[cAMP mediated cell growth regulation. II. Characterization of the biochemical change responsible for resistance to cAMP treatment].
In this paper we characterize the biochemical defect of a mutant (10248) of CHO cells, resistant to the cAMP treatment. Cells cultured on MEM were collected each three days, homogenized and centrifuged. The cell extract was assayed for protein kinases activity and the binding of 8-N3-(32P)cAMP. The same extract was also applied on to a DEAE cellulose column, eluted with a linear gradient and the fractions tested for the phosphotransferase activity and 8-N3-(32P)cAMP binding. Mutant 10248 shows a different profile of protein kinases activity as compared to 10001 control. Protein kinases II is absent whereas a normal RII binding activity is present. RI shows altered affinity for cAMP.
D000818:Animals; D002455:Cell Division; D002478:Cells, Cultured; D006224:Cricetinae; D003412:Cricetulus; D000242:Cyclic AMP / Q000502:physiology*; D004351:Drug Resistance; D005260:Female; D009154:Mutation; D010053:Ovary
D000242:Cyclic AMP
Regolazione della crescita cellulare da parte del cAMP. II. Caratterizzazione delle alterazioni biochimiche responsabili delle resistenze al trattamento col cAMP.