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Excretory-Secretory Products Produced by Paragonimus westermani Differentially Regulate the Nitric Oxide Production and Viability of Microglial Cells

Authors
 Jin Y.  ;  Lee J.-C.  ;  Choi I.Y.  ;  Kim E.A.  ;  Shin M.H.  ;  Kim W.-K. 
Citation
 INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY, Vol.139(1) : 16-24, 2006 
Journal Title
INTERNATIONAL ARCHIVES OF ALLERGY AND IMMUNOLOGY
ISSN
 1018-2438 
Issue Date
2006
MeSH
Animals ; Biological Factors/metabolism* ; Biological Factors/pharmacology* ; Cells, Cultured ; Hot Temperature ; L-Lactate Dehydrogenase/analysis ; L-Lactate Dehydrogenase/metabolism ; Microglia/metabolism* ; Microglia/pathology* ; Necrosis/pathology* ; Nitrates/analysis ; Nitrates/metabolism ; Nitric Oxide/metabolism* ; Paragonimus westermani/metabolism* ; Rats ; Rats, Sprague-Dawley
Abstract
BACKGROUND: Tissue-invading helminth parasites secrete a large amount of cysteine proteases that may play critical roles in tissue invasion and immune modulation. However, roles of excretory-secretory products (ESP) secreted by Paragonimus westermani in the activation and death of microglial cells in brain are poorly understood.
OBJECTIVES: In the present study, we investigated whether ESP could regulate microglial nitric oxide (NO) production and viability.
METHODS: The NO production and cell viability were assessed by respectively measuring the formation of nitrite and the release of lactate dehyrogenase.
RESULTS: At a low (0.2 microg/ml) concentration, ESP significantly stimulated NO production with no apparent cell injury or death in cultured microglial cells. However, at high (> or =2 microg/ml) concentrations, ESP induced severe cell death. Inhibition of inducible NO synthase significantly reduced the NO productivity, but not cytotoxicity, of ESP. Similarly, inhibitors of the extracellular signal-regulated kinase, p38 and nuclear factor kappa B also blocked only the NO productivity of ESP. Interestingly, heat inactivation did not hamper the ability of ESP to stimulate microglial NO production. Similarly, pretreatment with thiol-crosslinking reagents dramatically reduced both proteolytic activity and cytotoxicity of ESP, but did not alter NO production in microglial cells. Interestingly, although cysteine protease competitive inhibitors and thiol-alkylating reagents markedly reduced the proteolytic activity of ESP, they did not influence the NO productivity and cytotoxicity of ESP.
CONCLUSION: The present results indicate that the NO production and cytotoxicity by ESP may be differentially regulated via unknown mechanisms, not related with cysteine protease activity.
Full Text
http://www.karger.com/Article/FullText/89518
DOI
10.1159/000089518
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Tropica Medicine (열대의학교실) > 1. Journal Papers
Yonsei Authors
Shin, Myeong Heon(신명헌) ORCID logo https://orcid.org/0000-0001-8207-6110
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/109337
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