TY - JOUR
T1 - Hepatic tyrosine-phosphorylated proteins identified and localized following in vivo inhibition of protein tyrosine phosphatases
T2 - effects of H2O2 and vanadate administration into rat livers
AU - Hadari, Yaron R.
AU - Geiger, Benjamin
AU - Nadiv, Orna
AU - Sabanay, Ilana
AU - Roberts, Charles T.
AU - LeRoith, Derek
AU - Zick, Yehiel
N1 - Funding Information:
We thank Drs. Ronit Sagi-Eisenberga nd Simeon I. Taylor and Mrs. Yael Biener for helpful discussions and a critical review of this manuscript.W e thank Ruth Dror and Tova Volberg for excellent technical assistanceT. his work was supportedb y grantsf rom the Israel Cancer ResearchF und, the Israel Cancer Association, the Juvenile Diabetes Foundation International (to Y.Z.) and the Minerva Foundation (to B.G.). Y.Z. is the incumbento f the Philip Harris and Gerald Ronson Career Development Chair in Diabetes Research. D.L. is the Erna and Jacob Michael Visiting Professor at the WeizmannI nstitute of Science.B .G is E. Neter Professor for cell and tumor biology.
PY - 1993/11
Y1 - 1993/11
N2 - Injection of a combination of H2O2 and vanadate (H/V) into the portal vein of rat livers resulted in inhibition of protein tyrosine phosphatase activity and led to a dramatic enhanced in vivo protein tyrosine phosphorylation. Some of the phosphorylated proteins were identified as the β-subunit of the insulin receptor, the insulin receptor substrate 1 (ppl85), PLC-γ (pp145), and a 100 kDa PLC-γ-associated protein. Immunofluorescense and immune electron microscopy of frozen liver sections with anti-P-Tyr antibodies revealed that most of the tyrosine-phosphorylated proteins are localized in close proximity to the plasma membrane in intercellular adherence junctions and tight junction regions. This close in vivo association between membranal protein tyrosine kinases, their target proteins, and cytoskeletal elements could enable formation of 'signaling complexes' which may play a role in transmembrane signal transduction. By affinity chromatography over immobilized anti-P-Tyr antibodies, a large number of these tyrosine-phosphorylated proteins were partially purified.
AB - Injection of a combination of H2O2 and vanadate (H/V) into the portal vein of rat livers resulted in inhibition of protein tyrosine phosphatase activity and led to a dramatic enhanced in vivo protein tyrosine phosphorylation. Some of the phosphorylated proteins were identified as the β-subunit of the insulin receptor, the insulin receptor substrate 1 (ppl85), PLC-γ (pp145), and a 100 kDa PLC-γ-associated protein. Immunofluorescense and immune electron microscopy of frozen liver sections with anti-P-Tyr antibodies revealed that most of the tyrosine-phosphorylated proteins are localized in close proximity to the plasma membrane in intercellular adherence junctions and tight junction regions. This close in vivo association between membranal protein tyrosine kinases, their target proteins, and cytoskeletal elements could enable formation of 'signaling complexes' which may play a role in transmembrane signal transduction. By affinity chromatography over immobilized anti-P-Tyr antibodies, a large number of these tyrosine-phosphorylated proteins were partially purified.
KW - HO-vanadate
KW - Protein tyrosine kinase
KW - Tyrosine phosphorylation (Rat liver)
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U2 - 10.1016/0303-7207(93)90206-Y
DO - 10.1016/0303-7207(93)90206-Y
M3 - Article
C2 - 8143908
AN - SCOPUS:0027451409
SN - 0303-7207
VL - 97
SP - 9
EP - 17
JO - Molecular and Cellular Endocrinology
JF - Molecular and Cellular Endocrinology
IS - 1-2
ER -