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Human PEPCK Protein expressed in Wheat germ - ABIN1314318
Kanno, Watanabe, Takahashi, Abe, Ohira: Anti-phosphoenolpyruvate carboxykinase 2 antibody in patients with autoimmune hepatitis. in Hepatology research : the official journal of the Japan Society of Hepatology 2014
Our study indicates that the T allele of the rs4982856 single-nucleotide polymorphisms in the PCK2 gene may be a risk factor for glucose intolerance after kidney transplantation
Downregulation of PCK2 remodels tricarboxylic acid cycle in tumor-repopulating cells of melanoma
ApoA-IV colocalizes with NR4A1, which suppresses G6Pase and PEPCK gene expression at the transcriptional level, reducing hepatic glucose output and lowering blood glucose.
Results indicate that PEPCK promotes tumor growth by increasing glucose and glutamine metabolism, increases anabolic metabolism and promotes mTORC1 activity.
Mitochondrial PCK2 regulates metabolic adaptation and enables glucose-independent tumor growth in various neoplasms.
When autophagy was blocked, the level of glucose-6-phosphatase (G6Pase) and phosphoenolpyruvate carboxykinase (PEPCK) was reduced in HepG2 cells and not in Hep3B cells.
PEPCK activity was elevated threefold in lung cancer samples over normal lungs and its activation mediates an adaptive response to glucose depletion in lung cancer.
Amino acid limitation and ER stress inducers, conditions that activate the amino acid response (AAR) and the unfolded protein response (UPR), stimulate PCK2 gene transcription in tumor cell lines.
Expression of phosphoenolpyruvate carboxykinase linked to chemoradiation susceptibility of human colon cancer cells.
expression of HCV nonstructural component NS5A in Huh7 or primary hepatocytes stimulated PEPCK gene expression and glucose output in HepG2 cells.
results reveal a novel link between glucose metabolism and the DNA damage signaling pathway and suggest a possible role for PEPCK and G6P in the DNA damage response
Endoplasmic reticulum stress triggers suppression of AMPK while increasing C/EBPbeta and pCREB expression which activates PEPCK gene transcription.
Results suggest that pepck2 gene expression is regulated by its 5' flanking region up to 822 bp, and 317 bp upstream of transcriptional start point.
Wild-type AREBP, but not Ser(470) to Ala(470) substituted non-phosphorylating mutant, represses gene expression of the phosphoenolpyruvate carboxykinase (PEPCK), a key enzyme of gluconeogenesis.
skeletal muscle PEPCK has a role in determining physical activity levels
Increased transcriptional expression of PEPCK1 and G6Pc does not account for increased gluconeogenesis and fasting hyperglycemia in patients with type 2 diabetes mellitus.
Transition to lactation does not alter expression of the mitochondrial form of PEPCK.
Concurrent binding and modifications of AUF1 and HuR mediate the pH-responsive stabilization of phosphoenolpyruvate carboxykinase mRNA in kidney cells.
This gene encodes a member of the phosphoenolpyruvate carboxykinase (GTP) family. The protein is a mitochondrial enzyme that catalyzes the conversion of oxaloacetate to phosphoenolpyruvate in the presence of GTP. A cytosolic form encoded by a different gene has also been characterized and is the key enzyme of gluconeogenesis in the liver. The encoded protein may serve a similar function, although it is constitutively expressed and not modulated by hormones such as glucagon and insulin that regulate the cytosolic form. Alternatively spliced transcript variants have been described.
, phosphoenolpyruvate carboxykinase [GTP], mitochondrial
, phosphoenolpyruvate carboxylase
, phosphopyruvate carboxylase
, mitochondrial phosphoenolpyruvate carboxykinase 2
, phosphoenolpyruvate carboxykinase 2 (mitochondrial) L homeolog
, phosphoenolpyruvate carboxykinase 2 (mitochondrial) S homeolog