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Vol. 291, Issue 3, 967-975, December 1999
Todd Franklin Cardiac Research Laboratory, Children's Heart
Center, Department of Pediatrics, Emory University School of Medicine,
Atlanta, Georgia
We previously showed that stimulation of cGMP-dependent protein kinase
(PKG) stimulates L-type calcium current in newborn but not in adult
rabbit ventricular myocytes. We have now isolated rabbit PKG type I
cDNA (+1 to 2095), determined the sequence, and analyzed specific
expression of PKG in adult and newborn rabbit heart by Western and
Northern analyses to elucidate the developmental decline in the
significance of PKG in cardiac function. We obtained full-length cDNA
of PKG I from newborn rabbit heart mRNA with reverse
transcription-polymerase chain reaction. The coding region of rabbit
PKG I showed 94% homology to sequences of human and bovine PKG
I. The deduced amino acid sequence of 671 amino acids showed seven
substitutions between rabbit and either human or bovine PKG I. The
major substitutions were found in the cGMP-binding domain. The cloned
PKG 1 cDNA was expressed in COS cells. Expressed PKG showed cGMP
stimulated PKG activity and immunoreactivity. Northern blot analysis of
cardiac tissue demonstrated PKG I mRNA of 6.8 kb, with much higher
levels in newborn than in adult cells. Western analysis in homogenates
from ventricular tissues and isolated ventricular myocytes of rabbit
heart showed much higher expression of PKG type I protein in newborn
compared with adult cells. These findings suggest that PKG is
developmentally regulated in rabbit heart and is expressed at a much
higher level in newborn than in adult cells. The greater expression of
PKG in newborn cells could be responsible for differences in the
significance of cGMP in adult and newborn rabbit cells.
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