Disease relevance of PCK1

• Co-transfection of an expression vector for CAAT/enhancer binding protein alpha or CAAT/enhancer binding protein beta markedly stimulated transcription from both the chicken and rat PEPCK-C promoters in human hepatoma cells [1].

High impact information on PCK1

• In transiently transfected fibroblasts COUP-TFII acts at gAF1/PCK1 to inhibit PPARgamma/RXR activation via PCK2 [2].
• Thus, PEPCK-M and PEPCK-C, clearly represented the products of two distinct genes, which were distinguished by altered protein sequences and non-cross-hybridizing, differentially regulated mRNAs [3].
• An assay system for localisation of pyruvate and phosphoenolpyruvate carboxylase activity on polyacrylamide gels and its application to detection of these enzymes in tissue and cell extracts [4].
• White Leghorn chickens from a nonselected closed population were typed for two RFLP located in the 3' end of the gene coding for cytosolic phosphoenol-pyruvate carboxykinase (PEPCK-C), a major control gene of gluconeogenesis [5].
• There was significant interaction between PEPCK-C genotypes and mitochondrial PEPCK (PEPCK-M) genotypes defined by a single RFLP [5].

Biological context of PCK1

• A 3,792-bp segment of 5'-region of the PEPCK-C gene (position -1723 to 2069) was sequenced in four individuals from eight different strains of White Leghorn chickens (a total of 64 genomes) [6].
• Based on this analysis we can now identify individuals with the evolutionary most distant PEPCK-C haplotypes, establish strains of these haplotypes, and analyze trait associations and epistasis with other genes [6].

Anatomical context of PCK1

• These differences are likely to be genetic, as hormonal treatment of a chicken hepatoma cell line indicates that whereas the mRNA levels for PEPCK-C are hormonally regulated, the expression of PEPCK-M mRNA is unresponsive [7].

References