Effects of overexpressing wild-type and mutant PDGF receptors on translocation of GLUT4 in transfected rat adipose cells

Autor: Hui Chen, Brian L. Ing, Samuel W. Cushman, Simeon I. Taylor, Andrius Kazlauskas, Lixin Zhou, Michael J. Quon, Richard A. Klinghoffer, Chung H. Lin, Mary Jane Zarnowski
Rok vydání: 1996
Předmět:
Male
Monosaccharide Transport Proteins
medicine.medical_treatment
Biophysics
Adipose tissue
Muscle Proteins
Biology
Transfection
Biochemistry
Wortmannin
Receptor
Platelet-Derived Growth Factor beta
chemistry.chemical_compound
Epitopes
Phosphatidylinositol 3-Kinases
medicine
Animals
Humans
Insulin
Point Mutation
Receptors
Platelet-Derived Growth Factor
Cloning
Molecular
Phosphorylation
Receptor
Molecular Biology
PI3K/AKT/mTOR pathway
Sequence Tagged Sites
Epididymis
Platelet-Derived Growth Factor
Glucose Transporter Type 4
Cell Membrane
Cell Biology
Molecular biology
Recombinant Proteins
Rats
Phosphotransferases (Alcohol Group Acceptor)
chemistry
Adipose Tissue
biology.protein
Mutagenesis
Site-Directed
Protein Processing
Post-Translational
hormones
hormone substitutes
and hormone antagonists
Platelet-derived growth factor receptor
GLUT4
Zdroj: Biochemical and biophysical research communications. 226(3)
ISSN: 0006-291X
Popis: Activation of phosphatidylinositol 3-kinase (PI3K) by insulin is necessary for the effect of insulin to recruit GLUT4 to the cell surface in insulin target cells. In adipose cells, stimulation of endogenous PDGF receptors (PDGF-R) results in increased PI3K activity without causing recruitment of GLUT4. We overexpressed wild-type or mutant forms of the PDGF-R in rat adipose cells and examined their effects on PDGF- and insulin-stimulated recruitment of co-transfected epitope-tagged GLUT4. Control cells expressing only tagged GLUT4 had a 3-fold increase in cell surface GLUT4 upon insulin stimulation but no response to PDGF. Cells overexpressing wild-type PDGF-R maintained insulin responsiveness and, in addition, acquired the ability to recruit GLUT4 in response to PDGF. Surprisingly, overexpression of F740/F751 (mutant PDGF-R unable to directly activate PI3K) led to similar results. Nevertheless, wortmannin (an inhibitor of PI3K) blocked effects of both PDGF and insulin to recruit GLUT4. Our data suggest that overexpression of PDGF-R mediates positive effects on GLUT4 translocation by a wortmannin sensitive pathway not dependent on direct interaction of the PDGF-R with PI3K.
Databáze: OpenAIRE
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