The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Purification of a 72-kDa Protein-Tyrosine Kinase from Rat Liver and Its Identification as Syk: Involvement of Syk in Signaling Events of Hepatocytes
Shinobu TsuchidaShigeru YanagiRyoko InatomeJunyi DingPatrice HermannToshiaki TsujimuraNobuzo MatsuiHirohei Yamamura
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2000 Volume 127 Issue 2 Pages 321-327

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Abstract
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 liverderived 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-proteincoupled receptors. This is the first report of the expression of Syk in non-hematopoietic tissue.
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© The Japanese Biochemical Society
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