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Components of the mitogen-activated protein kinase cascade are activated in hepatic cells by Echinococcus

Ren-Yong Lin1, Jun-Hua Wang, Xiao-Mei Lu

  • 1Xinjiang Key Laboratory on Echinococcosis and Liver Surgery, 1st Teaching Hospital of Xinjiang Medical University, No.1 Liyushan Road, Urumqi 830054, China.

World Journal of Gastroenterology
|May 7, 2009
PubMed
Abstract

Insights

Echinococcus multilocularis parasite signals activate host liver cell mitogen-activated protein kinase (MAPK) pathways, including ERK and p38. This parasite-driven activation influences liver cell proliferation in alveolar echinococcosis.

Area of Science:

  • Parasitology
  • Molecular Biology
  • Hepatology

Background:

  • Alveolar echinococcosis (AE) is caused by Echinococcus multilocularis.
  • Host cell signaling pathways are crucial in parasitic infections.
  • Mitogen-activated protein kinase (MAPK) pathways regulate cell proliferation and survival.

Purpose of the Study:

  • To investigate the impact of E. multilocularis on host liver cell MAPK signaling.
  • To determine the effect of parasite-derived molecules on liver cell proliferation.

Main Methods:

  • Analysis of MAPK phosphorylation and PCNA expression in AE patient liver tissues.
  • In vitro studies using rat hepatocytes exposed to E. multilocularis vesicle fluid (EmF) and conditioned medium (EmCM).
  • Detection of phosphorylated MAPKs, MEK1/2, and RSK.

Main Results:

  • Activated ERK1/2 and p38 MAPK, with increased PCNA expression, were observed in AE patient livers.
  • In vitro, EmF induced p38, JNK, and ERK1/2 activation, along with MEK1/2 and RSK phosphorylation in hepatocytes.
  • EmCM exposure led to JNK up-regulation in hepatocytes without toxicity.

Conclusions:

  • Parasite-derived signals from E. multilocularis can activate host liver cell MAPK pathways.
  • This study demonstrates a parasite-to-host signaling mechanism impacting liver cells.
  • Findings suggest E. multilocularis actively manipulates host cell signaling for its own benefit.

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