TY - JOUR
T1 - Polyamines and protein kinase I. Induction of ornithine decarboxylase and activation of protein kinase in rat glioma cells
AU - Bachrach, Uriel
AU - Katz, Aviva
AU - Hochman, Jacob
PY - 1978/3
Y1 - 1978/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0017861812&partnerID=8YFLogxK
U2 - 10.1016/0024-3205(78)90252-7
DO - 10.1016/0024-3205(78)90252-7
M3 - ???researchoutput.researchoutputtypes.contributiontojournal.article???
C2 - 565453
AN - SCOPUS:0017861812
SN - 0024-3205
VL - 22
SP - 817
EP - 822
JO - Life Sciences
JF - Life Sciences
IS - 9
ER -