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

Cell Structure and Function

Atsushi Suzuki³  Kazuki Harada²  Noboru Fujitani¹  Shigeo Ohno³  Hiroshi Kimura¹  Kazi Mohammed Abu Shama²  Ken-ichi Yoshida² 

[1] Department of Legal Medicine, Kurume University School of Medicine, Kurume, Fukuoka, Japan;Department of Legal Medicine, Yamaguchi University School of Medicine, Ube, Yamaguchi, Japan;Department of Molecular Biology, Yokohama City University School of Medicine, Kanazawa-ku, Yokohama, Kanagawa, Japan

关键词: myotonic dystrophy protein kinase-binding protein;    heat shock protein 27;    myocardium;    age-dependency;    oxidative stress;   

DOI  :  10.1247/csf.24.1

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(10)Cited-By(12)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.

【 授权许可】

Unknown