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Inhibition of phospholipase C-β1-mediated signaling by O-GlcNAc modification.
- Source :
-
Journal of Cellular Physiology . Jun2006, Vol. 207 Issue 3, p689-696. 8p. 6 Graphs. - Publication Year :
- 2006
-
Abstract
- Here we report inhibition of phospholipase C-β1 (PLC-β1)-mediated signaling by post-translational glycosylation with β-N-acetylglucosamine (O-GlcNAc modification). In C2C12 myoblasts, isoform-specific knock-down experiments using siRNA showed that activation of bradykinin (BK) receptor led to stimulation of PLC-β1 and subsequent intracellular Ca2+ mobilization. In C2C12 myotubes, O-GlcNAc modification of PLC-β1 was markedly enhanced in response to treatment with glucosamine (GlcNH2), an inhibitor of O-GlcNAase (PUGNAc) and hyperglycemia. This was associated with more than 50% inhibition of intracellular production of IP3 and Ca2+ mobilization in response to BK. Since the abundance of PLC-β1 remained unchanged, these data suggest that O-GlcNAc modification of PLC-β1 led to inhibition of its activity. Moreover, glucose uptake stimulated by BK was significantly blunted by treatment with PUGNAc. These data support the notion that O-GlcNAc modification negatively modulates the activity of PLC-β1. J. Cell. Physiol. © 2006 Wiley-Liss, Inc. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00219541
- Volume :
- 207
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Journal of Cellular Physiology
- Publication Type :
- Academic Journal
- Accession number :
- 21619780
- Full Text :
- https://doi.org/10.1002/jcp.20609