Alteration by v-Ki-ras in NaF, cholera toxin and forskolin-induced adenylate cyclase activation in NIH/3T3 fibroblast cells.
It has been suggested that ras proteins are involved in the transmembrane signaling mechanism and they share structural features with GTP-binding proteins. To identify the role of ras oncogene and it's products in the coupling mechanisms of GTP-binding proteins to adenylate cyclase, we examined effect of NaF, cholera toxin and forskolin in normal and v-Ki-ras transformed NIH/3T3 fibroblast cells. In transformants, adenylate cyclase activity was markedly enhanced by NaF and cholera toxin, in contrast to normal cells. It is suggested that ras oncogene proteins plays enhancing role in coupling of GTP-binding proteins to adenylate cyclase.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D002472:Cell Transformation, Viral; D002772:Cholera Toxin / Q000494:pharmacology*; D005576:Colforsin / Q000494:pharmacology*; D004789:Enzyme Activation; D005347:Fibroblasts / Q000201:enzymology*; D019204:GTP-Binding Proteins / Q000494:pharmacology; D051379:Mice; D009857:Oncogenes; D012969:Sodium Fluoride / Q000494:pharmacology*; D014764:Viral Proteins / Q000494:pharmacology*
D014764:Viral Proteins; D005576:Colforsin; D012969:Sodium Fluoride; D002772:Cholera Toxin; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases