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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Pyruvate dehydrogenase kinase, isozyme 2

PDK2, pyruvate dehydrogenase kinase 2, pyruvate dehydrogenase kinase isoform 2, PDHK2
This gene encodes a member of the pyruvate dehydrogenase kinase family. The encoded protein phosphorylates pyruvate dehydrogenase, down-regulating the activity of the mitochondrial pyruvate dehydrogenase complex. Overexpression of this gene may play a role in both cancer and diabetes. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Dec 2010] (from NCBI)
Top mentioned proteins: PDK4, PDK1, ACID, Insulin, Akt
Papers on PDK2
Activation of mitochondrial oxidation by PDK2 inhibition reverses cisplatin resistance in head and neck cancer.
Kwon et al., Seoul, South Korea. In Cancer Lett, Mar 2016
Cisplatin-resistant cells overexpressed pyruvate dehydrogenase kinase 2 (PDK2).
Impact of maternal undernutrition around the time of conception on factors regulating hepatic lipid metabolism and microRNAs in singleton and twin fetuses.
McMillen et al., Adelaide, Australia. In Am J Physiol Endocrinol Metab, Feb 2016
We have demonstrated that periconceptional undernutrition and preimplantation undernutrition each resulted in decreased hepatic fatty acid β-oxidation regulators, PGC-1α (P < 0.05), PDK2 (P < 0.01), and PDK4 (P < 0.01) mRNA expression in singleton and twin fetuses at 135-138 days gestation.
Pyruvate Dehydrogenase Kinase-Mediated Glycolytic Metabolic Shift in the Dorsal Root Ganglion Drives Painful Diabetic Neuropathy.
Suk et al., United States. In J Biol Chem, Feb 2016
In this study, we report that pyruvate dehydrogenase kinases (PDK2 and PDK4), key regulatory enzymes in glucose metabolism, mediate glycolytic metabolic shift in the DRG leading to painful diabetic neuropathy.
Involvement of Pregnane X Receptor in the Impaired Glucose Utilization Induced by Atorvastatin in Hepatocytes.
Liu et al., Nanjing, China. In Biochem Pharmacol, Dec 2015
Glucose utilization, glucose uptake, protein levels of GLUT2, GCK, PDK2, PEPCK1 and G6Pase in HepG2 cells were measured.
Clinical Implication of Serine Metabolism-Associated Enzymes in Colon Cancer.
Kang et al., Taegu, South Korea. In Oncology, Nov 2015
Phosphoglycerate dehydrogenase (PHGDH), pyruvate dehydrogenase kinase (PDK) 1, PDK2, pyruvate kinase M2 (PKM2), and phosphoserine aminotransferase (PSAT) expression were investigated by immunohistochemical staining (IHC) in TT and pNT.
Metabolic Connection of Inflammatory Pain: Pivotal Role of a Pyruvate Dehydrogenase Kinase-Pyruvate Dehydrogenase-Lactic Acid Axis.
Suk et al., Taegu, South Korea. In J Neurosci, Nov 2015
Deficiency of Pdk2 and/or Pdk4 in mice attenuated complete Freund's adjuvant (CFA)-induced pain hypersensitivities.
Dichloroacetate prevents restenosis in preclinical animal models of vessel injury.
Schrepfer et al., Hamburg, Germany. In Nature, 2014
Pyruvate dehydrogenase kinase isoform 2 (PDK2) was identified as a key regulatory protein, and its activation proved necessary for relevant myointima formation.
Regulation of glycolysis by Pdk functions as a metabolic checkpoint for cell cycle quiescence in hematopoietic stem cells.
Suda et al., Tokyo, Japan. In Cell Stem Cell, 2013
Here we directly investigated this idea using metabolomic analysis and found that HSCs generate adenosine-5'-triphosphate by anaerobic glycolysis through a pyruvate dehydrogenase kinase (Pdk)-dependent mechanism.
p53 negatively regulates transcription of the pyruvate dehydrogenase kinase Pdk2.
Harris et al., New Brunswick, United States. In Cancer Res, 2012
Results established that wild-type p53 prevents manifestation of the Warburg effect by controlling Pdk2. These findings elucidate a new mechanism by which p53 suppresses tumorigenesis acting at the level of cancer cell metabolism.
Novel PKD1 and PKD2 mutations in autosomal dominant polycystic kidney disease (ADPKD).
Klein et al., Martinsried, Germany. In Nephrol Dial Transplant, 2011
PKD2 mutations are associated with autosomal dominant polycystic kidney disease.
PDH activation during in vitro muscle contractions in PDH kinase 2 knockout mice: effect of PDH kinase 1 compensation.
Peters et al., Canada. In Am J Physiol Regul Integr Comp Physiol, 2011
PDK2 activity is essential, even at rest, in regulation of carbohydrate oxidation and production of reducing equivalents for the electron transport chain.
Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate.
Chuang et al., Dallas, United States. In J Biol Chem, 2010
the DW-motif has a pivotal role in mediating communications between the DCA-, the nucleotide-, and the lipoyl domain-binding sites of PDK2
Genotype-phenotype correlation in children with autosomal dominant polycystic kidney disease.
Seeman et al., Praha, Czech Republic. In Pediatr Nephrol, 2009
PKD1 children have more and larger renal cysts, larger kidneys and higher ambulatory BP than do PKD2 children.
Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer.
Hiromasa et al., Manhattan, United States. In Cell Mol Life Sci, 2007
The fraction of pyruvate dehydrogenase complex (PDC) in the active form is reduced by the activities of dedicated PD kinase isozymes (PDK1, PDK2, PDK3 and PDK4).
A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth.
Michelakis et al., Edmonton, Canada. In Cancer Cell, 2007
Dichloroacetate (DCA) inhibits mitochondrial pyruvate dehydrogenase kinase (PDK), shifts metabolism from glycolysis to glucose oxidation, decreases DeltaPsim, increases mitochondrial H2O2, and activates Kv channels in all cancer, but not normal, cells; DCA upregulates Kv1.5 by an NFAT1-dependent mechanism.
SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity.
Su et al., United States. In Cell, 2006
Recent biochemical studies suggested that TORC2 is the elusive PDK2 for Akt/PKB Ser473 phosphorylation in the hydrophobic motif.
Mechanisms underlying regulation of the expression and activities of the mammalian pyruvate dehydrogenase kinases.
Holness et al., London, United Kingdom. In Arch Physiol Biochem, 2006
Here we review new developments in the regulation of the activities and expression of the PDKs, in particular PDK2 and PDK4, in relation to glucose and lipid homeostasis.
PDK2: the missing piece in the receptor tyrosine kinase signaling pathway puzzle.
Liu et al., San Antonio, United States. In Am J Physiol Endocrinol Metab, 2005
Activation of members of the protein kinase AGC (cAMP dependent, cGMP dependent, and protein kinase C) family is regulated primarily by phosphorylation at two sites: a conserved threonine residue in the activation loop and a serine/threonine residue in a hydrophobic motif (HM) near the COOH terminus.
PI3K-Akt pathway: its functions and alterations in human cancer.
Ito et al., Yonago, Japan. In Apoptosis, 2004
PI(3, 4, 5)P3 is a second messenger essential for the translocation of Akt to the plasma membrane where it is phosphorylated and activated by phosphoinositide-dependent kinase (PDK) 1 and PDK2.
PI3K/Akt signalling pathway and cancer.
González-Barón et al., Madrid, Spain. In Cancer Treat Rev, 2004
Akt interacts with these phospholipids, causing its translocation to the inner membrane, where it is phosphorylated and activated by PDK1 and PDK2.
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