C-jun N-terminal kinase-mediated signaling is essential for Staphylococcus aureus-induced U937 apoptosis.
- Author:
Jia-he WANG
1
;
Bo YU
;
Hui-yan NIU
;
Hui LI
;
Yi ZHANG
;
Xin WANG
;
Ping HE
Author Information
- Publication Type:Journal Article
- MeSH: Anthracenes; pharmacology; Apoptosis; physiology; Caspase 3; metabolism; Humans; JNK Mitogen-Activated Protein Kinases; metabolism; Macrophages; cytology; metabolism; microbiology; Mitogen-Activated Protein Kinase 8; antagonists & inhibitors; metabolism; Mitogen-Activated Protein Kinase 9; antagonists & inhibitors; metabolism; Phosphorylation; drug effects; Protein Kinase Inhibitors; pharmacology; Signal Transduction; physiology; Staphylococcus aureus; physiology; U937 Cells; bcl-2-Associated X Protein; metabolism
- From: Chinese Medical Sciences Journal 2009;24(1):26-29
- CountryChina
- Language:English
-
Abstract:
OBJECTIVETo investigate the effect of SP600125, a specific c-jun N-terminal protein kinase (JNK) inhibitor, on Staphylococcus aureus (S. aureus)-induced U937 cell death and the underlying mechanism.
METHODSThe human monocytic U937 cells were treated with S. aureus at different time with or without SP600125. Cell apoptosis was analyzed by flow cytometry. JNK, Bax, and caspase-3 activities were detected by Western blotting.
RESULTSS. aureus induced apoptosis in cultured U937 cells in a time-dependent manner. Expression of Bax and phospho-JNK significantly increased in S. aureus-treated U937 cells, and the level of activated caspase-3 also increased in a time-dependent manner. Inhibition of JNK with SP600125 significantly inhibited S. aureus-induced apoptosis in U937 cells.
CONCLUSIONSS. aureus can induce apoptosis in U937 cells by phosphorylation of JNK and activation of Bax and caspase-3. SP600125 protects U937 cells from apoptosis induced by S. aureus via inhibiting the activity of JNK.
