Transient Up-regulation of Myotonic Dystrophy Protein Kinase-binding Protein, MKBP, and HSP27 in the Neonatal Myocardium.

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  • Mohammed Abu Shama Kazi
    Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi, Japan
  • Suzuki Atsushi
    Department of Molecular Biology, Yokohama City University School of Medicine, Kanazawa-ku, Yokohama, Kanagawa, Japan
  • Harada Kazuki
    Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi, Japan
  • Fujitani Noboru
    Department of Legal Medicine, Kurume University School of Medicine, Kurume, Fukuoka, Japan
  • Kimura Hiroshi
    Department of Legal Medicine, Kurume University School of Medicine, Kurume, Fukuoka, Japan
  • Ohno Shigeo
    Department of Molecular Biology, Yokohama City University School of Medicine, Kanazawa-ku, Yokohama, Kanagawa, Japan
  • Yoshida Ken-ichi
    Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi, Japan

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Myotonic dystrophy protein kinase (DMPK)-binding protein, MKBP, has high homology with a small heat shock protein, HSP27. Western blotting analyses showed that MKBP level in rat heart rapidly increased, with a sharp peak at one week after birth (3-fold the level at the fetus), but that it rapidly decreased (1/10 of peak value at 13 weeks). Human myocardium also showed similar age-dependency. Similar but small increase of HSP27 was observed in the neonatal rat myocardium, but not in constitutive and inducible forms of HSP70. Immunofluorescence analysis localized MKBP at the Z lines and intercalated discs in the rat myocardium. MKBP may protect actin cytoskeleton or other proteins of heart muscle against oxidative stress in the neonate.

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