Molecular Cloning and funcitional Analysis of pp115, which is a substrate of Insulin receptor Kinase
| Project/Area Number |
08457261
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
内分泌・代謝学
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| Research Institution | Shinshu University |
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Principal Investigator |
YAMAUCHI Keishi Shinshu University School of Medicine Department of Geratrics, Lecturor, 医学部・老年科, 講師 (30191191)
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| Co-Investigator(Kenkyū-buntansha) |
MIYAMOTO Takahide Shinshu University School of Medicine Department of Geratrics Assistant Professo, 医学部・附属病院, 助手 (20192768)
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| Project Period (FY) |
1996 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥5,700,000 (Direct Cost: ¥5,700,000)
Fiscal Year 1998: ¥800,000 (Direct Cost: ¥800,000)
Fiscal Year 1997: ¥2,900,000 (Direct Cost: ¥2,900,000)
Fiscal Year 1996: ¥2,000,000 (Direct Cost: ¥2,000,000)
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| Keywords | Insulin / pp115 / SH-PTP2 / SHPZ / ppll5 / SHPTP2 / pp115 / pp90 / Cas |
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| Research Abstract |
Immunoprecipitation of SHPTP2 from insulin- and EGF-stimulated cells demonstrated the co-immunoprecipitation of a diffuse tyrosine phosphorylated band in the 115 kDa protein region on Western blots of SDS-polyacrylamide gels. The tyrosine phosphorylation of pp115 was specific for insulin since activation of the platelet-derived growth factor receptor did not significantly increase the co-immunoprecipitation of tyrosine phosphorylated pp115. Although SHPTP2 was also found to associate with tyrosine phosphorylated IRS1, the majority of SHPTP2 appeared to be directly associated with pp115 following insulin stimulation. Further, expression of a wild type SHPTP2 and a catalytically inactive point mutant SHPTP2 (SHPTP2C/S) demonstrated the specific association with tyrosine phosphorylated pp115. In addition, expression of SHPTP2C/S resulted in a marked enhancement in the amount of co-immunoprecipitated tyrosine phosphorylated pp115.
These data demonstrate that insulin- and EGF-stimulated the tyrosine phosphorylation of a diffuse 115 kDa protein band which is the predominant in vivo SHPTP2 binding protein(s). These data further suggest that pp115 also functions as an in vivo substrate for the SHPTP2 activity.
Now, we try to make pp 115-specific antibody
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Report
(4 results)
Research Products
(4 results)
