Shiga toxin activates p38 MAP kinase through cellular Ca2+ increase in Vero cells
| Autor: | Yoshifumi Takeda, Masahiro Ikeda, Yasuhiro Gunji, Shinji Yamasaki |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
MAPK/ERK pathway
p38 Mitogen-activated protein kinase Cell death Biophysics Mitogen-activated protein kinase kinase Biochemistry p38 Mitogen-Activated Protein Kinases Antioxidants MAP2K7 Extracellular signal-regulated kinase1/2 Structural Biology Chlorocebus aethiops Genetics Animals ASK1 Enzyme Inhibitors Phosphorylation Protein kinase A Molecular Biology Egtazic Acid Vero Cells Chelating Agents Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 MAP kinase kinase kinase biology Kinase Cyclin-dependent kinase 2 Cell Biology Shiga toxin Molecular biology Cell biology Enzyme Activation biology.protein Intracellular Ca2+ Calcium Mitogen-Activated Protein Kinases Reactive oxygen species Signal Transduction |
| Zdroj: | FEBS Letters. (1):94-98 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/S0014-5793(00)02204-3 |
| Popis: | We examined whether the mitogen-activated protein kinase (MAPK) pathway is involved in Shiga toxin (Stx)-induced Vero cell injury. Consonant with cell injury, Stx caused a transient extracellular signal-regulated kinase1/2 (ERK1/2) and a sustained p38 MAPK phosphorylation. p38 MAPK inhibitors (SB 203580 and PD 169316), but not an ERK1/2 kinase inhibitor (PD 98059), partially inhibited the Stx-induced cell death. BAPTA-AM, a Ca2+ chelator, reduced both cell injury and p38 MAPK phosphorylation. Antioxidants reduced Stx1-induced p38 MAPK phosphorylation. These data indicate that Stx activates p38 MAPK through an increase in intracellular Ca2+ and reactive oxygen species, and this signaling is involved in Stx-induced cell death. |
| Databáze: | OpenAIRE |
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