The SH2 domain containing inositol 5-phosphatase SHIP2 controls phosphatidylinositol 3,4,5-trisphosphate levels in CHO-IR cells stimulated by insulin
| Autor: | Daniel Blero, Christophe Erneux, Nathalie Paternotte, Bernard Payrastre, Colette Moreau, Florence De Smedt, Xavier Pesesse |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
medicine.medical_specialty
medicine.medical_treatment Biophysics Gene Expression CHO Cells Protein Serine-Threonine Kinases Transfection Biochemistry src Homology Domains chemistry.chemical_compound Phosphatidylinositol Phosphates Internal medicine Insulin receptor substrate Cricetinae Proto-Oncogene Proteins medicine Animals Insulin Inositol Phosphorylation Molecular Biology Protein kinase B biology Phosphatidylinositol (3 4 5)-trisphosphate GRB10 Cell Biology IRS2 Phosphoric Monoester Hydrolases Receptor Insulin Insulin receptor Endocrinology chemistry Phosphatidylinositol-3 4 5-Trisphosphate 5-Phosphatases biology.protein Tyrosine Mitogen-Activated Protein Kinases Proto-Oncogene Proteins c-akt |
| Zdroj: | Biochemical and biophysical research communications. 282(3) |
| ISSN: | 0006-291X |
| Popis: | The lipid phosphatase SHIP2 (SH2 domain containing inositol 5-phosphatase 2) has recently been shown to be a potent negative regulator of insulin signaling and insulin sensitivity in vivo. We show here that SHIP2 is expressed in Chinese hamster ovary cells overexpressing the insulin receptor (CHO-IR cells) and tyrosine phosphorylated upon insulin stimulation. We show that SHIP2, which is recruited in anti-phosphotyrosine immunoprecipitates in insulin-stimulated cells, accounts for the insulin sensitivity or apparent increase in activity reported by Guilherme et al. (J. Biol. Chem. 271, 29533-29536, 1996). Overexpression of SHIP2 led to a decrease of the insulin-dependent PIP3 production as well as Akt/PKB activation and MAPK stimulation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect