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10.1080/15384101.2015.1026490 http://scihub22266oqcxt.onion/10.1080/15384101.2015.1026490 C4612106!4612106!25790097     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Cycle 2015 ; 14 (10): 1559-67 Nephropedia Template TP {{tp|p=25790097|t=2015. IGF1 regulates PKM2 function through Akt phosphorylation |pdf=|usr=}}{{25790097}} gab.com Text IGF1 regulates PKM2 function through Akt phosphorylation JO: Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=25790097 #FOAvip 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. Twit Text FOAVip IGF1 regulates PKM2 function through Akt phosphorylation ????Cell Cycle http://www.kidney.de/pget.php?&tw=1&pmid=25790097 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25790097 #FOAvip English Wikipedia <ref>{{Cite pmid|25790097}}</ref> 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[May]; 14 (10): 1559-67 PMID25790097show ga 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. äIGF1 regulates PKM2 function through Akt phosphorylation (epmc).pdf DeepDyve Pubget Overpricing