Proteomic analysis of age-dependent changes in protein solubility identifies genes that modulate lifespan.

ABSTRACT: While it is generally recognized that misfolding of specific proteins can cause late-onset disease, the contribution of protein aggregation to the normal aging process is less well understood. To address this issue, a mass spectrometry-based proteomic analysis was performed to identify proteins that adopt sodium dodecyl sulfate (SDS)-insoluble conformations during aging in Caenorhabditis elegans. SDS-insoluble proteins extracted from young and aged C. elegans were chemically labeled by isobaric tagging for relative and absolute quantification (iTRAQ) and identified by liquid chromatography and mass spectrometry. Two hundred and three proteins were identified as being significantly enriched in an SDS-insoluble fraction in aged nematodes and were largely absent from a similar protein fractio

SUBMITTER: Reis-Rodrigues P 

PROVIDER: S-EPMC3437485 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature