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Experimental & Molecular Medicine ; : 509-518, 2006.
Article in English | WPRIM | ID: wpr-69447

ABSTRACT

Angiotensin II (Ang II), which is an important mediator of both vascular responsiveness and growth, has been shown to induce vascular smooth muscle cell (VSMC) hypertrophy via the activation of a complex series of intracellular signaling events. Heat shock protein 70 (Hsp70) has recently been shown to protect against Ang II-induced hypertension. In this study, we tested the hypothesis that Hsp70 can protect VSMC from Ang II-induced hypertrophy. We treated VSMCs with Ang II to induce hypertrophy and to activate MAPK signaling pathway. We observed that the augmentation of Hsp70 expression inhibited Ang II-stimulated VSMC hypertrophy. This inhibitory effect of Hsp70 appears to be partly due to extracellular signal-regulated kinase (ERK1/2) inactivation, which in turn, may possibly result from the accumulation of MAP kinase phosphatase-1 (MKP-1).


Subject(s)
Rats , Male , Animals , Rats, Sprague-Dawley , RNA, Small Interfering/pharmacology , Protein Tyrosine Phosphatases/metabolism , Phosphoprotein Phosphatases/metabolism , Muscle, Smooth, Vascular/cytology , Mitogen-Activated Protein Kinase 3/antagonists & inhibitors , Mitogen-Activated Protein Kinase 1/antagonists & inhibitors , MAP Kinase Kinase 2/metabolism , MAP Kinase Kinase 1/metabolism , Immediate-Early Proteins/metabolism , Hypertrophy , HSP70 Heat-Shock Proteins/antagonists & inhibitors , Flavonoids/pharmacology , Enzyme Stability/drug effects , Cells, Cultured , Cell Cycle Proteins/metabolism , Aorta/drug effects , Angiotensin II/pharmacology
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