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A Rhodiola Rosea Root Extract Protects Skeletal Muscle Cells Against Chemically Induced Oxidative Stress by Modulating Heat Shock Protein 70 (HSP70) Expression
Author(s) -
HernándezSantana Aaron,
PérezLópez Verónica,
Zubeldia Jose María,
JiménezdelRio Miguel
Publication year - 2014
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.5046
Subject(s) - rhodiola rosea , hsp70 , oxidative stress , heat shock protein , rhodiola , traditional medicine , pharmacognosy , protein expression , biology , chemistry , in vitro , biochemistry , pharmacology , medicine , salidroside , biological activity , gene
Rhodiola rosea is a perennial plant in the Crassulaceae family, recently postulated to exert its adaptogenic functions partially by modulating the expression of molecular factors such as heat shock proteins (HSP). The aim of this study was to analyze the efficacy of a Rhodiola rosea extract (Rhodiolife) in protecting murine skeletal muscle cells (C 2 C 12 myotubes) from chemically induced oxidative stress and to establish whether modulation of HSP70 expression is observed. C 2 C 12 cells treated with Rhodiolife did not experience any loss of viability (p > 0.05) at concentrations of 1–100 µg/mL for up to 24 h. In control cultures, viability decreased 25% following exposure to 2 mM H 2 O 2 (1 h). However, no significant decrease in viability in cells pre‐treated with extract at concentrations as low as 1 µg/mL was observed. HSP70 mRNA levels were up‐regulated two‐fold in cell cultures treated with Rhodiolife (10 µg/mL), and expression was further enhanced by exposure to H 2 O 2 (six‐fold, p < 0.05). HSP70 protein levels were maintained in pre‐treated cell cultures compared to controls but was significantly lower (−50%) in cells lacking treatment exposed to H 2 O 2 . The present results indicate that Rhodiolife protects C 2 C 12 myotubes against peroxide‐induced oxidative stress through the modulation of the molecular chaperone HSP70. Copyright © 2013 John Wiley & Sons, Ltd.