Key result
MKBP levels in rat and human myocardium rapidly increased to peak at one week after birth (3-fold fetal levels) before rapidly decreasing by 13 weeks, localizing at Z lines and intercalated discs.
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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Shama et al. (1999) studied Neonatal myocardium development. Neonatal developmental stage vs. Fetal and adult developmental stages was evaluated on MKBP and HSP27 protein levels. MKBP levels in rat and human myocardium rapidly increased to peak at one week after birth (3-fold fetal levels) before rapidly decreasing by 13 weeks, localizing at Z lines and intercalated discs.
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