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Here, the authors show that loss of Fxn (Montrer FXN Protéines) in the nervous system in mice also activates an iron/sphingolipid/PDK1 (Montrer PDPK1 Protéines)/Mef2 (Montrer MEF2C Protéines) pathway, indicating that the mechanism is evolutionarily conserved.
PDK1 (Montrer PDPK1 Protéines) has broad effects in hematopoiesis and is a critical factor for engraftment of both hematopoietic stem cells and multipotent progenitors upon transplantation to recipient mice.
PTEN is required for stabilization of planar cell packing in the neural plate and for the formation of stable apical-basal microtubule arrays, while PDPK1 (Montrer PDPK1 Protéines) is required for stabilization of apical junctions during epithelial morphogenesis.
results thus reveal an essential role for the PDK1 (Montrer PDPK1 Protéines)-Akt (Montrer AKT1 Protéines) pathway in the regulation of a key step of neuronal migration.
PDK1 (Montrer PDPK1 Protéines) plays a pivotal role in regulating cardiac function and tumor metastasis by interfering with microenvironment.
Our data suggest that two arms of the glucose metabolism synergistically regulate the differential activation of macrophages. Our findings also highlight the central role of PDK1 (Montrer PDPK1 Protéines) in this event via controlling glycolysis and glucose oxidation.
PDHK1 is expressed in Th17 cells, but not Th1 (Montrer HAND1 Protéines) cells, and at low levels in Tregs, and inhibition or knockdown of PDHK1 selectively suppressed Th17 cells and increased Tregs.
The tyrosine phosphorylation enhances PDHK1 kinase activity by promoting ATP and PDC (Montrer PDC Protéines) binding.
Pdk1 (Montrer PDPK1 Protéines) enzyme is critical in conserving mitochondrial function by diverting metabolic intermediates to glycolysis
MiR (Montrer MLXIP Protéines)-138 inhibits glycolysis but promotes mitochondrial respiration through directly targetting PDK1, and that contributes to cardiac cells' survival.
Study shows higher expression level of PDK1 in non-small cell lung cancer (NSCLC) and its promoter region targeted by miR (Montrer MLXIP Protéines)- 145.
These results indicate that the immunohistochemistry analysis of the protein expression of PDK1, PHD3 (Montrer EGLN3 Protéines), and HIF-1alpha (Montrer HIF1A Protéines) defines the hypoxic status of Neuroblastoma (Montrer ARHGEF16 Protéines) tumors.
The pyruvate dehydrogenase (Montrer PDP Protéines) kinases (PDKs) PDK1 and PDK3 (Montrer PDK3 Protéines) are direct targets of KDM4A (Montrer KDM4A Protéines) and E2F1 (Montrer E2F1 Protéines) and modulate the switch between glycolytic metabolism and mitochondrial oxidation.
dicumarol potently inhibited the kinase activity of PDK1, shifted the glucose metabolism from aerobic glycolysis to oxidative phosphorylation, generated a higher level of reactive oxygen species (ROS (Montrer ROS1 Protéines)), attenuated the mitochondrial membrane potential (MMP), induced apoptosis, and reduced cell viability in vitro.
miR (Montrer MLXIP Protéines)-379 could function as a tumour-suppressing miRNA via targeting PDK1 in osteosarcoma.
These results also suggest that inhibition of HIF-1a (Montrer HIF1A Protéines) with 2-MeOE2 sensitizes radioresistant melanoma cells 435R to X-ray irradiation through targeting the glycolysis that is regulated by PDK1
PDK1 is frequently upregulated in primary nasopharyngeal carcinoma and may serve as a prognostic marker.
A new function for PDK1 in metabolic reprogramming, which could be used to indicate the prognosis of Non small cell lung cancer and provide targeted therapeutic strategy for clinical treatment.
Our results demonstrated that down-regulation of SDHB (Montrer SDHB Protéines) and up-regulation of PDK1 may be novel biomarkers for predicting advanced tumor progression and unfavorable prognosis in recurrent nasopharyngeal carcinoma patients
Dephosphorylation of PDK1 may be a molecular switch for enhancement of protein tyrosine phosphorylation and flagellar hyperactivation in boar spermatozoa.
Pyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation.
pyruvate dehydrogenase kinase, isoenzyme 1
, pyruvate dehydrogenase kinase, isozyme 1
, pyruvate dehydrogenase [lipoamide] kinase isozyme 1, mitochondrial-like
, PDH kinase 1
, [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial
, mitochondrial pyruvate dehydrogenase, lipoamide, kinase isoenzyme 1
, PDK p48
, pyruvate dehydrogenase kinase 1