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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1

6-phosphofructo-2-kinase, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, fructose-2,6-bisphosphatase, PFK2
bifunctional enzyme; catalyzes synthesis and degradation of fructose 2,6-bisphosphate, a ubiquitous stimulator of glycolysis [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: ACID, HAD, Fru, Phosphofructokinase-1, CAN
Papers on 6-phosphofructo-2-kinase
Interleukin-6 stimulates aerobic glycolysis by regulating PFKFB3 at early stage of colorectal cancer.
New
Wu et al., Shanghai, China. In Int J Oncol, Jan 2016
6-phoshofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3) was the most downregulated gene by anti-IL-6 receptor antibody in colorectal adenoma tissues.
PFKFB3 modulates glycolytic metabolism and alleviates endoplasmic reticulum stress in human osteoarthritis cartilage.
New
Zhou et al., Xi'an, China. In Clin Exp Pharmacol Physiol, Jan 2016
In the present work, we aimed to investigate the expression and role of the glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (PFKFB3) in OA cartilage.
NaCl stress impact on the key enzymes in glycolysis from Lactobacillus bulgaricus during freeze-drying.
New
Liu et al., Harbin, China. In Braz J Microbiol, Dec 2015
However, a transcriptional analysis of the corresponding genes suggested that the effect of NaCl stress on the expression of the pfk2 gene was not obvious.
PFKFB3-mediated glycolysis is involved in reactive astrocyte proliferation after oxygen-glucose deprivation/reperfusion and is regulated by Cdh1.
New
Zhang et al., Wuhan, China. In Neurochem Int, Dec 2015
The enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase isoform 3 (PFKFB3), an allosteric activator of 6-phosphofructo-1-kinase (PFK1), controls glycolytic flux.
Characterization of two MODY2 mutations with different susceptibility to activation.
New
Baltrusch et al., Rostock, Germany. In Biochem Biophys Res Commun, Oct 2015
The endogenous activator fructose-2,6-bisphosphatase evoked an increase in glucokinase activity for both mutants, but much stronger for L315H compared to L304P.
Targeting the sugar metabolism of tumors with a first-in-class 6-phosphofructo-2-kinase (PFKFB4) inhibitor.
New
Telang et al., Louisville, United States. In Oncotarget, Aug 2015
Recent studies have demonstrated that cancer cells from several tissue origins and genetic backgrounds require the expression of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 (PFKFB4), a regulatory enzyme that synthesizes an allosteric activator of glycolysis, fructose-2,6-bisphosphate. We report the discovery of a first-in-class PFKFB4 inhibitor, 5-(n-(8-methoxy-4-quinolyl)amino)pentyl nitrate (5MPN), using structure-based virtual computational screening.
Endothelial Metabolism Driving Angiogenesis: Emerging Concepts and Principles.
Review
New
Carmeliet et al., Leuven, Belgium. In Cancer J, Jul 2015
During vessel sprouting, the glycolytic activator PFKFB3 (6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3) promotes vessel branching by rendering ECs more competitive to reach the tip of the vessel sprout, whereas fatty acid oxidation selectively regulates proliferation of endothelial stalk cells.
p53- and p73-independent activation of TIGAR expression in vivo.
Cheung et al., Glasgow, United Kingdom. In Cell Death Dis, 2014
TIGAR (TP53-induced glycolysis and apoptosis regulator) functions as a fructose-2,6-bisphosphatase and its expression results in a dampening of the glycolytic pathway, while increasing antioxidant capacity by increasing NADPH and GSH levels.
Angiogenesis revisited - role and therapeutic potential of targeting endothelial metabolism.
Review
Carmeliet et al., Leuven, Belgium. In J Cell Sci, 2014
Recent studies show that endothelial cells rely on glycolysis for ATP production, and that the key glycolytic regulator 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3 (PFKFB3) regulates angiogenesis by controlling the balance of tip versus stalk cells.
Mechanisms of regulation of PFKFB expression in pancreatic and gastric cancer cells.
Review
Esumi et al., Kiev, Ukraine. In World J Gastroenterol, 2014
Enzymes 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 and -4 (PFKFB-3 and PFKFB-4) play a significant role in the regulation of glycolysis in cancer cells as well as its proliferation and survival.
Role of AMPK-mediated adaptive responses in human cells with mitochondrial dysfunction to oxidative stress.
Review
Wei et al., Taipei, Taiwan. In Biochim Biophys Acta, 2014
MAJOR CONCLUSION: Induction of adaptive responses via AMPK-PFK2, AMPK-FOXO3a, AMPK-PGC-1α, and AMPK-mTOR signaling pathways, respectively is modulated for the survival of human cells under oxidative stress induced by mitochondrial dysfunction.
Partial and transient reduction of glycolysis by PFKFB3 blockade reduces pathological angiogenesis.
Impact
Carmeliet et al., Leuven, Belgium. In Cell Metab, 2014
We recently provided genetic evidence that the glycolytic activator phosphofructokinase-2/fructose-2,6-bisphosphatase 3 (PFKFB3) promotes vessel formation but did not explore the antiangiogenic therapeutic potential of PFKFB3 blockade.
Brain energy metabolism in glutamate-receptor activation and excitotoxicity: role for APC/C-Cdh1 in the balance glycolysis/pentose phosphate pathway.
Review
Bolaños et al., Salamanca, Spain. In Neurochem Int, 2013
Our laboratory identified 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase-3 (PFKFB3) -a key glycolytic-promoting enzyme- as an APC/C-Cdh1 substrate.
Targeted overexpression of inducible 6-phosphofructo-2-kinase in adipose tissue increases fat deposition but protects against diet-induced insulin resistance and inflammatory responses.
GeneRIF
Wu et al., Augusta, United States. In J Biol Chem, 2012
a unique role for PFKFB3/iPFK2 in adipocytes with regard to diet-induced inflammatory responses in both adipose and liver tissues.
Dimer interface rearrangement of the 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase rat liver isoenzyme by cAMP-dependent Ser-32 phosphorylation.
GeneRIF
Baltrusch et al., Hannover, Germany. In Febs Lett, 2012
flexible kinase interaction mode exists, suggesting dimer conformation mediated coupling of hormonal and posttranslational enzyme regulation to the metabolic response in liver
Upregulation of heart PFK-2/FBPase-2 isozyme in skeletal muscle after persistent contraction.
GeneRIF
Cussó et al., Barcelona, Spain. In Pflugers Arch, 2012
A persistent increase in 6-phosphofructo-2-kinase produced by a change in PFK-2/FBPase-2 isoform expression that may play an important role in the regulation of muscle glycolysis.
Molecular basis of the fructose-2,6-bisphosphatase reaction of PFKFB3: transition state and the C-terminal function.
GeneRIF
Lee et al., Baton Rouge, United States. In Proteins, 2012
Low bisphosphatase activity of PFKFB3 is solely due to the presence of a serine at residue 302.
Molecular basis for the differential use of glucose and glutamine in cell proliferation as revealed by synchronized HeLa cells.
GeneRIF
Moncada et al., London, United Kingdom. In Proc Natl Acad Sci U S A, 2012
The breakdown of PFKFB3 during S phase occurs specifically via a distinct residue (S(273)) within the conserved recognition site for SCF-beta-TrCP.
Enhancing hepatic glycolysis reduces obesity: differential effects on lipogenesis depend on site of glycolytic modulation.
Impact
Lange et al., Minneapolis, United States. In Cell Metab, 2005
Overexpression of glucokinase or 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase is used to increase hepatic glycolysis.
Nitric oxide switches on glycolysis through the AMP protein kinase and 6-phosphofructo-2-kinase pathway.
Impact
Bolaños et al., Salamanca, Spain. In Nat Cell Biol, 2004
This failure could be accounted for by the much lower amount of 6-phosphofructo-2-kinase (PFK2, the enzyme responsible for F2,6P(2) biosynthesis) in neurons.
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