VvpM Induces Human Cell Death via Multifarious Modes Including Necroptosis and Autophagy

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Bibliographic Details
Title: VvpM Induces Human Cell Death via Multifarious Modes Including Necroptosis and Autophagy
Authors: Jeong-A Kim, Mee-Young Shin, Soon-Jung Park, Mi-Ae Lee, Jeong K. Lee, Kyu-Ho Lee
Contributors: Mi Ae Lee, Jeong A Kim, Mee Young Shin, Jeong K Lee, Soon Jung Park, Kyu Ho Lee, Park, Soon Jung, Shin, Mee Young
Source: Journal of Microbiology and Biotechnology. 25:302-306
Publisher Information: Korean Society for Microbiology and Biotechnology, 2015.
Publication Year: 2015
Subject Terms: 0301 basic medicine, autophagy, Indoles, Vibrio vulnificus/pathogenicity, Cell Survival, necroptosis, Apoptosis, Autophagy, Cell Line, Cytochromes c/metabolism, Necrosis, 03 medical and health sciences, Vibrio vulnificus/enzymology, Cell Line, Tumor, Humans, Vibrio vulnificus, Imidazoles/pharmacology, 0303 health sciences, Tumor, Indoles/pharmacology, Cell Death, Metalloproteases/metabolism, Caspase 3, Caspases/metabolism, Imidazoles, Cytochromes c, 3. Good health, Caspases, Metalloproteases, Vibrio vulnificus/metabolism, metalloprotease VvpM, Caspase 3/metabolism
Description: VvpM, one of the extracellular metalloproteases produced by Vibrio vulnificus, induces apoptotic cell death via a pathway consisting of ERK activation, cytochrome c release, and activation of caspases-9 and -3. VvpM-treated cells also showed necrotic cell death as stained by propidium iodide (PI). The percentage of PI-stained cells was decreased by pretreatment with Necrostatin-1, indicating that VvpM-mediated cell death occurs through necroptosis. The appearance of autophagic vesicles and lipidated form of light-chain-3B in rVvpM-treated cells suggests an involvement of autophagy in this process. Therefore, the multifarious action of VvpM might be one of the factors responsible for V. vulnificus pathogenesis.
Document Type: Article
File Description: 302~306
Language: English
ISSN: 1738-8872
1017-7825
DOI: 10.4014/jmb.1501.01007
Access URL: https://pubmed.ncbi.nlm.nih.gov/25649984
https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART001966598
https://www.ncbi.nlm.nih.gov/pubmed/25649984
https://europepmc.org/article/MED/25649984
http://www.jmb.or.kr/journal/view.html?doi=10.4014/jmb.1501.01007
Rights: CC BY NC ND
Accession Number: edsair.doi.dedup.....01d656526bb15a8e56a20a2b73ec1234
Database: OpenAIRE
Description
Abstract:VvpM, one of the extracellular metalloproteases produced by Vibrio vulnificus, induces apoptotic cell death via a pathway consisting of ERK activation, cytochrome c release, and activation of caspases-9 and -3. VvpM-treated cells also showed necrotic cell death as stained by propidium iodide (PI). The percentage of PI-stained cells was decreased by pretreatment with Necrostatin-1, indicating that VvpM-mediated cell death occurs through necroptosis. The appearance of autophagic vesicles and lipidated form of light-chain-3B in rVvpM-treated cells suggests an involvement of autophagy in this process. Therefore, the multifarious action of VvpM might be one of the factors responsible for V. vulnificus pathogenesis.
ISSN:17388872
10177825
DOI:10.4014/jmb.1501.01007