| Identification of Trichomonas vaginalis cysteine proteases that induce apoptosis in human vaginal epithelial cells. | |
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MedLine Citation:
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PMID: 15843376 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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A secreted cysteine protease (CP) fraction from Trichomonas vaginalis is shown here to induce apoptosis in human vaginal epithelial cells (HVEC) and is analyzed by mass spectrometry. The trichomonad parasite T. vaginalis causes one of the most common non-viral sexually transmitted infection in humans, trichomoniasis. The parasite as well as a secreted cysteine protease (CP) fraction, isolated by affinity chromatography followed by Bio-Gel P-60 column chromatography, are shown to induce HVEC apoptosis, as demonstrated by the Cell Death Detection ELISA(PLUS) assay and annexin V-fluorescein isothiocyanate flow cytometry analyses. Initiation of apoptosis is correlated with protease activity because the specific CP inhibitor E-64 inhibits both activities. SDS-PAGE analysis of the CP fraction reveals triplet bands around 30 kDa, and matrix-assisted laser desorption ionization time-of-flight MS indicates two closely associated peaks of molecular mass 23.6 and 23.8 kDa. Mass spectral peptide sequencing of the proteolytically digested CPs results in matches to previously reported cDNA clones, CP2, CP3, and CP4 (Mallinson, D. J., Lockwood, B. C., Coombs, G. H., and North, M. J. (1994) Microbiology 140, 2725-2735), as well as another sequence with high homology to CP4 (www.tigr.org). These last two species are the most abundant components of the CP fraction. The present results, suggesting that CP-induced programmed cell death may be involved in the pathogenesis of T. vaginalis infection in vivo, may have important implications for therapeutic intervention. |
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Authors:
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Ulf Sommer; Catherine E Costello; Gary R Hayes; David H Beach; Robert O Gilbert; John J Lucas; Bibhuti N Singh |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. Date: 2005-04-20 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 280 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2005 Jun |
Date Detail:
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Created Date: 2005-06-20 Completed Date: 2005-09-29 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 23853-60 Citation Subset: IM |
Affiliation:
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Mass Spectrometry Resource, Boston University School of Medicine, Boston, Massachusetts 02118, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Apoptosis / physiology* Cells, Cultured Cysteine Endopeptidases / chemistry, metabolism*, physiology Epithelial Cells / cytology Female Humans Molecular Sequence Data Sequence Homology, Amino Acid Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Trichomonas vaginalis / enzymology* Vagina / cytology* |
| Grant Support | |
ID/Acronym/Agency:
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AI47334/AI/NIAID NIH HHS; P41-RR10888/RR/NCRR NIH HHS; S10-RR015942/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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EC 3.4.22.-/Cysteine Endopeptidases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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