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Sialic acid lyase in human promyelocytic leukemic cells (HL-60) during phorbol-ester-induced differentiation.

作者信息

Warren L

出版信息

Biochim Biophys Acta. 1986 Oct 10;888(3):278-81. doi: 10.1016/0167-4889(86)90226-0.

Abstract

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.

摘要

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