Regulation of GLUT1-mediated glucose uptake by PKClambda-PKCbeta(II) interactions in 3T3-L1 adipocytes
| Autor: | Merlijn Bazuine, J. Antonie Maassen, Remko R. Bosch, Cees J. Tack, Ad R. M. M. Hermus, Paul N. Span, André J. Olthaar, Helga van Rennes, Peter H.G.M. Willems, C.G.J. Sweep |
|---|---|
| Přispěvatelé: | Other departments |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Snf3
Monosaccharide Transport Proteins Glucose uptake Molecular Sequence Data Vascular medicine and diabetes [UMCN 2.2] Mitogen-activated protein kinase kinase Myristic Acid Biochemistry Cell Line Mice 3T3-L1 Cells Protein Kinase C beta Adipocytes Animals Immunoprecipitation Amino Acid Sequence Enzyme Inhibitors Protein kinase A Molecular Biology Protein Kinase C Protein kinase C Mitogen-Activated Protein Kinase Kinases Glucose Transporter Type 1 biology Endocrinology and reproduction [UMCN 5.2] Glucose transporter Cell Biology Cell biology Enzyme Activation Isoenzymes Glucose biology.protein Tetradecanoylphorbol Acetate GLUT1 Peptides Cellular energy metabolism [UMCN 5.3] Research Article |
| Zdroj: | Biochemical journal, 384(Part 2), 349-355. Portland Press Ltd. Biochemical Journal, 384, 349-55 Biochemical Journal, 384, Pt 2, pp. 349-55 |
| ISSN: | 0264-6021 |
| DOI: | 10.1042/bj20040797 |
| Popis: | Contains fulltext : 57749.pdf (Publisher’s version ) (Open Access) Members of the PKC (protein kinase C) superfamily play key regulatory roles in glucose transport. How the different PKC isotypes are involved in the regulation of glucose transport is still poorly defined. PMA is a potent activator of conventional and novel PKCs and PMA increases the rate of glucose uptake in many different cell systems. In the present study, we show that PMA treatment increases glucose uptake in 3T3-L1 adipocytes by two mechanisms: a mitogen-activated protein kinase kinase-dependent increase in GLUT1 (glucose transporter 1) expression levels and a PKClambda-dependent translocation of GLUT1 towards the plasma membrane. Intriguingly, PKClambda co-immunoprecipitated with PKCbeta(II) and did not with PKCbeta(I). Previously, we have described that down-regulation of PKCbeta(II) protein levels or inhibiting PKCbeta(II) by means of the myristoylated PKCbetaC2-4 peptide inhibitor induced GLUT1 translocation towards the plasma membrane in 3T3-L1 adipocytes. Combined with the present findings, these results suggest that the liberation of PKClambda from PKCbeta(II) is an important factor in the regulation of GLUT1 distribution in 3T3-L1 adipocytes. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|