Document Detail


Study on ultrastructural cytochemistry and pathogenic mechanism of Trichomonas vaginalis.
MedLine Citation:
PMID:  9275338     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
OBJECTIVE: To study the relation among enzymic ultrastructural localizations, cell organelles and functions of Trichomonas vaginalis (T. vaginalis) as well as its pathogenic mechanism. MATERIAL AND METHODS: The specimens were Trichomonas vaginalis cultured purely for several generations. After prefixation, several electron microscopic cytochemical reactions for marker enzymes of lysosome, Golgi body, mitochondrion and microbody as well as Ur-Pb-Cu impregnation were undertaken. Then the specimens were post-fixed and embedded, and the unstained ultrathin sections were observed under a transmission electron microscope. RESULTS: The activities of acid phosphatase and cytidine monophosphatase appeared in the primary and secondary lysosomes of the parasite, and the reaction product of peroxidase was found in the secondary lysosomes. It was found that lysosomes could release hydrolytic enzymes out of the cell. The reaction products of thiamine pyrophosphatase and nicotinamide adenine dinucleotide phosphatase were located within the mature-surface and intermediate saccules of Golgi body respectively. The reactions for succinate dehydrogenase, cytochrome oxidase and catalase were negative. The hydrogenosomes, endoplasmic reticulum and Golgi bodies of the parasite were densely stained by Ur-Pb-Cu impregnation method. CONCLUSIONS: T.vaginalis has lysosomal system which can release hydrolases out of the parasite, causing damage to the vaginal and urethral epithelial cells. This may be an important pathogenic mechanism of vaginitis and urethritis caused by T.vaginalis. This protozoon has well-developed Golgi bodies and rich endoplasmic reticulum. It lacks mitochondrion and microbody, but has abundant hydrogenosomes which are energy producing organelles of anaerobic metabolism and resemble microbody in morphology and mitochondrion in some functions.
Authors:
W Chen; H Cai; J Chen; X Zhong; L Chen
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Chinese medical journal     Volume:  109     ISSN:  0366-6999     ISO Abbreviation:  Chin. Med. J.     Publication Date:  1996 Sep 
Date Detail:
Created Date:  1997-09-23     Completed Date:  1997-09-23     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7513795     Medline TA:  Chin Med J (Engl)     Country:  CHINA    
Other Details:
Languages:  eng     Pagination:  695-9     Citation Subset:  IM    
Affiliation:
Laboratory of Electron Microscopy, Fujian Medical College, Fuzhou.
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MeSH Terms
Descriptor/Qualifier:
Animals
Endopeptidases / analysis
Female
Glycoside Hydrolases / analysis
Histocytochemistry
Humans
Lysosomes / enzymology
Microscopy, Electron
Phospholipases / analysis
Trichomonas Vaginitis / parasitology
Trichomonas vaginalis / enzymology,  pathogenicity*,  ultrastructure*
Chemical
Reg. No./Substance:
EC 3.1.-/Phospholipases; EC 3.2.1.-/Glycoside Hydrolases; EC 3.4.-/Endopeptidases

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