Ornithine decarboxylase and polyamine levels are reduced in CHO cells deficient in cAMP-dependent protein kinase.

Abstract A Chinese hamster ovary cell mutant with greatly reduced catalytic activity of cAMP-dependent protein kinase was compared with wild type cells having normal kinase activity for differences in biosynthesis, uptake and conjugation of polyamines. The inducibility of ornithine decarboxylase in response to cAMP, serum, human chorionic gonadotropin, asparagine and phorbol esters was greatly reduced in the mutant cells. Putrescine, spermidine and spermine levels rose 2–6 fold in wild type cells but in kinase mutant cells the basal and stimulated levels were generally lower. The cellular uptake and conjugation of radiolabelled putrescine and spermidine were reduced 5–10 fold in the kinase mutant cells. These results provide further evidence of the positive regulatory control exerted by cAMP-dependent protein kinase on polyamine biosynthesis.