Cdk7- and Cdc25A-Independent Dephosphorylation of Cdk2 during
Phorbol Ester-Mediated Cell Cycle Arrest in U937 Cells
- Affiliated Author(s)
- 권택규; 박종욱
- Alternative Author(s)
- Kwon, Taeg Kyu; Park, Jong Wook
- Journal Title
- Experimental Cell Research
- ISSN
- 0014-4827
- Issued Date
- 2000
- Abstract
- The molecular mechanism underlying protein kinase
C (PKC)-mediated cell cycle arrest is poorly understood.
We undertook to characterize phorbol esteractivated
PKC-mediated cell cycle arrest. Treatment
with phorbol ester inhibited cell growth of human
histiocytic lymphoma U937 cells with 83% of the cells
arrested in G1 phase. Reduced activity of cdk2 correlated
with cdk2 dephosphorylation and accumulation
of cdk2 inhibitor p21Waf in phorbol ester-treated cells.
Dephosphorylation of cdk2 was not associated with
cdk7 and cdc25A activity in phorbol ester-treated
cells. Protein phosphatase inhibitor assays suggest
that the dephosphorylation of cdk2 results in the activation
of a specific protein tyrosine phosphatase.
Thus, dephosphorylation of cdk2 as well as accumulation
of cdk2 inhibitor is likely to contribute to the G1
phase arrest in phorbol ester-treated in U937 cells.
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