 2002 Wiley‐Liss, Inc.