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Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes.

Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Research Abstract Details 

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  • Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Abstract Text:

    s tsuchidaS Tsuchida,s yanagiS Yanagi,r inatomeR Inatome,j dingJ Ding,p hermannP Hermann,t tsujimuraT Tsujimura,n matsuiN Matsui,h yamamuraH Yamamura,

    Syk protein-tyrosine kinase (PTK) has been implicated in a variety of hematopoietic cell responses including immunoreceptor signaling. However, so far, there has been no evidence of the expression of Syk or Syk-related PTK in non-hematopoietic tissues. In this study, we have purified from blood cell-depleted rat liver a 72-kDa cytoplasmic PTK which shows cross-reactivity with anti-Syk antibody. Partial amino acid sequence analysis revealed that this 72-kDa PTK is identical to Syk. Immunohistochemical and RT-PCR analyses demonstrated that Syk is expressed in human hepatocytes and two rat liver-derived cell lines, JTC-27 and RLC-16. Furthermore, Syk is significantly tyrosine-phosphorylated in response to angiotensin II in JTC-27 cells, and angiotensin II-induced MAP kinase activation is blocked by the treatment of cells with a Syk-selective inhibitor, piceatannol. These results suggest that Syk plays an important role in signaling events of hepatocytes, such as signaling steps leading to MAP kinase activation by G-protein-coupled receptors. This is the first report of the expression of Syk in non-hematopoietic tissue.

    Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Publishing Authors By Initials

    s tsuchidaS Tsuchida,s yanagiS Yanagi,r inatomeR Inatome,j dingJ Ding,p hermannP Hermann,t tsujimuraT Tsujimura,n matsuiN Matsui,h yamamuraH Yamamura,

    For similar organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: benzene derivatives: benzylidene compounds: stilbenes research abstracts see: organic chemicals: hydrocarbons: hydrocarbons, cyclic: hydrocarbons, aromatic: benzene derivatives: benzylidene compounds: stilbenes research

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    Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Journal of biochemistry

    VOLUME: 127

    Page Numbers: 321-7

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Feb

    YEAR: 2000

    Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Keywords Mesh Terms:

    KEYWORDS: Stilbenes

    MESH TERMS: pharmacology

    Chemical & Substance for Abstract: Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes. Information

    Substance Name: GTP-Binding Proteins

    Registry Number: EC 3.6.1.-

    Grant and Affiliation Information for Purification of a 72-kDa protein-tyrosine kinase from rat liver and its identification as Syk: involvement of Syk in signaling events of hepatocytes.

    AFFILIATION: Department of Biochemistry, Kobe University School of Medicine, Chuo-ku, Kobe 650-0017, Japan.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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