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2015 ; 14
(10
): 1559-67
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IGF1 regulates PKM2 function through Akt phosphorylation
#MMPMID25790097
Salani B
; Ravera S
; Amaro A
; Salis A
; Passalacqua M
; Millo E
; Damonte G
; Marini C
; Pfeffer U
; Sambuceti G
; Cordera R
; Maggi D
Cell Cycle
2015[]; 14
(10
): 1559-67
PMID25790097
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Pyruvate kinase M2 (PKM2) acts at the crossroad of growth and metabolism pathways
in cells. PKM2 regulation by growth factors can redirect glycolytic intermediates
into key biosynthetic pathway. Here we show that IGF1 can regulate glycolysis
rate, stimulate PKM2 Ser/Thr phosphorylation and decrease cellular pyruvate
kinase activity. Upon IGF1 treatment we found an increase of the dimeric form of
PKM2 and the enrichment of PKM2 in the nucleus. This effect was associated to a
reduction of pyruvate kinase enzymatic activity and was reversed using metformin,
which decreases Akt phosphorylation. IGF1 induced an increased nuclear
localization of PKM2 and STAT3, which correlated with an increased HIF1?, HK2,
and GLUT1 expression and glucose entrapment. Metformin inhibited HK2, GLUT1,
HIF-1? expression and glucose consumption. These findings suggest a role of
IGFIR/Akt axis in regulating glycolysis by Ser/Thr PKM2 phosphorylation in cancer
cells.
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