期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 385, 期 4, 页码 503-506出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.05.121
关键词
p38 MAPK; Bacterial pore-forming toxins; Potassium K+; Staphylococcus aureus alpha-toxin; Escherichia coli hemolysin A; Streptolysin O; Vibrio cholerae cytolysin; Osmotic stress
Mitogen activated protein kinase (MAPK) p38 has emerged as a survival protein in cells that are attacked by bacterial toxins forming small membrane pores. Activation of p38 by pore forming toxins (PFT) has been attributed to osmotic stress, but here we show that loss of K+ is likely to be the critical parameter. Several lines of evidence support this conclusion: First, osmoprotection did not prevent p38-phosphorylation in alpha-toxin-loaded cells. Second, treatment of cells with a K+ ionophore, or simple incubation in K+-free medium sufficed to cause robust p38-phosphorylation. Third, media containing high [K+] prevented p38-activation by Staphylococcus aureus alpha-toxin, Vibrio cholerae cytolysin (VCC), Streptolysin O (SLO), or Escherichia coli hemolysin (HlyA), but did not impair activation by H2O2. Fourth, potential roles of LPS, TLR4, or calcium-influx were ruled out. Therefore, we propose that PFT trigger the p38 MAPK-pathway by causing loss of cellular K+. (c) 2009 Elsevier Inc. All rights reserved.
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