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Geroprotection by Glycerol
Author(s) -
DEOCARIS CUSTER C.,
SHRESTHA BHUPAL G.,
KRAFT DAVID C.,
YAMASAKI KAZUHIKO,
KAUL SUNIL C.,
RATTAN SURESH I. S.,
WADHWA RENU
Publication year - 2006
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1354.070
Subject(s) - heat shock protein , chaperone (clinical) , downregulation and upregulation , chemistry , glycerol , luciferase , hsp70 , proteasome , chemical chaperone , microbiology and biotechnology , in vivo , oxidative stress , cytotoxicity , hsp90 , homeostasis , heat shock , biochemistry , in vitro , transfection , unfolded protein response , biology , gene , medicine , pathology
Chaperones, particularly the heat‐shock proteins, are considered as key players in the maintenance of protein homeostasis and are associated with longevity and cellular immortalization. In this study, we investigated the geroprotective activity of the chemical chaperone glycerol. Glycerol showed significant chaperoning activity in refolding heat‐denatured luciferase in vivo and in protecting cells from heat stress‐induced cytotoxicity. This was accompanied by decrease in p53, an upregulation of a stress chaperone mortalin/mtHsp70, and an increase in proteasome activity in the presence of oxidative stress.