Calcium-activated, phospholipid-dependent protein kinase activity and protein phosphorylation in HL60 cells induced to differentiate by retinoic acid.
Treatment of human promyelocytic (HL60) cells with retinoic acid for at least 48 h causes differentiation to more mature myeloid forms. Prior to commitment of cells to the myeloid pathway there is a marked increase in cytosolic calcium-activated, phospholipid-dependent protein kinase activity. This increase does not result from an intracellular redistribution of the enzyme. Concomitant with the increased enzyme activity there is enhanced phospholipid-dependent phosphorylation of proteins of 29, 49, 52, 58, 68, 69, 120, 170, 200 and 245 kDa.
Durham
J P
JP
Emler
C A
CA
Butcher
F R
FR
Fontana
J A
JA
D002118:Calcium / Q000494:pharmacology*; D002454:Cell Differentiation / Q000187:drug effects; D002460:Cell Line; D003600:Cytosol / Q000201:enzymology; D006098:Granulocytes / Q000166:cytology / Q000201:enzymology*; D006801:Humans; D010743:Phospholipids / Q000494:pharmacology*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D006656:Protamine Kinase; D011494:Protein Kinases / Q000378:metabolism*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology; D014212:Tretinoin / Q000494:pharmacology*
D010743:Phospholipids; D010750:Phosphoproteins; D014212:Tretinoin; D011494:Protein Kinases; D006656:Protamine Kinase; D013755:Tetradecanoylphorbol Acetate; D002118:Calcium