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anti-Mouse (Murine) PDK1 Anticorps:
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High PDK1 expression promotes breast cancer stemness.
HIF-1alpha-PDK1-mediated metabolic changes occur in mild hypoxia, where mitochondrial cytochrome c oxidase activity is unimpaired, suggesting a mode of glycolytic reprogramming.
PDK1 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.
These findings reveal that there are divergent roles of PDKs during oocyte maturation and indicate a new mechanism controlling meiotic structure.
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 in this event via controlling glycolysis and glucose oxidation.
PDHK1 is expressed in Th17 cells, but not Th1 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 binding.
Pdk1 enzyme is critical in conserving mitochondrial function by diverting metabolic intermediates to glycolysis
mir-138-5p could repress the development of Retinoblastoma (RB) via suppressing PDK1, which may offer a new vision for interpreting the mechanism of RB tumorigenesis.
miR-375 and its probable PDK1 target may be utilized for the management of Kidney cancer.
The importance of PDK1 in tumor growth and progression.A role of PDK1 in tumor microenvironment.[review]
MiR-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- 145.
These results indicate that the immunohistochemistry analysis of the protein expression of PDK1, PHD3, and HIF-1alpha defines the hypoxic status of Neuroblastoma tumors.
The pyruvate dehydrogenase kinases (PDKs) PDK1 and PDK3 are direct targets of KDM4A and E2F1 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), attenuated the mitochondrial membrane potential (MMP), induced apoptosis, and reduced cell viability in vitro.
miR-379 could function as a tumour-suppressing miRNA via targeting PDK1 in osteosarcoma.
These results also suggest that inhibition of HIF-1a 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 and up-regulation of PDK1 may be novel biomarkers for predicting advanced tumor progression and unfavorable prognosis in recurrent nasopharyngeal carcinoma patients
n the conditon of miR- 128b over-expression, we also observed spontaneous inactivation of the Akt/NF-kappaB signalling, implying PDK1 was a potential regulator of this pathway. In conclusion, our study shed some novel light on miR-128b-PDK1/Akt/NF-kappaB axis onGastric cancer (GC) progression
Dichloroacetate, an Iihibitor of PDK1, can reverse the mitochondrial suppression of renal cell carcinoma and decrease HIF transcriptional activity, decreasing tumor growth and angiogenesis.
Tergeting PDK1 with dichloroacetophenone inhibited acute myeloid leukemia cell growth via multiple signaling pathways.
PDK1 was specifically required for metabolic adaptation to nutrient limitation and hypoxia.
High expression of PDK1 is associated with Colon Cancer.
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
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