Sialic acid lyase in human promyelocytic leukemic cells (HL-60) during phorbol-ester-induced differentiation.
There is a marked increase in the activity of sialic acid lyase (N-acetylneuraminate lyase; EC 4.1.3.3; also known as sialic acid aldolase) in HL-60 cells induced to differentiate into macrophages by the phorbol ester, tetradecanoylphorbol 12-myristate 13 acetate (TPA). Exposure of HL-60 cells to retinoic acid, butyric acid or dimethyl sulfoxide has little or no effect. The level of the enzyme remains unaltered in HL-60 cells grown in the presence of an inactive analog of TPA, nor does it change in variants of HL-60 cells resistant to TPA.
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D002087:Butyrates / Q000494:pharmacology; D020148:Butyric Acid; D002454:Cell Differentiation / Q000187:drug effects*; D002460:Cell Line; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D006801:Humans; D007945:Leukemia, Lymphoid / Q000201:enzymology*; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D010703:Phorbol Esters / Q000494:pharmacology; D012799:Sialyltransferases / Q000378:metabolism; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*; D014212:Tretinoin / Q000494:pharmacology; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D002087:Butyrates; D010703:Phorbol Esters; D020148:Butyric Acid; C008876:phorbol-12,13-didecanoate; D014212:Tretinoin; D012799:Sialyltransferases; D007652:Oxo-Acid-Lyases; C018728:N-acetylneuraminate lyase; D013755:Tetradecanoylphorbol Acetate; D004121:Dimethyl Sulfoxide; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase