Lung cancer cells often express high levels of protein kinase C activity.
We analyzed protein kinase C (PKC) activity in twenty-two tumor cell lines derived from lung, pancreas, stomach, tongue and vulva, and found that lung cancer cells often (9 out of 13) exhibit significantly higher PKC activity than other types of cancer cells. The PKC in these lung cancer cells was separated into one major and one minor peaks by a Mono Q column chromatography. The PKC in the major peak had an absolute requirement for Ca2+, phosphatidylserine and 12-O-tetradecanoylphorbol-13-acetate (TPA), as expected. However, the PKC in the minor peak did not require TPA for its activation. Hydroxyapatite column chromatography revealed that the PKC in the major peak is type III. These results indicate that in lung cancer cells type III PKC activity is often elevated compared to other types of cancer cells. The growth of many lung cancer cell lines was inhibited by TPA.
Hirai
M
M
Department of Molecular Biology, Keio University School of Medicine, Tokyo.
Gamou
S
S
Kobayashi
M
M
Shimizu
N
N
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002845:Chromatography; D005260:Female; D006801:Humans; D008175:Lung Neoplasms / Q000201:enzymology*; D051379:Mice; D010190:Pancreatic Neoplasms / Q000201:enzymology; D010718:Phosphatidylserines / Q000494:pharmacology; D011493:Protein Kinase C / Q000302:isolation & purification / Q000378:metabolism*; D013274:Stomach Neoplasms / Q000201:enzymology; D013755:Tetradecanoylphorbol Acetate; D014062:Tongue Neoplasms / Q000201:enzymology; D014407:Tumor Cells, Cultured; D014846:Vulvar Neoplasms / Q000201:enzymology
D010718:Phosphatidylserines; D011493:Protein Kinase C; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium