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PDK2/PARL senses defects in mitochondrial bioenergetics.
The data demonstrate potential roles of PDK2 and ABCG2 polymorphisms in the metabolic phenotypes of Tibetan gout patients.
High glycolysis and PDK2 overexpression are closely linked to cisplatin resistance in head and neck cancer cells, which can be reversed by PDK2 nhibition.
both PDK 1 and 2 isoforms are overexpressed in cutaneous melanoma compared to nevi, this expression being associated with the expression of the mTOR pathway effectors and independent of the BRAF mutational status
The findings of the present study reveal a novel survival pathway that functionally couples the unique glycolytic phenotype in cancer cells to hypoxia resistance via a PDK2-dependent mechanism that switches Bnip3 from cell death to survival.
The final compound of this series, 2-[(2,4-dihydroxyphenyl)sulfonyl]isoindoline-4,6-diol, designated PS10, inhibits all four PDK isoforms with IC50 = 0.8 muM for PDK2.
Germline mutations in PKD2 gene is associated with autosomal-dominant polycystic kidney disease.
we for the first time demonstrated that a low-nutrient condition drives cancer cells to utilize glycolysis to produce ATP, and this increases the Warburg effect through a novel mechanism involving ROS/AMPK-dependent activation of PDK.
Mitochondrial activation by inhibition of PDKII suppresses HIF1a signaling and angiogenesis in cancer.
Inactivation of pyruvate dehydrogenase kinase 2 by mitochondrial reactive oxygen species.
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.
PKD2 mutations are associated with autosomal dominant polycystic kidney disease.
study of facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase
The increased PDK activity was independent of changes in intra-mitochondrial effectors, and PDK-2 and PDK-4 protein content, suggesting that it was caused by a change in the specific activity of the existing kinases.
A mechanism for pyruvate dehydrogenase kinase isoform 2 regulation is supported in which kinase activity is limited by ADP dissociation and pyruvate binding.
Reductive acetylation stimulates activity of pyruvate dehydrogenase kinase isoform 2 by speeding up ADP dissociation.
in human muscle, hormonal and nutritional conditions may control PDK2 and PDK4 mRNA expression via a common signalling mechanism.
Crystallographic studies reveal several PDHK2 structures with C-terminal cross arms that span a large trough region between the N-terminal regulatory (R) domains of the PDHK2 dimers. Three novel ligand binding sites are located in the R domain of PDHK2.
analysis of ligand induced effects on pyruvate dehydrogenase kinase isoform 2
These studies identify ORP9 as a PDK-2 substrate and negative regulator of Akt phosphorylation at the PDK-2 site.
our results suggest that PDK2/4 can be a potential target for the development of pharmacotherapy for the treatment of acute inflammatory pain
The current study reports that increasing hepatic PDC activity by inhibition of PDK2 ameliorates hepatic steatosis and insulin sensitivity by regulating TCA cycle anaplerosis and ketogenesis. The findings suggest PDK2 is a potential therapeutic target for nonalcoholic fatty liver disease.
PDK2/4 induction and the subsequent lactate surge induce the metabolic shift in the diabetic dorsal root ganglion thereby contributing to the pathogenesis of painful diabetic neuropathy.
These findings reveal that there are divergent roles of PDKs during oocyte maturation and indicate a new mechanism controlling meiotic structure.
Double-knockout mice with global deletion of PDK2 and PDK4, which results in constitutively activated pyruvate dehydrogenase, preferentially oxidize glucose in muscle.
The Pdk4 gene knockdown led to better glucose tolerance than the Pdk2 gene knockdown.
loss of both Pdk2 and Pdk4 attenuated HSC quiescence, glycolysis, and transplantation capacity.
PDK2 activity is essential, even at rest, in regulation of carbohydrate oxidation and production of reducing equivalents for the electron transport chain.
mitochondrial ND2 mutation contributes to HIF1alpha accumulation via increased ROS production, up-regulation of PDK2, attenuating PDH activity, thereby increasing pyruvate, resulting in HIF1alpha stabilization
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.
PDH kinase 2
, pyruvate dehydrogenase kinase, isoenzyme 2
, pyruvate dehydrogenase, lipoamide, kinase isozyme 2, mitochondrial
, [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial
, pyruvate dehydrogenase 2
, pyruvate dehydrogenase kinase, isozyme 2
, PDK P45
, pyruvate dehydrogenase kinase 2 subunit p45 (PDK2)