Ca2+/phospholipid-dependent protein kinase activity correlates to the ability of transformed liver cells to proliferate in Ca2+-deficient medium.
Extracellular Ca2+-deprivation inhibited the proliferation of normal T51B rat liver cells and reduced (2-4 fold) the amount of EDTA/EGTA-extractable protein kinase C activity. By contrast, preneoplastic and neoplastic T51B rat liver cells were able to proliferate in Ca2+-deficient medium and retained all of their extractable protein kinase C activity.
D016604:Aflatoxin B1; D000348:Aflatoxins / Q000633:toxicity*; D000818:Animals; D002122:Calcium Chloride / Q000494:pharmacology*; D002273:Carcinogens / Q000633:toxicity*; D002455:Cell Division / Q000187:drug effects; D002460:Cell Line; D002471:Cell Transformation, Neoplastic / Q000187:drug effects*; D004261:DNA Replication / Q000187:drug effects; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000201:enzymology / Q000503:physiopathology*; D008113:Liver Neoplasms / Q000139:chemically induced / Q000503:physiopathology; D011230:Precancerous Conditions / Q000503:physiopathology*; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D000348:Aflatoxins; D002273:Carcinogens; D016604:Aflatoxin B1; D011494:Protein Kinases; D011493:Protein Kinase C; D002122:Calcium Chloride