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Carbonylated proteins are eliminated during reproduction in C. elegans.
Aging Cell. 2010 Dec; 9(6):991-1003
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26 Jan 2012
Confirmation, New Finding
DOI: 10.3410/f.13489035.14866153
Protein carbonylation is a prominent type of oxidative damage to proteins that accumulates with age in many species. This damage has to be somehow eliminated from germline cells to ensure the production of healthy offspring. Caenorhabditis elegans is a major model system to study aging, but carbonyl and...Continue reading
Protein carbonylation is a prominent type of oxidative damage to proteins that accumulates with age in many species. This damage has to be somehow eliminated from germline cells to ensure the production of healthy offspring. Caenorhabditis elegans is a major model system to study aging, but carbonyl and damage elimination has not been extensively studied. This paper shows that carbonyls are abruptly eliminated at the time of oocyte maturation and that this process requires proteasome function, as in mice, but not Sir2, as in yeast. This finding is important in reconciling major mechanisms of aging and longevity among metazoans.
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Hekimi S: F1000Prime Recommendation of [Goudeau J and Aguilaniu H, Aging Cell 2010, 9(6):991-1003]. In F1000Prime, 26 Jan 2012; DOI: 10.3410/f.13489035.14866153. F1000Prime.com/13489035#eval14866153
F1000Prime Recommendations, Dissents and Comments for [Goudeau J and Aguilaniu H, Aging Cell 2010, 9(6):991-1003]. In F1000Prime, 23 May 2013; F1000Prime.com/13489035
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Oxidatively damaged proteins accumulate with age in many species (Stadtman (1992) Science257, 1220-1224). This means that damage must be reset at the time of reproduction. To visualize this resetting in the roundworm Caenorhabditis elegans, a novel immunofluorescence technique that allows the detection of carbonylated proteins in situ was developed. The application of this technique revealed that carbonylated proteins are eliminated during C. elegans reproduction. This purging occurs abruptly within the germline at the time of oocyte maturation. Surprisingly, the germline was markedly more oxidized than the surrounding somatic tissues. Because distinct mechanisms have been proposed to explain damage elimination in yeast and mice (Aguilaniu et al. (2003) Science299, 1751-1753; Hernebring et al. (2006) Proc Natl Acad Sci USA103, 7700-7705), possible common mechanisms between worms and one of these systems were tested. The results show that, unlike in yeast (Aguilaniu et al. (2003) Science299, 1751-1753; Erjavec et al. (2008) Proc Natl Acad Sci USA105, 18764-18769), the elimination of carbonylated proteins in worms does not require the presence of the longevity-ensuring gene, SIR-2.1. However, similar to findings in mice (Hernebring et al. (2006) Proc Natl Acad Sci USA103, 7700-7705), proteasome activity in the germline is required for the resetting of carbonylated proteins during reproduction in C. elegans. Thus, oxidatively damaged proteins are eliminated during reproduction in worms through the proteasome. This finding suggests that the resetting of damaged proteins during reproduction is conserved, therefore validating the use of C. elegans as a model to study the molecular basis of damage elimination.
© 2010 The Authors. Aging Cell © 2010 Blackwell Publishing Ltd/Anatomical Society of Great Britain and Ireland.
DOI: 10.1111/j.1474-9726.2010.00625.x
PMID: 21040398
