Further studies on the biochemical characterization of the MC-29 virus derived transplantable hepatoma (VTH). I. Binding of 3H-cortisol to cytoplasmic receptor and DNA.
The molecular mechanisms underlying the failure of steroids to stimulate glucose-6-Pase and arylhydrocarbonhydroxylase activities in the MC-29-virus-derived transplantable hepatoma (VTH) were investigated. Following cellular uptake of 3H-Cortisol, its subcellular distribution, binding to a specific cytoplasmic receptor and the interaction between steroid-bound receptor and DNA were compared in VTH and in normal chicken liver. No appreciable difference was observed either in 3H-Cortisol uptake or in binding to cytoplasmic receptors. However, compared with normal liver, only half as much hepatoma steroid receptor was able to interact with DNA at the protein/DNA ratio of 60. This reduced DNA binding of VTH 3H-Cortisol-receptor was irrespective of the source of DNA (VTH or liver). It is concluded that one of the causes for abnormal gene regulation in VTH may lie at the level of DNA-protein interaction.
D000818:Animals; D002645:Chickens; D003593:Cytoplasm / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D005260:Female; D006854:Hydrocortisone / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D008297:Male; D009368:Neoplasm Transplantation; D011965:Receptors, Glucocorticoid / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*; D014018:Tissue Distribution
D011965:Receptors, Glucocorticoid; D011987:Receptors, Steroid; C029360:hydrocortisone receptor; D004247:DNA; D006854:Hydrocortisone