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VvpM, an extracellular metalloprotease of Vibrio vulnificus, induces apoptotic death of human cells.

Authors
 Mi Ae Lee  ;  Jeong A Kim  ;  Yu Jin Yang  ;  Mee Young Shin  ;  Soon Jung Park  ;  Kyu Ho Lee 
Citation
 JOURNAL OF MICROBIOLOGY, Vol.52(12) : 1036-1043, 2014 
Journal Title
 JOURNAL OF MICROBIOLOGY 
ISSN
 1225-8873 
Issue Date
2014
MeSH
Amino Acid Sequence ; Annexin A5/analysis ; Apoptosis*/physiology ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism* ; Caspase 3/metabolism ; Caspase 9/metabolism ; Computer Simulation ; Cytochromes c/metabolism ; Cytosol/metabolism ; Enzyme Activation ; HCT116 Cells ; HT29 Cells ; Humans ; Metalloproteases/chemistry ; Metalloproteases/genetics ; Metalloproteases/isolation & purification ; Metalloproteases/metabolism* ; Microscopy, Electron, Transmission ; Mitochondria/metabolism ; Molecular Sequence Data ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Sequence Alignment ; Signal Transduction ; Vibrio vulnificus/enzymology* ; Vibrio vulnificus/pathogenicity*
Keywords
metalloprotease ; apoptosis ; Vibrio vulnificus
Abstract
A pathogenic bacterium, Vibrio vulnificus produces various extracellular proteases including the elastolytic metalloprotease, VvpE. In silico analysis of its genome revealed a VvpE-homologous protease, VvpM whose proteolytic activity was abolished by specific inhibitors against metalloproteases. To investigate whether this newly identified protease has pathogenic role in host interaction in addition to proteolytic role, human cell lines were incubated with recombinant VvpM (rVvpM). rVvpM-challenged cells showed typical morphological changes found in cells under apoptosis. Apoptotic cell death was further evidenced by estimating the Annexin V-stained cells, whose proportions were dependent upon the concentrations of rVvpM treated to human cells. To elucidate the signaling pathway for VvpM-induced apoptosis, three MAPKs were tested if their activation were mediated by rVvpM. ERK1/2 was phosphorylated by treatment of rVvpM and rVvpM-induced cell death was blocked by a specific inhibitor against ERK1/2. In rVvpM-treated cells, the cytosolic levels of cytochrome c were increased in a VvpM concentration-dependent manner, while the levels of cytochrome c in mitochondria were decreased. Cell deaths were accompanied by apparent cleavages of procaspases-9 and -3 to the active caspases-9 and -3, respectively. Therefore, this study demonstrates that an extracellular metalloprotease of V. vulnificus, VvpM induces apoptosis of human cells via a pathway consisting of ERK activation, cytochrome c release, and then activation of caspases-9 and -3.
Full Text
http://link.springer.com/article/10.1007/s12275-014-4531-0
DOI
10.1007/s12275-014-4531-0
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Park, Soon Jung(박순정) ORCID logo https://orcid.org/0000-0002-0423-1944
Shin, Mee Young(신미영) ORCID logo https://orcid.org/0000-0003-3676-2683
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/138869
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