Glycerol stimulates innate chaperoning, proteasomal and stress-resistance functions: Implications for geronto-manipulation
College
College of Science
Department/Unit
Biology
Document Type
Article
Source Title
Biogerontology
Volume
9
First Page
269
Last Page
282
Publication Date
2008
Abstract
Aging is associated with accumulation of toxic intracellular and extracellular protein aggregates. Cells manage “aged” proteins by mobilizing their molecular chaperones or heat shock proteins that are also considered as determinants of lifespan in diverse species. In this study, we tested whether an exogenous addition of the non-toxic chemical chaperone ‘glycerol’ could elicit stress and geronto-protective activities. We found that glycerol enhanced chaperoning of heat-denatured proteins. In addition to stimulating proteasome activity, glycerol led to an increased expression of the stress chaperone ‘mortalin’ and decreased p53 function in human cells. Glycerol-fed worms exhibited thermo-tolerance and lower level of age-associated auto-fluorescence. Through the combined stimulation of the proteasome and chaperoning activities of mortalin, in particular, glycerol treatment resulted in increased survival and fitness against oxidative- and heat-stress. These results may have significant implications in the use of glycerol as a candidate geronto-modulator in development of practical interventions for “healthy aging”.
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Recommended Citation
Deocaris, C. C., Takano, S., Priyandoko, D., Kaul, Z., Yaguchi, T., Kraft, D. C., Yamasaki, K., Kaul, S. C., & Wadhwa, R. (2008). Glycerol stimulates innate chaperoning, proteasomal and stress-resistance functions: Implications for geronto-manipulation. Biogerontology, 9, 269-282. Retrieved from https://animorepository.dlsu.edu.ph/faculty_research/5468
Disciplines
Biochemistry, Biophysics, and Structural Biology | Biology
Keywords
Glycerin; Molecular chaperones; Stress (Physiology); Gerontology; Protein folding; Homeostasis
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