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Science Forum Index » Life Extension Forum » simvastatin induces heat shock protein (HSP) 27, HSP70, and
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| kofi |
 Posted: Sat Jan 03, 2004 1:25 am |
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Arch Biochem Biophys. 2003 Jul 1;415(1):6-13. Related Articles, Links
Click here to read
Mechanism of simvastatin on induction of heat shock protein in
osteoblasts.
Wang X, Tokuda H, Hatakeyama D, Hirade K, Niwa M, Ito H, Kato K,
Kozawa O.
Department of Pharmacology, Gifu University School of Medicine, 40
Tsukasa-machi, Gifu-shi, Gifu-ken 500-8705, Japan.
It has recently been reported that 3-hydroxy-3-methylglutaryl
coenzyme A reductase inhibitors (statins) stimulate bone formation.
However, the mechanism of stimulation of bone metabolism by statins is
not precisely clarified. In this study, we investigated whether
simvastatin induces heat shock protein (HSP) 27, HSP70, and HSP90 in
osteoblast-like MC3T3-E1 cells. Simvastatin increased the levels of
HSP27 while having little effect on the levels of HSP70 or HSP90. The
effect of simvastatin on HSP27 accumulation was dose dependent.
Cycloheximide reduced the accumulation. Simvastatin induced an increase
in the levels of mRNA for HSP27. Actinomycin D suppressed the mRNA
levels. Simvastatin induced the phosphorylation of p38 mitogen-activated
protein (MAP) kinase among the MAP kinase superfamily. SB203580 and
PD169316, inhibitors of p38 MAP kinase, suppressed the HSP27
accumulation by simvastatin while SB202474, a negative control of p38
MAP kinase inhibitor, had no effect. SB203580 reduced the
simvastatin-increased mRNA levels for HSP27. Lovastatin, another statin,
also induced the HSP27 accumulation and SB203580 suppressed the HSP27
accumulation. These results strongly suggest that statins such as
simvastatin do not stimulate the induction of HSP70 and HSP90, but do
stimulate the induction of HSP27 in osteoblasts and that p38 MAP kinase
plays a role in this induction.
PMID: 12801507 [PubMed - indexed for MEDLINE] |
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