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Interaction between chicken protein tyrosine phosphatase 1 (CPTP1)-like rat protein phosphatase 1 (PTP1) and p60v-src in v-src-transformed Rat-1 fibroblasts
Article em En | WPRIM | ID: wpr-13040
Biblioteca responsável: WPRO
ABSTRACT
CPTP1 is a nontransmembrane chicken protein tyrosine phosphatase having 92% sequence homology to the corresponding 321 amino acids of human protein tyrosine phosphatase 1B (HPTP1B). Using anti-CPTP1 antibody, we identified CPTP1-like rat PTP1 of 51 kappa Da in Rat-1 and v-src-transformed Rat-1 fibroblasts. Here we show that CPTP1-like rat PTP1 binds to p60v-src in vivo and CPTP1 also can associate with p60v-src in cell lysate of v-src- transformed Rat-1 fibroblasts. Interaction between HPTP1B-type PTPs, CPTP1-like rat PTP1 and CPTP1, and p60v-src was reduced by vanadate treatment for 13 h due to down regulation of the protein level of p60v-src in vivo. Interestingly, CPTP1-like rat PTP1 was coimmunoprecipitated with a 70-kappa Da protein which has a possibility to be tyrosine- phosphorylated by p60v-src in v-src-transformed Rat- 1 fibroblasts. These results suggest that HPTP1B- type PTPs may play an important role in p60src dependent signal pathway in eucaryotic cells.
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Texto completo: 1 Base de dados: WPRIM Assunto principal: Ligação Proteica / Proteínas Recombinantes de Fusão / Testes de Precipitina / Linhagem Celular Transformada / Galinhas / Western Blotting / Proteína Oncogênica pp60(v-src) / Proteínas Tirosina Fosfatases / Fosfoproteínas Fosfatases / Fibroblastos Limite: Animals Idioma: En Revista: Experimental & Molecular Medicine Ano de publicação: 2002 Tipo de documento: Article
Texto completo: 1 Base de dados: WPRIM Assunto principal: Ligação Proteica / Proteínas Recombinantes de Fusão / Testes de Precipitina / Linhagem Celular Transformada / Galinhas / Western Blotting / Proteína Oncogênica pp60(v-src) / Proteínas Tirosina Fosfatases / Fosfoproteínas Fosfatases / Fibroblastos Limite: Animals Idioma: En Revista: Experimental & Molecular Medicine Ano de publicação: 2002 Tipo de documento: Article