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2016 ; 11
(9
): e0162658
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Glutaminolysis Was Induced by TGF-?1 through PP2Ac Regulated Raf-MEK-ERK
Signaling in Endothelial Cells
#MMPMID27612201
Guo Y
; Deng Y
; Li X
; Ning Y
; Lin X
; Guo S
; Chen M
; Han M
PLoS One
2016[]; 11
(9
): e0162658
PMID27612201
show ga
Vascular endothelial cells can survive under hypoxic and inflammatory conditions
by alterations of the cellular energy metabolism. In addition to high rates of
glycolysis, glutaminolysis is another important way of providing the required
energy to support cellular sprouting in such situations. However, the exact
mechanism in which endothelial cells upregulate glutaminolysis remains unclear.
Here we demonstrated that protein phosphatase 2A (PP2A)-mediated Raf-MEK-ERK
signaling was involved in glutaminolysis in endothelial cells. Using models of
human umbilical vein endothelial cells (HUVECs) treated with transforming growth
factor-?1 (TGF-?1), we observed a dramatic induction in cellular glutamate levels
accompanied by Raf-MEK-ERK activation. By addition of U0126, the specific
inhibitor of MEK1/2, the expression of kidney-type glutaminase (KGA, a critical
glutaminase in glutaminolysis) was significantly decreased. Moreover, inhibition
of PP2A by okadaic acid (OA), a specific inhibitor of PP2A phosphatase activity
or by depletion of its catalytic subunit (PP2Ac), led to a significant
inactivation of Raf-MEK-ERK signaling and reduced glutaminolysis in endothelial
cells. Taken together, these results indicated that PP2A-dependent Raf-MEK-ERK
activation was involved in glutaminolysis and inhibition of PP2A signals was
sufficient to block Raf-MEK-ERK pathway and reduced glutamine metabolism in
endothelial cells.