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Proteasome serves as pivotal regulator in Angiostrongylus cantonensis-induced eosinophilic meningoencephalitis.
PLoS One. 2019; 14(8):e0220503.Plos

Abstract

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<0.05) compared with the untreated control. The phosphorylated nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) showed similar result. In addition, MMP-9 activity and occludin degradation were reduced because of MG132 treatment. These results suggested that the proteasome in A. cantonensis infection degraded phosphorylated IκBα, modulated phosphorylated NF-κB, and then regulated the activation of MMP-9 and occludin degradation. Proteasome alterations were presented in eosinophilic meningitis of BALB/c mice and may contribute to the pathophysiology of eosinophilic meningitis by increasing occludin degradation. This molecule would serve as pivotal regulator in A. cantonensis-induced eosinophilic meningoencephalitis.

Authors+Show Affiliations

Department of Neurology, Chung-Shan Medical University Hospital, Taichung, Taiwan.Department of Parasitology, Chung Shan Medical University, Taichung, Taiwan.Department of Parasitology, Chung Shan Medical University, Taichung, Taiwan.Department of Parasitology, Chung Shan Medical University, Taichung, Taiwan.Department of Parasitology, Chung Shan Medical University, Taichung, Taiwan.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31415587

Citation

Chen, An-Chih, et al. "Proteasome Serves as Pivotal Regulator in Angiostrongylus Cantonensis-induced Eosinophilic Meningoencephalitis." PloS One, vol. 14, no. 8, 2019, pp. e0220503.
Chen AC, Shyu LY, Lin YC, et al. Proteasome serves as pivotal regulator in Angiostrongylus cantonensis-induced eosinophilic meningoencephalitis. PLoS One. 2019;14(8):e0220503.
Chen, A. C., Shyu, L. Y., Lin, Y. C., Chen, K. M., & Lai, S. C. (2019). Proteasome serves as pivotal regulator in Angiostrongylus cantonensis-induced eosinophilic meningoencephalitis. PloS One, 14(8), e0220503. https://doi.org/10.1371/journal.pone.0220503
Chen AC, et al. Proteasome Serves as Pivotal Regulator in Angiostrongylus Cantonensis-induced Eosinophilic Meningoencephalitis. PLoS One. 2019;14(8):e0220503. PubMed PMID: 31415587.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Proteasome serves as pivotal regulator in Angiostrongylus cantonensis-induced eosinophilic meningoencephalitis. AU - Chen,An-Chih, AU - Shyu,Ling-Yuh, AU - Lin,Yi-Chieh, AU - Chen,Ke-Min, AU - Lai,Shih-Chan, Y1 - 2019/08/15/ PY - 2018/12/04/received PY - 2019/07/17/accepted PY - 2019/8/16/entrez PY - 2019/8/16/pubmed PY - 2020/3/7/medline SP - e0220503 EP - e0220503 JF - PloS one JO - PLoS One VL - 14 IS - 8 N2 - 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<0.05) compared with the untreated control. The phosphorylated nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) showed similar result. In addition, MMP-9 activity and occludin degradation were reduced because of MG132 treatment. These results suggested that the proteasome in A. cantonensis infection degraded phosphorylated IκBα, modulated phosphorylated NF-κB, and then regulated the activation of MMP-9 and occludin degradation. Proteasome alterations were presented in eosinophilic meningitis of BALB/c mice and may contribute to the pathophysiology of eosinophilic meningitis by increasing occludin degradation. This molecule would serve as pivotal regulator in A. cantonensis-induced eosinophilic meningoencephalitis. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/31415587/Proteasome_serves_as_pivotal_regulator_in_Angiostrongylus_cantonensis_induced_eosinophilic_meningoencephalitis_ L2 - https://dx.plos.org/10.1371/journal.pone.0220503 DB - PRIME DP - Unbound Medicine ER -