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PCK1 is detrimental to malignant hepatocytes and activating PCK1 expression is a potential treatment strategy for patients with hepatocellular carcinoma.
This study reveals a unique mechanism to suppress hepatocellular carcinoma by switching from glycolysis to gluconeogenesis through Nur77 antagonism of PEPCK1 degradation.
circC3P1 acts as a tumor suppressor via enhancing PCK1 expression by sponging miR-4641 in hepatocellular carcinoma.
The expression levels of PCK1 were suppressed in hepatocellular carcinoma (HCC) samples and in cells derived from HCC tissues.
Study investigated the molecular basis of such effects focusing on a commonly studied polymorphism in pig Pgc1alpha, which changes a cysteine at position 430 (WT) of the protein to a serine (C430S); found that differential O-GlcNAcylation of Pgc1alpha regulates PCK1 activity and this molecular mechanism could explain at least in part the epistatic interaction between both genes.
Study identified a novel homozygous PCK1 missense mutation causing cytosolic phosphoenolpyruvate carboxykinase deficiency presenting as childhood hypoglycemia.
HBXIP is able to depress the gluconeogenesis in hepatoma cells by suppressing PCK1 to promote hepatocarcinogenesis, involving miR-135a/FOXO1 axis and PI3K/Akt/p-FOXO1 pathway.
an extended binding site in the catalytic cleft of cPEPCK which is used by 3-MPA to inhibit cPEPCK non-competitively.
A mutation of PCK1 associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity.
Insulin-dependent translocation of FOXO1 regulated transcriptional repression of PCK1 concomitant with the formation of the FOXO1-euchromatic histone-lysine N-methyltransferase2 (EHMT2) complex and histone modifications of the PCK1 promoter region
Lipopolysaccharide and monophosphoryl lipid A also up-regulated G6PC and PCK1 transcript abundance in a TLR4-dependent manner.
The PCK1 tag-single nucleotide polymorphisms influenced insulin resistance by interacting with plasma n-3 polyunsaturated fatty acids levels in metabolic syndrome patients.
HCV core protein expression-mediated FOXO1 activation and the increased PGC-1alpha leaded to the elevation of PCK1 at the mRNA level
Acetylation regulates the stability of the gluconeogenic rate-limiting enzyme PEPCK1.
Data show PEPCK-C and CPT-1 mRNAs are more abundant in non-tumoral tissues than in the tumoral counterpart, whereas the opposite occurred for the FAS gene.
Studies demonstrate the association between PCK1 and smaller average brain volume.
Study in the EYHS cohort failed to identify an association of PCK1 polymorphisms with obesity, physical activity, and fitness.
crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site
Conserved amino acids within CCAAT enhancer-binding proteins (C/EBP(alpha) and beta) regulate gene expression
promoter context may influence which domains within a transcription factor are employed to mediate transactivation of PEPCK
A Pck1-directed glycogen metabolic program regulates formation and maintenance of memory CD8(+) T cells.
Pck1 contributes to M1 polarization in macrophages
The results reveal a previously unrecognized physiological function of NFYA in controlling glucose metabolism by up-regulating the gluconeogenic genes Pck1 and G6pc.
Data (including data from studies in knockout mice) suggest that Pck1 in liver plays role in glucose homeostasis; here, Pck1 deficiency (in knockout mice) can be successfully treated by re-expression of Pck1 in liver, thus partially rescuing pups from fatal neonatal hypoglycemia. Pck1 appears to play roles in metabolism in lung and skeletal muscle.
Silencing PCK1 or inhibiting its enzymatic activity slows the growth of tumor-repopulating cells in vitro and impedes tumorigenesis in vivo.
PEPCK-M expression partially rescued defects in lipid metabolism, gluconeogenesis and TCA cycle function impaired by PEPCK-C deletion, while approximately 10% re-expression of PEPCK-C normalized most parameters.
FAT/CD36 regulates PEPCK in adipose tissue and that this could be secondary to reductions in lipolysis.
PCB 126 blunted the forskolin-stimulated increase in phosphoenolpyruvate carboxykinase (PEPCK) mRNA levels.
the role of IL-6 signalling in adipose tissue during exercise
there are multiple cytokine pathways by which inflammation inhibits PEPCK expression in adipose tissue which could contribute to the increased mobilization of fatty acids during inflammation
Glucagon can also regulate Pck1 in the intestine, but not in the kidneys.
Pck1 plays an important role in both the mammary gland adipocytes and epithelial cells during lactation
Results suggest that HDAC3 mediates NF-kappaB activity to repress Pepck transcription.
Results show the effect of miR-29a in counteracting insulin action on PEPCK gene expression by primarily targeting PI3K and abrogating downstream insulin signaling in HepG2 cells.
PPARgamma binding site in the promoter of Pck1 is essential for maintenance of lipid metabolism and glucose homeostasis and disease prevention.
hyperhomocysteinemia may be considered as a risk factor that contributes to the development of insulin resistance with respect to elevated glucose output and upregulation of PEPCK, probably via the PKA pathway
Data show that gamma-linoleic acid positively modulates TR4 activity to promote the expression of downstream genes apolipoprotein E (ApoE) and phosphoenolpyruvate carboxykinase.
ATF3 bound to the ATF/cAMP-responsvie element site derived from the promoter of the gene encoding the gluconeogenic enzyme phosphoenolpyruvate carboxykinase
The binding of nuclear receptors to PEPCK RARE1, RARE2 and RARE3 indicates a complex pattern of retinoid receptor and orphan nuclear receptor binding.
Liver-specific PEPCK knockout mice are able to maintain normal blood sugar while fasting by increasing gluconeogenesis and by glucose metabolism
the renal proximal tubule, may require the remodeling of AUF1 binding to the elements that mediate the rapid turnover of PEPCK mRNA
Collectively, the identified 3'-untranslated-region SNP variant highlights the importance of PCK1 in the fecundity of Holstein bulls, and implicates a role for bta-miR-26a in regulating PCK1 abundance.
Expression of cytosolic PEPCK mRNA is transiently increased during early lactation, indicating that enhanced hepatic gluconeogenesis during lactation may be tied to enhanced capacity for cytosolic formation of phosphoenolpyruvate.
The regulatory properties of maize phosphoenolpyruvate carboxylase were significantly altered by site-directed mutagenesis of residues 226 through 232.
Arabidopsis uses two gluconeogenic gateways for organic acids to fuel seedling establishment, one is via PCK1, and a second via PPDK.
Malate metabolism is important during dark-induced stomatal closure and that phosphoenolpyruvate carboxykinase (PEPCK) is involved in this process.
This gene is a main control point for the regulation of gluconeogenesis. The cytosolic enzyme encoded by this gene, along with GTP, catalyzes the formation of phosphoenolpyruvate from oxaloacetate, with the release of carbon dioxide and GDP. The expression of this gene can be regulated by insulin, glucocorticoids, glucagon, cAMP, and diet. Defects in this gene are a cause of cytosolic phosphoenolpyruvate carboxykinase deficiency. A mitochondrial isozyme of the encoded protein also has been characterized.
, phosphoenolpyruvate carboxykinase, cytosolic
, phosphoenolpyruvate carboxykinase, cytosolic [GTP]
, phosphoenolpyruvate carboxylase
, phosphopyruvate carboxylase
, phosphoenolpyruvate carboxykinase 1 (soluble)
, Phosphoenolpyruvate carboxykinase, cytosolic
, Phosphoenolpyruvate carboxykinase 1 (soluble)-like
, phosphoenolpyruvate carboxykinase (GTP)
, phosphoenolpyruvate carboxykinase 1, cytosolic
, phosphoenolpyruvate carboxykinase, cytosolic (GTP)
, cytosolic phosphoenolpyruvate carboxykinase
, gluconeogenic enzyme
, phosphoenolpyruvate carboxykinase 1 variant 1
, phosphoenolpyruvate carboxykinase 1 variant 2
, phosphoenolpyruvate carboxykinase 1 variant 3
, phosphoenolpyruvate carboxykinase 1 variant 4
, phosphoenolpyruvate carboxykinase 1 variant 5
, synonymous gene name: Pep2 in maize linkage map
, phosphoenol pyruvate carboxykinase
, phosphoenolpyruvate carboxy kinase
, phosphoenolpyruvate carboxykinase
, cytosolic phosphoenolpyruvate carboxykinase 1