Translocation of HSP27 and MKBP in Ischemic Heart

Ken-ichi Yoshida; Toshihiko Aki; Kazuki Harada; Kazi M.A. Shama; Yasuhisa Kamoda; Atsushi Suzuki; Shigeo Ohno

doi:10.1247/csf.24.181

REGULAR ARTICLES

Translocation of HSP27 and MKBP in Ischemic Heart

Ken-ichi Yoshida, Toshihiko Aki, Kazuki Harada, Kazi M.A. Shama, Yasuhisa Kamoda, Atsushi Suzuki, Shigeo Ohno

Author information

Ken-ichi Yoshida
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505, Japan
Department of Legal Medicine, Graduate School of Medicine, University of Tokyo, Tokyo 113-0033, Japan
Toshihiko Aki
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505, Japan
Kazuki Harada
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505, Japan
Kazi M.A. Shama
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505, Japan
Yasuhisa Kamoda
Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi 755-8505, Japan
Atsushi Suzuki
Department of Molecular Biology, Yokohama City University School of Medicine, Yokohama, Kanagawa 236-0004, Japan
Shigeo Ohno
Department of Molecular Biology, Yokohama City University School of Medicine, Yokohama, Kanagawa 236-0004, Japan

Keywords: HSP27, MKBP, translocation, ischemia, myofibril, oxidative stress

JOURNAL FREE ACCESS

1999 Volume 24 Issue 4 Pages 181-185

DOI https://doi.org/10.1247/csf.24.181

Details

Abstract

HSP27 and MKBP translocate from the cytosolic to myofibril fraction in ischemic rat heart as demonstrated by immunoblotting. Immunohistochemistry analysis showed that ischemia enhances the Z line labeling of HSP27 and MKBP. Two dimensional gel electrophoresis showed that ischemia increases the hyperphosphorylated form of HSP27. These data suggest that HSP27 and MKBP may be involved in the Z line protection against postischemic reperfusion injury.

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