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Journal of Experimental Hematology ; (6): 65-68, 2009.
Article in Chinese | WPRIM | ID: wpr-302196

ABSTRACT

The study was aimed to explore the mechanism of SYK and CBL family of ubiquitin ligases in Bufalin-induced HL-60 cells apoptosis. Cell viability was tested by trypan blue staining and apoptosis was detected by using flow cytometry. The expressions of CBL and CBL-b and the phosphorylation of SYK were detected by using immunoprecipitation and Western blot. The results showed that Bufalin inhibited HL-60 cell proliferation in time- and dose-dependent manners. IC(50) of suppressing cell viability at 24, 48 and 72 hours were about 26.3, 7.8 and 2.0 nmol/L respectively. The high dose of bufalin already induced apoptosis of HL-60 cells at 8 hours. SYK was quickly phosphorylated, and the expressions of CBL and CBL-b were down-regulated after treatment with Bufalin. It is concluded that SYK activation and CBL protein down-regulation may be involved in Bufalin-induced HL-60 cell apoptosis.


Subject(s)
Humans , Apoptosis , Bufanolides , Pharmacology , Cell Proliferation , Down-Regulation , Gene Expression Regulation, Leukemic , HL-60 Cells , Intracellular Signaling Peptides and Proteins , Metabolism , Protein-Tyrosine Kinases , Metabolism , Proto-Oncogene Proteins c-cbl , Metabolism , Signal Transduction , Syk Kinase
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