The regulation of thymidine kinase in HL-60 human promyeloleukemia cells

Zee Fen Chang*, Duen Yi Huang

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

27 Scopus citations


It has been well established that the regulation of thymidine kinase (TK) expression is highly growth-dependent. In this report, we present evidence that TK expression in undifferentiated HL-60 cells is not stringently controlled in a growth-dependent manner, except for a very moderate activation of TK in response to growth stimulation. Moreover, we have demonstrated for the first time that TK becomes phosphorylated, and the fluctuation of TK activity in these cells is related to the extent of phosphorylation of seryl residues of the TK polypeptide. This is further reinforced by the observation that the presence of Ser/Thr phosphatases inhibitor in the crude extract increases TK activity. Our data suggest that post-translational modification by phosphorylation is implicated in TK regulation in HL-60 cells.

Original languageEnglish
Pages (from-to)1266-1271
Number of pages6
JournalJournal of Biological Chemistry
Issue number2
StatePublished - 15 01 1993


Dive into the research topics of 'The regulation of thymidine kinase in HL-60 human promyeloleukemia cells'. Together they form a unique fingerprint.

Cite this