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A novel pancreatic beta-cell isoform of calcium/calmodulin-dependent protein kinase II (beta 3 isoform) contains a proline-rich tandem repeat in the association domain.
Urquidi, V; Ashcroft, S J.
Afiliação
  • Urquidi V; Nuffield Department of Clinical Biochemistry, John Radcliffe Hospital, Headington, Oxford, UK.
FEBS Lett ; 358(1): 23-6, 1995 Jan 16.
Article em En | MEDLINE | ID: mdl-7821422
ABSTRACT
There is evidence for a role for calcium/calmodulin-dependent protein phosphorylation in regulation of insulin secretion but the molecular nature of the kinase(s) responsible is unknown. In this study, the screening of a neonatal rat islet cDNA library resulted in the isolation of a 2 kb clone that was 99% homologous to the beta' isoform of calcium/calmodulin-dependent protein kinase II. The predicted 589 amino acid sequence with a calculated mass of 64,976 Da contained a 24 amino acid deletion in addition to the 15 amino acid deletion that differentiates the beta' from the beta isoform, and included an 86 amino acid novel domain consisting of a tandem repeat of proline-rich residues. The expression of this new isoform of calcium/calmodulin-dependent protein kinase II (beta 3) was confirmed in beta-cell lines and testis by DNA amplification of the sequence encoding the inserted domain by reverse transcriptase-polymerase chain reaction, followed by Southern analysis.
Assuntos
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Base de dados: MEDLINE Assunto principal: Sequências Repetitivas de Ácido Nucleico / Ilhotas Pancreáticas / Proteínas Quinases Dependentes de Cálcio-Calmodulina Tipo de estudo: Risk_factors_studies Limite: Animals Idioma: En Ano de publicação: 1995 Tipo de documento: Article
Buscar no Google
Base de dados: MEDLINE Assunto principal: Sequências Repetitivas de Ácido Nucleico / Ilhotas Pancreáticas / Proteínas Quinases Dependentes de Cálcio-Calmodulina Tipo de estudo: Risk_factors_studies Limite: Animals Idioma: En Ano de publicação: 1995 Tipo de documento: Article