Proteasome serves as pivotal regulator in Angiostrongylus cantonensis-induced eosinophilic meningoencephalitis

Proteasome primarily degrades the unneeded or damaged proteins by proteolysis. Disruption of the brain barrier and its resulting meningoencephalitis caused by Angiostrongylus cantonensis are important pathological events in non-permissive hosts. In this study, the results showed upregulated proteaso...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2019-08, Vol.14 (8), p.e0220503-e0220503
Main Authors: Chen, An-Chih, Shyu, Ling-Yuh, Lin, Yi-Chieh, Chen, Ke-Min, Lai, Shih-Chan
Format: Article
Language:English
Subjects:
Angiostrongylus cantonensis
Animals
B cells
Biology and Life Sciences
Brain
Brain - drug effects
Brain - metabolism
Brain damage
Care and treatment
Causes of
Cell activation
Cell growth
Cerebrospinal fluid
Cysteine Proteinase Inhibitors - pharmacology
Degradation
Disease Models, Animal
Disruption
Encephalitis
Enzymes
Gelatinase B
Health aspects
Infection
Infections
Inflammation
Laboratory animals
Leukocytes (eosinophilic)
Leupeptins - pharmacology
Lymphocytes B
Male
Matrix metalloproteinase
Matrix Metalloproteinase 9 - metabolism
Matrix metalloproteinases
Medicine and Health Sciences
Meningitis
Meningoencephalitis
Meningoencephalitis - metabolism
Meningoencephalitis - parasitology
Metalloproteinase
Mice
Microscopy
NF-kappa B - metabolism
NF-κB protein
Occludin - metabolism
Parasitology
Phosphorylation
Polyclonal antibodies
Proteasome Endopeptidase Complex - metabolism
Proteasomes
Proteins
Proteolysis
Research and Analysis Methods
Strongylida Infections - metabolism
Transcription factors
Ubiquitin-proteasome system
Up-Regulation
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Proteasome primarily degrades the unneeded or damaged proteins by proteolysis. Disruption of the brain barrier and its resulting meningoencephalitis caused by Angiostrongylus cantonensis are important pathological events in non-permissive hosts. In this study, the results showed upregulated proteasome during A. cantonensis infection. Occludin degradation and matrix metalloproteinase-9 (MMP-9) activity were significantly increased in infected mice than in uninfected mice. Moreover, confocal immunoflourescence microscopy showed that occludin was co-localized with MMP-9. The infected-mice were treated with proteasomal activity inhibitor MG132 by 1.5 and 3.0 mg/kg/day, which resulted in significantly reduced protein levels of phosphorylated IκBα (P
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0220503