Wnt-1 regulation of connexin43 in cardiac myocytes
نویسندگان
چکیده
منابع مشابه
Wnt-1 regulation of connexin43 in cardiac myocytes.
Gap junction channels composed of connexin43 (Cx43) are essential for normal heart formation and function. We studied the potential role of the Wnt family of secreted polypeptides as regulators of Cx43 expression and gap junction channel function in dissociated myocytes and intact hearts. Neonatal rat cardiomyocytes responded to Li(+), which mimics Wnt signaling, by accumulating the effector pr...
متن کاملImpulse propagation in synthetic strands of neonatal cardiac myocytes with genetically reduced levels of connexin43.
Connexin43 (Cx43) is a major determinant of the electrical properties of the myocardium. Closure of gap junctions causes rapid slowing of propagation velocity (theta), but the precise effect of a reduction in Cx43 levels due to genetic manipulation has only partially been clarified. In this study, morphological and electrical properties of synthetic strands of cultured neonatal ventricular myoc...
متن کاملConnexin43 Hemichannel-Mediated Regulation of Connexin43
BACKGROUND Many signaling molecules and pathways that regulate gap junctions (GJs) protein expression and function are, in fact, also controlled by GJs. We, therefore, speculated an existence of the GJ channel-mediated self-regulation of GJs. Using a cell culture model in which nonjunctional connexin43 (Cx43) hemichannels were activated by cadmium (Cd(2+)), we tested this hypothesis. PRINCIPA...
متن کاملProteolysis of connexin43-containing gap junctions in normal and heat-stressed cardiac myocytes.
OBJECTIVE The present studies were performed to examine the degradation of connexin43-containing gap junctions by the lysosome or the proteasome in normal and heat-stressed cultures of neonatal rat ventricular myocytes. METHODS Primary cultures were prepared from neonatal rat ventricular myocytes. Connexin43 was detected by immunoblotting, immunofluorescence, or immunoprecipitation. Gap junct...
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Calmodulin (CaM) as a ubiquitous Ca2+ sensor interacts with multiple key molecules involved in excitation-contraction (EC) coupling. In the present study, we report that adenoviral expression of a mutant CaM lacking all of its four Ca2+-binding sites, CaM(1-4), at a level 6.5-fold over endogenous CaM markedly increases the amplitude and abbreviates the decay time of Ca2+ transients and contract...
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ژورنال
عنوان ژورنال: Journal of Clinical Investigation
سال: 2000
ISSN: 0021-9738
DOI: 10.1172/jci7798