Proteomic analyses of Caenorhabditis elegans dauer larvae and long-lived daf-2 mutants implicates a shared detoxification system in longevity assurance

Laura Megan Jones, Katharina Staffa, Samirah Perally, E. James LaCourse, Peter Michael Brophy, Joanne Veronica Hamilton

Allbwn ymchwil: Cyfraniad at gyfnodolynErthygladolygiad gan gymheiriaid

20 Dyfyniadau (Scopus)

Crynodeb

The insulin/insulin-like growth factor-1 (IGF-1) signaling system is a public regulator of aging in the model animals Caenorhabditis elegans, Drosophila melanogaster, and Mus musculus. For the first time, proteomic analyses of the environmentally resistant and ‘nonaging’ C. elegans dauer stage and long-lived daf-2 mutants has provided a unique insight into the protein changes which mediate survival against endogenously produced toxins. These changes support a diversion of energy consumption away from anabolic processes toward enhanced cellular maintenance and detoxification processes as previously described by the ‘Green Theory of Aging’. Important components of this enhanced longevity system identified in this proteomics study include the alpha-crystallin family of small heat shock proteins, anti-ROS defense systems and cellular phase II detoxification (in daf-2 only). Among those proteins involved in phase II cellular detoxification that were significantly upregulated was a Pi-class glutathione transferase (GST) CE00302. Targeting this GST with RNAi revealed compensatory regulation within the Pi-class GSTs. Furthermore, a recombinant form of the GST protein was found to detoxify and/or bind short-chain aldehydic natural toxic products of lipid peroxidation and long-chained fatty-acids at physiologically relevant concentrations, which may indicate a role in longevity. Keywords: C. elegans; dauer; daf-2; longevity; Insulin/IGF-1 signaling; IIS; 2-DE; proteomics; RNAi; glutathione transferase; GST-1; heat shock protein; HSP-12.6; glutathione peroxidise; superoxide dismutase; SOD-1; lipid binding protein; LBP-6; ribosomal protein; RPS-12.
Iaith wreiddiolSaesneg
Tudalennau (o-i)2871-2881
Nifer y tudalennau11
CyfnodolynJournal of Proteome Research
Cyfrol9
Rhif cyhoeddi6
Dynodwyr Gwrthrych Digidol (DOIs)
StatwsCyhoeddwyd - 15 Ebr 2010

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