Growth-dependent modulation of casein kinase II and its substrate nucleolin in primary human cell cultures and HeLa cells.
We have previously provided evidence that casein kinase II (CKII) and its substrate nucleolin increase concomitantly during certain development stages during embryogenesis (Schneider et al., Eur. J. Biochem. 161, 733-738). We now show that during normal growth of primary cell cultures and HeLa cells CKII activity is increased concomitant with cellular growth and that the activity declines when confluency is reached. Parallel to the CKII activity increase, nucleolin, which has been shown to be a potential substrate of CKII changes its phosphorylation status, reaching a maximum at the time when CKII activity is highest and decreasing again when CKII activity declines.
Schneider
H R
HR
Institut für Humangenetik, Universität des Saarlandes, Homburg, F.R.G.
Issinger
O G
OG
D047388:Casein Kinases; D002453:Cell Cycle; D002478:Cells, Cultured; D006367:HeLa Cells; D006801:Humans; D008970:Molecular Weight; D009687:Nuclear Proteins / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D016601:RNA-Binding Proteins; D000097796:Nucleolin
D047388:Casein Kinases; D009687:Nuclear Proteins; D010750:Phosphoproteins; D011494:Protein Kinases; D016601:RNA-Binding Proteins; D000097796:Nucleolin