Transient up-regulation of myotonic dystrophy protein kinase-binding protein, MKBP, and HSP27 in the neonatal myocardium

Citation
Km. Abu Shama et al., Transient up-regulation of myotonic dystrophy protein kinase-binding protein, MKBP, and HSP27 in the neonatal myocardium, CELL STRUCT, 24(1), 1999, pp. 1-4
Citations number
10
Categorie Soggetti
Cell & Developmental Biology
Journal title
CELL STRUCTURE AND FUNCTION
ISSN journal
03867196 → ACNP
Volume
24
Issue
1
Year of publication
1999
Pages
1 - 4
Database
ISI
SICI code
0386-7196(199902)24:1<1:TUOMDP>2.0.ZU;2-3
Abstract
Myotonic dystrophy protein kinase (DMPK)-binding protein, MKBP, has high ho mology with a small heat shock protein, HSP27. Western blotting analyses sh owed that MKBP level in rat heart rapidly increased, with a sharp peak at o ne week after birth (3-fold the level at the fetus), but that it rapidly de creased (1/10 of peak value at 13 weeks). Human myocardium also showed simi lar age-dependency. Similar but small increase of HSP27 was observed in the neonatal rat myocardium, but not in constitutive and inducible forms of HS P70. Immunofluorescence analysis localized MKBP at the Z lines and intercal ated discs in the rat myocardium. MKBP may protect actin cytoskeleton or ot her proteins of heart muscle against oxidative stress in the neonate.