Caenorhabditis elegans respond to high-glucose diets through a network of stress-responsive transcription factors.

08:00 EDT 10th July 2018 | BioPortfolio

Summary of "Caenorhabditis elegans respond to high-glucose diets through a network of stress-responsive transcription factors."

High-glycemic-index diets, as well as a sedentary lifestyle are considered as determinant factors for the development of obesity, type 2 diabetes, and cardiovascular diseases in humans. These diets have been shown to shorten the life span of C. elegans in a manner that is dependent on insulin signaling, but the participation of other signaling pathways have not been addressed. In this study, we have determined that worms fed with high-glucose diets show alterations in glucose content and uptake, triglyceride content, body size, number of eggs laid, egg-laying defects, and signs of oxidative stress and accelerated aging. Additionally, we analyzed the participation of different key regulators of carbohydrate and lipid metabolism, oxidative stress and longevity such as SKN-1/NRF2, HIF-1/HIF1α, SBP-1/SREBP, CRH-1/CREB, CEP-1/p53, and DAF-16/FOXO, in the reduction of lifespan in glucose-fed worms.


Journal Details

This article was published in the following journal.

Name: PloS one
ISSN: 1932-6203
Pages: e0199888


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Medical and Biotech [MESH] Definitions

Proteins from the nematode species CAENORHABDITIS ELEGANS. The proteins from this species are the subject of scientific interest in the area of multicellular organism MORPHOGENESIS.

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Food and dietary formulations including elemental (chemically defined formula) diets, synthetic and semisynthetic diets, space diets, weight-reduction formulas, tube-feeding diets, complete liquid diets, and supplemental liquid and solid diets.

A species of nematode that is widely used in biological, biochemical, and genetic studies.

A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.

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