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TRICHOMONAS VAGINALIS: IDENTIFICATION OF A PHOSPHOLIPASE A–DEPENDENT HEMOLYTIC ACTIVITY IN A VESICULAR SUBCELLULAR FRACTION
Trichomonad total extracts (TTE), or vesicular (P30) and soluble (S30) subcellular fractions from 3 pathogenic Trichomonas vaginalis strains (GT-3, GT-13, and GT-15), lysed both human and Sprague–Dawley rat erythrocytes in a time- and dose-dependent manner. The entire hemolytic activity of TTE was l...
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| Published in: | The Journal of parasitology 2003-02, Vol.89 (1), p.105-112 |
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| container_title | The Journal of parasitology |
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| creator | Vargas-Villarreal, Javier Mata-Cárdenas, Benito D González-Salazar, Francisco Lozano-Garza, Héctor G Cortes-Gutierrez, Elva I Palacios-Corona, Rebeca Martínez-Rodríguez, Herminia G Ramírez-Bon, Enrique Said-Fernández, Salvador |
| description | Trichomonad total extracts (TTE), or vesicular (P30) and soluble (S30) subcellular fractions from 3 pathogenic Trichomonas vaginalis strains (GT-3, GT-13, and GT-15), lysed both human and Sprague–Dawley rat erythrocytes in a time- and dose-dependent manner. The entire hemolytic activity of TTE was located in P30, showing 2 peaks of maximum activity, one at pH 6.0 and another at pH 8.0, in the presence of 1 mM Ca2+. Hemolytic activity on rat erythrocytes was greater at pH 6.0 (6.71 ± 0.33 hemolytic units [HU]/mg/hr to 11.60 ± 0.24 HU/mg/hr) than at pH 8.0 (3.81 ± 0.30 HU/mg/hr to 5.75 ± 0.65 HU/mg/hr), and it was greater than that on human red blood cells at pH 6.0 (2.67 ± 0.19 HU/mg/hr to 4.08 ± 0.15 HU/mg/hr) or pH 8.0 (2.24 ± 0.09 HU/mg/hr to 2.81 ± 0.06 HU/mg/hr). The alkaline and acidic hemolytic activity diminished (60–93% at pH 6.0 and 78–93% at pH 8.0) by the effect of 80 μM Rosenthal's inhibitor, which also inhibited 27–45% and 29–54% trichomonad alkaline and acidic phospholipase A activities, respectively. Vesicles, vacuoles, and hydrogenosomes were rich in P30. Trichomonas vaginalis has a hemolytic PLA, which could be involved in its cytopathogenic mechanism. |
| doi_str_mv | 10.1645/0022-3395(2003)089[0105:TVIOAP]2.0.CO;2 |
| format | article |
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The entire hemolytic activity of TTE was located in P30, showing 2 peaks of maximum activity, one at pH 6.0 and another at pH 8.0, in the presence of 1 mM Ca2+. Hemolytic activity on rat erythrocytes was greater at pH 6.0 (6.71 ± 0.33 hemolytic units [HU]/mg/hr to 11.60 ± 0.24 HU/mg/hr) than at pH 8.0 (3.81 ± 0.30 HU/mg/hr to 5.75 ± 0.65 HU/mg/hr), and it was greater than that on human red blood cells at pH 6.0 (2.67 ± 0.19 HU/mg/hr to 4.08 ± 0.15 HU/mg/hr) or pH 8.0 (2.24 ± 0.09 HU/mg/hr to 2.81 ± 0.06 HU/mg/hr). The alkaline and acidic hemolytic activity diminished (60–93% at pH 6.0 and 78–93% at pH 8.0) by the effect of 80 μM Rosenthal's inhibitor, which also inhibited 27–45% and 29–54% trichomonad alkaline and acidic phospholipase A activities, respectively. Vesicles, vacuoles, and hydrogenosomes were rich in P30. Trichomonas vaginalis has a hemolytic PLA, which could be involved in its cytopathogenic mechanism.</description><identifier>ISSN: 0022-3395</identifier><identifier>EISSN: 1937-2345</identifier><identifier>DOI: 10.1645/0022-3395(2003)089[0105:TVIOAP]2.0.CO;2</identifier><identifier>PMID: 12659311</identifier><identifier>CODEN: JOPAA2</identifier><language>eng</language><publisher>Lawrence, KS: American Society of Parasitologists</publisher><subject>Animals ; Biochemistry ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Calcium - metabolism ; Dose-Response Relationship, Drug ; Enzymes ; Epithelial cells ; Erythrocytes ; Erythrocytes - metabolism ; Fundamental and applied biological sciences. Psychology ; Hemolysin proteins ; Hemolysis ; Hemolysis - physiology ; Humans ; Hydrogen-Ion Concentration ; Invertebrates ; Nemathelminthia. Plathelmintha ; Parasitism ; Parasitology ; PATHOLOGY ; Phospholipases A - antagonists & inhibitors ; Phospholipases A - metabolism ; Physiology. Development ; Rats ; Stearates - pharmacology ; Subcellular fractions ; Trichomonas vaginalis - enzymology ; Trichomonas vaginalis - metabolism ; Trichomonas vaginalis - pathogenicity ; Virulence</subject><ispartof>The Journal of parasitology, 2003-02, Vol.89 (1), p.105-112</ispartof><rights>American Society of Parasitologists</rights><rights>Copyright 2003 American Society of Parasitologists</rights><rights>2003 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3286090$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3286090$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,58238,58471</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14651764$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12659311$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Vargas-Villarreal, Javier</creatorcontrib><creatorcontrib>Mata-Cárdenas, Benito D</creatorcontrib><creatorcontrib>González-Salazar, Francisco</creatorcontrib><creatorcontrib>Lozano-Garza, Héctor G</creatorcontrib><creatorcontrib>Cortes-Gutierrez, Elva I</creatorcontrib><creatorcontrib>Palacios-Corona, Rebeca</creatorcontrib><creatorcontrib>Martínez-Rodríguez, Herminia G</creatorcontrib><creatorcontrib>Ramírez-Bon, Enrique</creatorcontrib><creatorcontrib>Said-Fernández, Salvador</creatorcontrib><title>TRICHOMONAS VAGINALIS: IDENTIFICATION OF A PHOSPHOLIPASE A–DEPENDENT HEMOLYTIC ACTIVITY IN A VESICULAR SUBCELLULAR FRACTION</title><title>The Journal of parasitology</title><addtitle>J Parasitol</addtitle><description>Trichomonad total extracts (TTE), or vesicular (P30) and soluble (S30) subcellular fractions from 3 pathogenic Trichomonas vaginalis strains (GT-3, GT-13, and GT-15), lysed both human and Sprague–Dawley rat erythrocytes in a time- and dose-dependent manner. The entire hemolytic activity of TTE was located in P30, showing 2 peaks of maximum activity, one at pH 6.0 and another at pH 8.0, in the presence of 1 mM Ca2+. Hemolytic activity on rat erythrocytes was greater at pH 6.0 (6.71 ± 0.33 hemolytic units [HU]/mg/hr to 11.60 ± 0.24 HU/mg/hr) than at pH 8.0 (3.81 ± 0.30 HU/mg/hr to 5.75 ± 0.65 HU/mg/hr), and it was greater than that on human red blood cells at pH 6.0 (2.67 ± 0.19 HU/mg/hr to 4.08 ± 0.15 HU/mg/hr) or pH 8.0 (2.24 ± 0.09 HU/mg/hr to 2.81 ± 0.06 HU/mg/hr). The alkaline and acidic hemolytic activity diminished (60–93% at pH 6.0 and 78–93% at pH 8.0) by the effect of 80 μM Rosenthal's inhibitor, which also inhibited 27–45% and 29–54% trichomonad alkaline and acidic phospholipase A activities, respectively. Vesicles, vacuoles, and hydrogenosomes were rich in P30. Trichomonas vaginalis has a hemolytic PLA, which could be involved in its cytopathogenic mechanism.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Calcium - metabolism</subject><subject>Dose-Response Relationship, Drug</subject><subject>Enzymes</subject><subject>Epithelial cells</subject><subject>Erythrocytes</subject><subject>Erythrocytes - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemolysin proteins</subject><subject>Hemolysis</subject><subject>Hemolysis - physiology</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Invertebrates</subject><subject>Nemathelminthia. Plathelmintha</subject><subject>Parasitism</subject><subject>Parasitology</subject><subject>PATHOLOGY</subject><subject>Phospholipases A - antagonists & inhibitors</subject><subject>Phospholipases A - metabolism</subject><subject>Physiology. Development</subject><subject>Rats</subject><subject>Stearates - pharmacology</subject><subject>Subcellular fractions</subject><subject>Trichomonas vaginalis - enzymology</subject><subject>Trichomonas vaginalis - metabolism</subject><subject>Trichomonas vaginalis - pathogenicity</subject><subject>Virulence</subject><issn>0022-3395</issn><issn>1937-2345</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNpFkc1q20AQx5fS0jhp36CUvbSkBzmzX5I3PW0VOV5QtMaSDaGURR8rcLCtVLIPPRT6Dn3DPkml2k0OwyzM778D80PoisCY-FxcAVDqMSbFJQVgn2AivwIBcZ2ttFHzb3QM49B8pi_QiEgWeJRx8RKNnlJn6LzrHgBA9PUanRHqC8kIGaGf2UKHM3NnEpXilbrViYp1eo31TZRkeqpDlWmTYDPFCs9nJu0r1nOVRlj9-fX7JppHyUDiWXRn4vtMh1iFmV7p7B7rpM-solSHy1gtcLr8EkZx_O89XQyUSd6gV3W-6dzbU79Ay2mUhTMvNrf96tgrGIW9VxW1JCWZQM4Dv2LS1T7kfkAqSgWUeVGLuqyE4wVjIuC8pNzxgLuA-lIWnHB2gT4e_31sm-8H1-3tdt2VbrPJd645dDZghPf3kD34_gQeiq2r7GO73ubtD_v_YD3w4QTkXZlv6jbflevumeO-IIE_bHx35B66fdM-zRmd-CChH0fHcbFump17zoMdfNvBnB3M2cG37X3bwbc9-rbUgg2Npewv-V-Tlw</recordid><startdate>20030201</startdate><enddate>20030201</enddate><creator>Vargas-Villarreal, Javier</creator><creator>Mata-Cárdenas, Benito D</creator><creator>González-Salazar, Francisco</creator><creator>Lozano-Garza, Héctor G</creator><creator>Cortes-Gutierrez, Elva I</creator><creator>Palacios-Corona, Rebeca</creator><creator>Martínez-Rodríguez, Herminia G</creator><creator>Ramírez-Bon, Enrique</creator><creator>Said-Fernández, Salvador</creator><general>American Society of Parasitologists</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20030201</creationdate><title>TRICHOMONAS VAGINALIS: IDENTIFICATION OF A PHOSPHOLIPASE A–DEPENDENT HEMOLYTIC ACTIVITY IN A VESICULAR SUBCELLULAR FRACTION</title><author>Vargas-Villarreal, Javier ; Mata-Cárdenas, Benito D ; González-Salazar, Francisco ; Lozano-Garza, Héctor G ; Cortes-Gutierrez, Elva I ; Palacios-Corona, Rebeca ; Martínez-Rodríguez, Herminia G ; Ramírez-Bon, Enrique ; Said-Fernández, Salvador</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b320t-dbf91c180a476d39ef60a671d2250cabf5fcd5e4b335744c24e474e72699b4143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Calcium - metabolism</topic><topic>Dose-Response Relationship, Drug</topic><topic>Enzymes</topic><topic>Epithelial cells</topic><topic>Erythrocytes</topic><topic>Erythrocytes - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemolysin proteins</topic><topic>Hemolysis</topic><topic>Hemolysis - physiology</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Invertebrates</topic><topic>Nemathelminthia. Plathelmintha</topic><topic>Parasitism</topic><topic>Parasitology</topic><topic>PATHOLOGY</topic><topic>Phospholipases A - antagonists & inhibitors</topic><topic>Phospholipases A - metabolism</topic><topic>Physiology. Development</topic><topic>Rats</topic><topic>Stearates - pharmacology</topic><topic>Subcellular fractions</topic><topic>Trichomonas vaginalis - enzymology</topic><topic>Trichomonas vaginalis - metabolism</topic><topic>Trichomonas vaginalis - pathogenicity</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vargas-Villarreal, Javier</creatorcontrib><creatorcontrib>Mata-Cárdenas, Benito D</creatorcontrib><creatorcontrib>González-Salazar, Francisco</creatorcontrib><creatorcontrib>Lozano-Garza, Héctor G</creatorcontrib><creatorcontrib>Cortes-Gutierrez, Elva I</creatorcontrib><creatorcontrib>Palacios-Corona, Rebeca</creatorcontrib><creatorcontrib>Martínez-Rodríguez, Herminia G</creatorcontrib><creatorcontrib>Ramírez-Bon, Enrique</creatorcontrib><creatorcontrib>Said-Fernández, Salvador</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of parasitology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vargas-Villarreal, Javier</au><au>Mata-Cárdenas, Benito D</au><au>González-Salazar, Francisco</au><au>Lozano-Garza, Héctor G</au><au>Cortes-Gutierrez, Elva I</au><au>Palacios-Corona, Rebeca</au><au>Martínez-Rodríguez, Herminia G</au><au>Ramírez-Bon, Enrique</au><au>Said-Fernández, Salvador</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>TRICHOMONAS VAGINALIS: IDENTIFICATION OF A PHOSPHOLIPASE A–DEPENDENT HEMOLYTIC ACTIVITY IN A VESICULAR SUBCELLULAR FRACTION</atitle><jtitle>The Journal of parasitology</jtitle><addtitle>J Parasitol</addtitle><date>2003-02-01</date><risdate>2003</risdate><volume>89</volume><issue>1</issue><spage>105</spage><epage>112</epage><pages>105-112</pages><issn>0022-3395</issn><eissn>1937-2345</eissn><coden>JOPAA2</coden><abstract>Trichomonad total extracts (TTE), or vesicular (P30) and soluble (S30) subcellular fractions from 3 pathogenic Trichomonas vaginalis strains (GT-3, GT-13, and GT-15), lysed both human and Sprague–Dawley rat erythrocytes in a time- and dose-dependent manner. The entire hemolytic activity of TTE was located in P30, showing 2 peaks of maximum activity, one at pH 6.0 and another at pH 8.0, in the presence of 1 mM Ca2+. Hemolytic activity on rat erythrocytes was greater at pH 6.0 (6.71 ± 0.33 hemolytic units [HU]/mg/hr to 11.60 ± 0.24 HU/mg/hr) than at pH 8.0 (3.81 ± 0.30 HU/mg/hr to 5.75 ± 0.65 HU/mg/hr), and it was greater than that on human red blood cells at pH 6.0 (2.67 ± 0.19 HU/mg/hr to 4.08 ± 0.15 HU/mg/hr) or pH 8.0 (2.24 ± 0.09 HU/mg/hr to 2.81 ± 0.06 HU/mg/hr). The alkaline and acidic hemolytic activity diminished (60–93% at pH 6.0 and 78–93% at pH 8.0) by the effect of 80 μM Rosenthal's inhibitor, which also inhibited 27–45% and 29–54% trichomonad alkaline and acidic phospholipase A activities, respectively. Vesicles, vacuoles, and hydrogenosomes were rich in P30. Trichomonas vaginalis has a hemolytic PLA, which could be involved in its cytopathogenic mechanism.</abstract><cop>Lawrence, KS</cop><pub>American Society of Parasitologists</pub><pmid>12659311</pmid><doi>10.1645/0022-3395(2003)089[0105:TVIOAP]2.0.CO;2</doi><tpages>8</tpages></addata></record> |
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| subjects | Animals Biochemistry Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Calcium - metabolism Dose-Response Relationship, Drug Enzymes Epithelial cells Erythrocytes Erythrocytes - metabolism Fundamental and applied biological sciences. Psychology Hemolysin proteins Hemolysis Hemolysis - physiology Humans Hydrogen-Ion Concentration Invertebrates Nemathelminthia. Plathelmintha Parasitism Parasitology PATHOLOGY Phospholipases A - antagonists & inhibitors Phospholipases A - metabolism Physiology. Development Rats Stearates - pharmacology Subcellular fractions Trichomonas vaginalis - enzymology Trichomonas vaginalis - metabolism Trichomonas vaginalis - pathogenicity Virulence |
| title | TRICHOMONAS VAGINALIS: IDENTIFICATION OF A PHOSPHOLIPASE A–DEPENDENT HEMOLYTIC ACTIVITY IN A VESICULAR SUBCELLULAR FRACTION |
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