Polyamines and protein kinase I. Induction of ornithine decarboxylase and activation of protein kinase in rat glioma cells

Uriel Bachrach*, Aviva Katz, Jacob Hochman

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

The activities of cAMP-dependent and independent protein kinases were determined after feeding confluent glioma C6-BU-1 cultures. It has been shown that the activity of both enzymes rose considerably after feeding, and that the ratio of 32P incorporation into histone, in the absence and the presence of cAMP, was maximal 4 hours after feeding. This increase in protein kinase activity was followed by the activation of ornithine decarboxylase and accumulation of putrescine. Spermine, at millimolar concentrations, inhibited protein kinase, apparently by inactivating the catalytic subunit. It is suggested that this inhibition of protein kinase by polyamines is another regulatory mechanism, which controls cellular growth.

Original languageEnglish
Pages (from-to)817-822
Number of pages6
JournalLife Sciences
Volume22
Issue number9
DOIs
StatePublished - Mar 1978

Fingerprint

Dive into the research topics of 'Polyamines and protein kinase I. Induction of ornithine decarboxylase and activation of protein kinase in rat glioma cells'. Together they form a unique fingerprint.

Cite this