Comparison of ryanodine binding to cardiac sarcoplasmic reticulum and nuclear envelope of rat / 中国应用生理学杂志
Chinese Journal of Applied Physiology
;
(6): 43-46, 2002.
Artículo
en Chino
| WPRIM
| ID: wpr-319385
ABSTRACT
<p><b>AIM</b>The characteristics of ryanodine receptor in rat cardiac sarcoplasmic reticulum (SR) and nuclear envelope (NE) were studied.</p><p><b>METHODS</b>Velocity and isopyknic gradient centrifugation was employed to fractionate rat SR and NE. Ryanodine receptor was assayed with [3H] ryanodine saturate binding to the preparations.</p><p><b>RESULTS</b>The maximal binding (Bmax) and dissociating constant (Kd) of ryanodine receptor in rat cardiac NE were, 1.7% and 60% of those in SR respectively. Phosphorylation in vitro by PKA and PKC increased Bmax of the receptors in SR by 372% and 121%, and augmented those in NE by 221% and 306%, without any effects on Kd.</p><p><b>CONCLUSION</b>Ryanodine receptors were present in rat myocardial NE, with lower density and higher affinity than those located in SR, which can be activated by PKA and PKC.</p>
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Fosforilación
/
Fisiología
/
Rianodina
/
Retículo Sarcoplasmático
/
Cinética
/
Calcio
/
Ratas Sprague-Dawley
/
Canal Liberador de Calcio Receptor de Rianodina
/
Metabolismo
/
Miocardio
Límite:
Animales
Idioma:
Chino
Revista:
Chinese Journal of Applied Physiology
Año:
2002
Tipo del documento:
Artículo
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