Longevity and stress in Caenorhabditis elegans

Zhou, Katherine I.; Pincus, Zachary; Slack, Frank J.

doi:10.18632/aging.100367

Cited by 150 publications

(136 citation statements)

References 190 publications

(420 reference statements)

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“…Reduction in IIS as well as TOR and S6K promotes lifespan extension in this organism. TOR activity is reduced by decreased availability of AA and growth factors [4, 18–20]. Furthermore, inhibition of the TOR amino acid-sensing pathway under DR conditions extends lifespan (Fig.…”

Section: Dietary Restriction and Lifespan In Worms And Fliesmentioning

confidence: 99%

Protein and amino acid restriction, aging and disease: from yeast to humans

Mirzaei

Suárez

Longo

2014

Trends in Endocrinology & Metabolism

213

158

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Many of the effects of dietary restriction (DR) on longevity and health span in model organisms have been linked to reduced protein and amino acid (AA) intake and the stimulation of specific nutrient signaling pathways. Studies in yeast have shown that addition of serine, threonine, and valine in media promotes cellular sensitization and aging by activating different but connected pathways. Protein or essential AA restriction extends both lifespan and healthspan in rodent models. In humans, protein restriction (PR) has been associated with reduced cancer, diabetes, and overall mortality. Thus, interventions aimed at lowering the intake of proteins or specific AAs can be beneficial and have the potential to be widely adopted and effective in optimizing healthspan.

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Section: Dietary Restriction and Lifespan In Worms And Fliesmentioning

confidence: 99%

Protein and amino acid restriction, aging and disease: from yeast to humans

Mirzaei

Suárez

Longo

2014

Trends in Endocrinology & Metabolism

213

158

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“…Interestingly, there is significant cross-talk between these two pathways in C. elegans and other organisms (53,54). The set of ascr#2-regulated phosphoproteins contains 22 phosphorylated proteins with established or emerging roles in stress response (55)(56)(57)(58)(59)(60)(61)(62)(63)(64)(65)(66)(67)(68)(69) and 24 phosphorylated proteins with roles in aging and longevity (59, 63, 64, 66, 67, 70 -81), some of which overlap (Table I).…”

Section: Fig 3 Protein and Phosphopeptide Identification Overlap Amentioning

confidence: 99%

NeuCode Labeling in Nematodes: Proteomic and Phosphoproteomic Impact of Ascaroside Treatment in Caenorhabditis elegans

Rhoads¹,

Prasad

Kwiecien

et al. 2015

Molecular & Cellular Proteomics

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The nematode Caenorhabditis elegans is an important model organism for biomedical research. We previously described NeuCode stable isotope labeling by amino acids in cell culture (SILAC), a method for accurate proteome quantification with potential for multiplexing beyond the limits of traditional stable isotope labeling by amino acids in cell culture. Here we apply NeuCode SILAC to profile the proteomic and phosphoproteomic response of C. elegans to two potent members of the ascaroside family of nematode pheromones. By consuming labeled E. coli as part of their diet, C. elegans nematodes quickly and easily incorporate the NeuCode heavy lysine isotopologues by the young adult stage. Using this approach, we report, at high confidence, one of the largest proteomic and phosphoproteomic data sets to date in C. elegans: 6596 proteins at a false discovery rate < 1% and 6620 phosphorylation isoforms with localization probability >75%. Our data reveal a post-translational signature of pheromone sensing that includes many conserved proteins implicated in longevity and response to stress. Molecular & Cellular

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“…The molecular mechanisms underlying this process are not all understood and multiple theories have been proposed to explain it [reviewed in (Vina et al 2007;Zhou et al 2011)]. Among them the mitochondrial free radical theory of aging has been intensively studied in the past decades and places mitochondria at the center of the aging process.…”

Section: Introductionmentioning

confidence: 99%

Drosophila melanogaster mitochondrial Hsp22: a role in resistance to oxidative stress, aging and the mitochondrial unfolding protein response

2015

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Aging is characterized by the accumulation of dysfunctional mitochondria. Since these organelles are involved in many important cellular processes, different mechanisms exist to maintain their integrity. Among them is the mitochondrial unfolding protein response, which triggers the expression of a set of proteins aimed at re-establishing mitochondrial homeostasis. The induction of mitochondrial chaperones expression, particularly of Hsp60 and Hsp70, is a hallmark of this pathway. In Drosophila melanogaster, Hsp22 is also up-regulated by mitochondrial stress. This small heat shock protein is one of the members of the family to be localized inside mitochondria. One characteristic of Drosophila Hsp22 is its preferential up-regulation during aging and in oxidative stress conditions. It is a beneficial protein since its over-expression increases lifespan and resistance to stress while its down-regulation is detrimental. This review focuses on Drosophila Hsp22 and its links with the mitochondrial unfolding protein response and the aging process, in addition to highlight the important role of this sHSP in mitochondrial homeostasis.

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Longevity and stress in Caenorhabditis elegans

Cited by 150 publications

References 190 publications

Protein and amino acid restriction, aging and disease: from yeast to humans

Protein and amino acid restriction, aging and disease: from yeast to humans

NeuCode Labeling in Nematodes: Proteomic and Phosphoproteomic Impact of Ascaroside Treatment in Caenorhabditis elegans

Drosophila melanogaster mitochondrial Hsp22: a role in resistance to oxidative stress, aging and the mitochondrial unfolding protein response

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