Cell Structure and Function | |
Transient Up-regulation of Myotonic Dystrophy Protein Kinase-binding Protein, MKBP, and HSP27 in the Neonatal Myocardium | |
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
【 预 览 】
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RO201912080704803ZK.pdf | 333KB | download |