KCNE2 protein S98 phosphorylation in heart of old SHR rats detected by point mutagenesis / 浙江大学学报·医学版
Zhejiang Daxue xuebao. Yixue ban
; (6): 364-370, 2007.
Article
en Zh
| WPRIM
| ID: wpr-271520
Biblioteca responsable:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To investigate the phosphorylation of KCNE2 protein in heart of old SHR rats.</p><p><b>METHODS</b>The membrane proteins from ventricular myocardium of old SHR were extracted, treated with or without alkaline phosphatase and tested binding with Ab2 (an anti-KCNE2 polyclonal antibody) by Western blot. A KCNE2 fusion protein with c-myc was obtained from in vitro translation system and treated with or without alkaline phosphatase. A series of mono- and double-point mutated fusion KCNE2 proteins with c-myc were obtained from an in vitro translation system, and Western blots with Ab2 or anti-myc antibody were performed.</p><p><b>RESULTS</b>After alkaline phosphatase treatment, Ab2 significantly attenuated its binding with KCNE2. In vitro translation system confirmed that after alkaline phosphatase treatment, Ab2 weakened binding ability to KCNE2 while binding to c-myc was not changed. Point mutation experiments showed that serine residue in position 98 of KCNE2 proteins might be phosphorylated.</p><p><b>CONCLUSION</b>KCNE2 protein in heart of old SHR rats is phosphorylated and this phosphorylation takes place in serine residue of position 98.</p>
Texto completo:
1
Base de datos:
WPRIM
Asunto principal:
Fosforilación
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Unión Proteica
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Ratas Endogámicas SHR
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Proteínas Recombinantes de Fusión
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Envejecimiento
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Western Blotting
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Proteínas Proto-Oncogénicas c-myc
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Mutación Puntual
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Canales de Potasio con Entrada de Voltaje
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Genética
Límite:
Animals
Idioma:
Zh
Revista:
Zhejiang Daxue xuebao. Yixue ban
Año:
2007
Tipo del documento:
Article