Adenovirus E1A Proteins Regulate Phosphoenolpyruvate Carboxykinase Gene Transcription through Multiple Mechanisms

CREB Binding Protein Coordinates the Function of Multiple Transcription Factors Including Nuclear Factor I to Regulate Phosphoenolpyruvate Carboxykinase (GTP) Gene Transcription

“…Their cells were maintained for 20 h after adenoviral infection, so that viral-induced transcription factors could participate in the regulation of PEPCK gene transcription. Kalvakalanu et al (36) infected HepG2 cells with adenovirus but isolated nuclei for transcription measurements within 2.5 h. In addition Kalvakalanu et al (36,58) determined the direct effect of E1A, introduced into the HepG2 cells via an expression plasmid, on transcription from the PEPCK gene promoter. The most likely explanation for the differences between the two studies is that the long term expression of the adenoviral genes in hepatoma cells could alter PEPCK gene expression in an indirect manner due to the expression of viral genes in the late stage of infection.…”

Direct binding of hepatitis B virus X protein and retinoid X receptor contributes to phosphoenolpyruvate carboxykinase gene transactivation

“…Notably, adenovirus infection was previously shown to regulate the PEPCK gene transcription through E1A expression [16]. Notably, adenovirus infection was previously shown to regulate the PEPCK gene transcription through E1A expression [16].…”

Antiangiogenesis gene armed tumor‐targeting adenovirus yields multiple antitumor activities in human HCC xenografts in nude mice

“…Deletion of the CR2 LXCXE motif that defines the minimal requirement for Rb binding similarly reduces the ability of E1a to cooperate in transformation. Mutagenesis studies have indicated that the deletion of residues 125–128 amino acid residules and the site mutation of 120146 147 and 219 amino acids are essential for mediating the E1a interaction with Rb 34,35 . Studies had shown that deletion of the CR2 domain or even a site mutation to knock out the RB‐binding site on E1a is sufficient to abolish the immortalization function of E1a .…”

“…Mutagenesis studies have indicated that the deletion of residues 125-128 amino acid residules and the site mutation of 120146 147 and 219 amino acids are essential for mediating the E1a interaction with Rb. 34,35 Studies had shown that deletion of the CR2 domain or even a site mutation to knock out the RB-binding site on E1a is sufficient to abolish the immortalization function of E1a. Similarly, our results showed that this mutant adenoviral E1a did not bind to Rb protein in vitro.…”