Biochemical and Biophysical Research Communications
The effect of neuronal expression of heat shock proteins 26 and 27 on lifespan, neurodegeneration, and apoptosis in Drosophila
Section snippets
Materials and methods
Fly strains. UAS-hsp26 and UAS-hsp27 have been described previously [9]. UAS-reaper, UAS-hid, and UAS-grim were obtained from Dr. Ann-Shyn Chiang’s lab. Double UAS lines, UAS-rpr;UAS-hsp26, UAS-rpr;UAS-hsp27, UAS-hid;UAS-hsp26, UAS-hid;UAS-hsp27, UAS-grim;UAS-hsp26, and UAS-grim; UAS-hsp27 were generated. A pan-neuronal driver, elav-GAL4, was used to induce transgene expression. GMR-GAL4/Cyo;UAS-41Q and GMR-GAL4/Cyo;UAS-127Q were obtained from Dr. Seymour Benzer’s lab. All flies were raised on
Neuronal overexpression of hsp26 or hsp27 increases lifespan and resistance to oxidative stress in Drosophila
Our previous study showed that ubiquitous expression of hsp26 or hsp27 increases Drosophila lifespan and resistance to oxidative stress [9]. Neuronal tissue is suggested to be important for the control of lifespan [14]. To examine whether neuronal overexpression of hsp26 or hsp27 is sufficient to extend lifespan, we measured the lifespan of flies overexpressing hsp26 or hsp27 by the elav-GAL4, and of the corresponding control flies, at 25 °C. There is an increase of approximately 32–44% in the
Acknowledgments
This study was supported by grants from the National Science Council (NSC-96-2311-B-007-003) and the APEX from the Brain Research Center at National Tsing-Hua University to H.-D. Wang.
References (43)
- et al.
Longevity and the stress response in Drosophila
Exp. Gerontol.
(2007) Neuronal regulation of lifespan: clues from flies and worms
Mech. Ageing Dev.
(2001)- et al.
Geldanamycin induces heat shock protein 70 and protects against MPTP-induced dopaminergic neurotoxicity in mice
J. Biol. Chem.
(2005) - et al.
Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation
J. Biol. Chem.
(2000) - et al.
Small stress proteins as novel regulators of apoptosis. Heat shock protein 27 blocks Fas/APO-1- and staurosporine-induced cell death
J. Biol. Chem.
(1996) - et al.
Paraquat exposure as an etiological factor of Parkinson’s disease
Neurotoxicology
(2006) - et al.
Neuroprotection by Hsp104 and Hsp27 in lentiviral-based rat models of Huntington’s disease
Mol. Ther.
(2007) - et al.
The Drosophila gene hid is a direct molecular target of Ras-dependent survival signaling
Cell
(1998) - et al.
A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
J. Biol. Chem.
(2005) - et al.
Molecular chaperones in the cytosol: from nascent chain to folded protein
Science
(2002)
Posttranslational quality control: folding, refolding, and degrading proteins
Science
Molecular chaperones—cellular machines for protein folding
Angew. Chem. Int. Ed. Engl.
Regulation of heat shock gene induction and expression during Drosophila development
Cell. Mol. Life Sci.
Drosophila as a model for human neurodegenerative disease
Annu. Rev. Genet.
Heat shock genes—integrating cell survival and death
J. Biosci.
Chaperoning extended life
Nature
Multiple-stress analysis for isolation of Drosophila longevity genes
Proc. Natl. Acad. Sci. USA
Overexpression of the small mitochondrial Hsp22 extends Drosophila life span and increases resistance to oxidative stress
FASEB J.
Regulation of aging and age-related disease by DAF-16 and heat-shock factor
Science
Lifespan extension in C. elegans by a molecular chaperone dependent upon insulin-like signals
Aging Cell
Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
Mol. Biol. Cell
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These authors contributed equally to this work.