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10.1161/ATVBAHA.113.303041 http://scihub22266oqcxt.onion/10.1161/ATVBAHA.113.303041 C4120754!4120754 !24700124     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24700124 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Arterioscler+Thromb+Vasc+Biol 2014 ; 34 (6 ): 1231-9 Nephropedia Template TP {{tp|p=24700124 |t=2014. Endothelial PFKFB3 plays a critical role in angiogenesis |pdf=|usr=}}{{24700124 }} gab.com Text Endothelial PFKFB3 plays a critical role in angiogenesis JO: Arterioscler Thromb Vasc Biol http://www.kidney.de/pget.php?&tw=1&pmid=24700124 #FOAvip OBJECTIVE: Vascular cells, particularly endothelial cells, adopt aerobic glycolysis to generate energy to support cellular functions. The effect of endothelial glycolysis on angiogenesis remains unclear. 6-Phosphofructo-2-kinase/fructose-2, 6-bisphosphatase, isoform 3 (PFKFB3) is a critical enzyme for endothelial glycolysis. By blocking or deleting PFKFB3 in endothelial cells, we investigated the influence of endothelial glycolysis on angiogenesis both in vitro and in vivo. APPROACH AND RESULTS: Under hypoxic conditions or after treatment with angiogenic factors, endothelial PFKFB3 was upregulated both in vitro and in vivo. The knockdown or overexpression of PFKFB3 suppressed or accelerated endothelial proliferation and migration in vitro, respectively. Neonatal mice from a model of oxygen-induced retinopathy showed suppressed neovascular growth in the retina when endothelial PFKFB3 was genetically deleted or when the mice were treated with a PFKFB3 inhibitor. In addition, tumors implanted in mice deficient in endothelial PFKFB3 grew more slowly and were provided with less blood flow. A lower level of phosphorylated protein kinase B was observed in PFKFB3-knockdown endothelial cells, which was accompanied by a decrease in intracellular lactate. The addition of lactate to PFKFB3-knockdown cells rescued the suppression of endothelial proliferation and migration. CONCLUSIONS: The blockade or deletion of endothelial PFKFB3 decreases angiogenesis both in vitro and in vivo. Thus, PFKFB3 is a promising target for the reduction of endothelial glycolysis and its related pathological angiogenesis. Twit Text FOAVip Endothelial PFKFB3 plays a critical role in angiogenesis ????Arterioscler Thromb Vasc Biol http://www.kidney.de/pget.php?&tw=1&pmid=24700124 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24700124 #FOAvip English Wikipedia <ref>{{Cite pmid|24700124 }}</ref> Endothelial PFKFB3 plays a critical role in angiogenesis #MMPMID24700124 Xu Y ; An X ; Guo X ; Habtetsion TG ; Wang Y ; Xu X ; Kandala S ; Li Q ; Li H ; Zhang C ; Caldwell RB ; Fulton DJ ; Su Y ; Hoda MN ; Zhou G ; Wu C ; Huo Y Arterioscler Thromb Vasc Biol 2014[Jun]; 34 (6 ): 1231-9 PMID24700124 show ga OBJECTIVE: Vascular cells, particularly endothelial cells, adopt aerobic glycolysis to generate energy to support cellular functions. The effect of endothelial glycolysis on angiogenesis remains unclear. 6-Phosphofructo-2-kinase/fructose-2, 6-bisphosphatase, isoform 3 (PFKFB3) is a critical enzyme for endothelial glycolysis. By blocking or deleting PFKFB3 in endothelial cells, we investigated the influence of endothelial glycolysis on angiogenesis both in vitro and in vivo. APPROACH AND RESULTS: Under hypoxic conditions or after treatment with angiogenic factors, endothelial PFKFB3 was upregulated both in vitro and in vivo. The knockdown or overexpression of PFKFB3 suppressed or accelerated endothelial proliferation and migration in vitro, respectively. Neonatal mice from a model of oxygen-induced retinopathy showed suppressed neovascular growth in the retina when endothelial PFKFB3 was genetically deleted or when the mice were treated with a PFKFB3 inhibitor. In addition, tumors implanted in mice deficient in endothelial PFKFB3 grew more slowly and were provided with less blood flow. A lower level of phosphorylated protein kinase B was observed in PFKFB3-knockdown endothelial cells, which was accompanied by a decrease in intracellular lactate. The addition of lactate to PFKFB3-knockdown cells rescued the suppression of endothelial proliferation and migration. CONCLUSIONS: The blockade or deletion of endothelial PFKFB3 decreases angiogenesis both in vitro and in vivo. Thus, PFKFB3 is a promising target for the reduction of endothelial glycolysis and its related pathological angiogenesis. |Animals [MESH] |Cell Proliferation [MESH] |Cells, Cultured [MESH] |Endothelial Cells/*physiology [MESH] |Female [MESH] |Glycolysis [MESH] |Humans [MESH] |Lactic Acid/metabolism [MESH] |Male [MESH] |Mice [MESH] |Mice, Inbred C57BL [MESH] |Neovascularization, Pathologic/*etiology [MESH] |Phosphofructokinase-2/*physiology [MESH] |Proto-Oncogene Proteins c-akt/physiology [MESH]Endothelial PFKFB3 plays a critical role in angiogenesis (epmc).pdf DeepDyve Pubget Overpricing