Trichomonas vaginalis Metalloproteinase Induces mTOR Cleavage of SiHa Cells

Trichomonas vaginalis secretes a number of proteases which are suspected to be the cause of pathogenesis; however, little is understood how they manipulate host cells. The mammalian target of rapamycin (mTOR) regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis,...

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Bibliographic Details
Published in:Korean journal of parasitology 2014, Hosts and Diseases, 52(6), , pp.595-603
Main Authors: Quan, Juan-Hua, Choi, In-Wook, Yang, Jung-Bo, Zhou, Wei, Cha, Guang-Ho, Zhou, Yu, Ryu, Jae-Sook, Lee, Young-Ha
Format: Article
Language:English
Subjects:
Blotting, Western
Cell Line, Tumor
Epithelial Cells - metabolism
Epithelial Cells - parasitology
Humans
Metalloproteases - genetics
Metalloproteases - metabolism
Original
Proteolysis
Sequence Analysis, DNA
TOR Serine-Threonine Kinases - metabolism
Trichomonas vaginalis - enzymology
Trichomonas vaginalis - genetics
예방의학
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Summary:Trichomonas vaginalis secretes a number of proteases which are suspected to be the cause of pathogenesis; however, little is understood how they manipulate host cells. The mammalian target of rapamycin (mTOR) regulates cell growth, cell proliferation, cell motility, cell survival, protein synthesis, and transcription. We detected various types of metalloproteinases including GP63 protein from T. vaginalis trophozoites, and T. vaginalis GP63 metalloproteinase was confirmed by sequencing and western blot. When SiHa cells were stimulated with live T. vaginalis, T. vaginalis excretory-secretory products (ESP) or T. vaginalis lysate, live T. vaginalis and T. vaginalis ESP induced the mTOR cleavage in both time- and parasite load-dependent manner, but T. vaginalis lysate did not. Pretreatment of T. vaginalis with a metalloproteinase inhibitor, 1,10-phenanthroline, completely disappeared the mTOR cleavage in SiHa cells. Collectively, T. vaginalis metallopeptidase induces host cell mTOR cleavage, which may be related to survival of the parasite.
ISSN:0023-4001
1738-0006
2982-5164
1738-0006
2982-6799
DOI:10.3347/kjp.2014.52.6.595