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Increased protein stability and decreased protein turnover in the Caenorhabditis elegans Ins/IGF-1 daf-2 mutant

Geert Depuydt (UGent) , Nilesh Shanmugam (UGent) , Madina Rasulova (UGent) , Ineke Dhondt (UGent) and Bart Braeckman (UGent)
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Abstract
In Caenorhabditis elegans, cellular proteostasis is likely essential for longevity. Autophagy has been shown to be essential for lifespan extension of daf-2 insulin/IGF mutants. Therefore, it can be hypothesized that daf-2 mutants achieve this phenotype by increasing protein turnover. However, such a mechanism would exert a substantial energy cost. By using classical S-35 pulse-chase labeling, we observed that protein synthesis and degradation rates are decreased in young adults of the daf-2 insulin/IGF mutants. Although reduction of protein turnover may be energetically favorable, it may lead to accumulation and aggregation of damaged proteins. As this has been shown not to be the case in daf-2 mutants, another mechanism must exist to maintain proteostasis in this strain. We observed that proteins isolated from daf-2 mutants are more soluble in acidic conditions due to increased levels of trehalose. This suggests that trehalose may decrease the potential for protein aggregation and increases proteostasis in the daf-2 mutants. We postulate that daf-2 mutants save energy by decreasing protein turnover rates and instead stabilize their proteome by trehalose.
Keywords
Caenorhabditis, Protein metabolism, Trehalose, Radiolabeling, LIFE-SPAN EXTENSION, AGE-RELATED-CHANGES, C-ELEGANS, DIETARY RESTRICTION, AUTOPHAGIC PROTEOLYSIS, MITOCHONDRIAL TURNOVER, PROTEASOME ACTIVITIES, INHIBIT TRANSLATION, IN-VIVO, TREHALOSE

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MLA
Depuydt, Geert et al. “Increased Protein Stability and Decreased Protein Turnover in the Caenorhabditis Elegans Ins/IGF-1 Daf-2 Mutant.” JOURNALS OF GERONTOLOGY SERIES A-BIOLOGICAL SCIENCES AND MEDICAL SCIENCES 71.12 (2016): 1553–1559. Print.
APA
Depuydt, G., Shanmugam, N., Rasulova, M., Dhondt, I., & Braeckman, B. (2016). Increased protein stability and decreased protein turnover in the Caenorhabditis elegans Ins/IGF-1 daf-2 mutant. JOURNALS OF GERONTOLOGY SERIES A-BIOLOGICAL SCIENCES AND MEDICAL SCIENCES, 71(12), 1553–1559.
Chicago author-date
Depuydt, Geert, Nilesh Shanmugam, Madina Rasulova, Ineke Dhondt, and Bart Braeckman. 2016. “Increased Protein Stability and Decreased Protein Turnover in the Caenorhabditis Elegans Ins/IGF-1 Daf-2 Mutant.” Journals of Gerontology Series A-biological Sciences and Medical Sciences 71 (12): 1553–1559.
Chicago author-date (all authors)
Depuydt, Geert, Nilesh Shanmugam, Madina Rasulova, Ineke Dhondt, and Bart Braeckman. 2016. “Increased Protein Stability and Decreased Protein Turnover in the Caenorhabditis Elegans Ins/IGF-1 Daf-2 Mutant.” Journals of Gerontology Series A-biological Sciences and Medical Sciences 71 (12): 1553–1559.
Vancouver
1.
Depuydt G, Shanmugam N, Rasulova M, Dhondt I, Braeckman B. Increased protein stability and decreased protein turnover in the Caenorhabditis elegans Ins/IGF-1 daf-2 mutant. JOURNALS OF GERONTOLOGY SERIES A-BIOLOGICAL SCIENCES AND MEDICAL SCIENCES. 2016;71(12):1553–9.
IEEE
[1]
G. Depuydt, N. Shanmugam, M. Rasulova, I. Dhondt, and B. Braeckman, “Increased protein stability and decreased protein turnover in the Caenorhabditis elegans Ins/IGF-1 daf-2 mutant,” JOURNALS OF GERONTOLOGY SERIES A-BIOLOGICAL SCIENCES AND MEDICAL SCIENCES, vol. 71, no. 12, pp. 1553–1559, 2016.
@article{8048158,
  abstract     = {In Caenorhabditis elegans, cellular proteostasis is likely essential for longevity. Autophagy has been shown to be essential for lifespan extension of daf-2 insulin/IGF mutants. Therefore, it can be hypothesized that daf-2 mutants achieve this phenotype by increasing protein turnover. However, such a mechanism would exert a substantial energy cost. By using classical S-35 pulse-chase labeling, we observed that protein synthesis and degradation rates are decreased in young adults of the daf-2 insulin/IGF mutants. Although reduction of protein turnover may be energetically favorable, it may lead to accumulation and aggregation of damaged proteins. As this has been shown not to be the case in daf-2 mutants, another mechanism must exist to maintain proteostasis in this strain. We observed that proteins isolated from daf-2 mutants are more soluble in acidic conditions due to increased levels of trehalose. This suggests that trehalose may decrease the potential for protein aggregation and increases proteostasis in the daf-2 mutants. We postulate that daf-2 mutants save energy by decreasing protein turnover rates and instead stabilize their proteome by trehalose.},
  author       = {Depuydt, Geert and Shanmugam, Nilesh and Rasulova, Madina and Dhondt, Ineke and Braeckman, Bart},
  issn         = {1079-5006},
  journal      = {JOURNALS OF GERONTOLOGY SERIES A-BIOLOGICAL SCIENCES AND MEDICAL SCIENCES},
  keywords     = {Caenorhabditis,Protein metabolism,Trehalose,Radiolabeling,LIFE-SPAN EXTENSION,AGE-RELATED-CHANGES,C-ELEGANS,DIETARY RESTRICTION,AUTOPHAGIC PROTEOLYSIS,MITOCHONDRIAL TURNOVER,PROTEASOME ACTIVITIES,INHIBIT TRANSLATION,IN-VIVO,TREHALOSE},
  language     = {eng},
  number       = {12},
  pages        = {1553--1559},
  title        = {Increased protein stability and decreased protein turnover in the Caenorhabditis elegans Ins/IGF-1 daf-2 mutant},
  url          = {http://dx.doi.org/10.1093/gerona/glv221},
  volume       = {71},
  year         = {2016},
}

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