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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Inhibition of phospholipase c-beta 1-mediated signaling by O-GlcNAc modification

Cited 14 times inthomson ciCited 14 times inthomson ci
Title
Inhibition of phospholipase c-beta 1-mediated signaling by O-GlcNAc modification
Author
Kim, YHSong, MOh, YSHeo, KChoi, JWPark, JMKim, SHLim, SKwon, H. MooRyu, SHSuh, Pann-Ghill
Keywords
LINKED N-ACETYLGLUCOSAMINE; PROTEIN-KINASE-C; INDUCED INSULIN-RESISTANCE; SKELETAL-MUSCLE; GLUCOSE-UPTAKE; NEONATAL CARDIOMYOCYTES; INOSITOL PHOSPHATES; FEEDBACK-REGULATION; CYTOSOLIC PROTEINS; 3T3-L1 ADIPOCYTES
Issue Date
200606
Publisher
WILEY-BLACKWELL
Citation
JOURNAL OF CELLULAR PHYSIOLOGY, v.207, no.3, pp.689 - 696
Abstract
Here we report inhibition of phospholipase C-beta 1 (PLC-beta 1)-mediated signaling by post-translational glycosylation with beta-N-acetylglucosamine (O-GIcNAc modification). In C2C12 myoblasts, isoform-specific knock-down experiments using siRNA showed that activation of bradykinin (BK) receptor led to Stimulation of PLC-beta 1 and subsequent intracellular Ca2+ mobilization. In C2C12 myotubes, O-GlcNAc modification of PLC-beta 1 was markedly enhanced in response to treatment with glucosamine (GIcNH(2)), an inhibitor of O-GIcNAase (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-beta 1 remained unchanged, these data suggest that O-GIcNAc modification of PLC-PI 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-GIcNAc modification negatively modulates the activity of PLC-beta 1.
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DOI
http://dx.doi.org/10.1002/jcp.20609
ISSN
0021-9541
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