Identification ofEntamoeba histolytica intracellular phospholipase A and lysophospholipase L1 activities

Vargas‐Villarreal, Javier; Martı́nez-Rodrı́guez, Herminia Guadalupe; Castro-Garza, Jorge; Mata-Cárdenas, Benito David; González‐Garza, María Teresa; Said‐Fernández, Salvador

doi:10.1007/bf00931538

Cited by 27 publications

(21 citation statements)

References 10 publications

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“…We have demonstrated the presence of phospholipases in Trichomonas [21], amoeba [46], and giardia [47]. But the presence of sphingomyelinases has not been described in T. vaginalis.…”

Section: Discussionmentioning

confidence: 99%

Sphingomyelinase Activity ofTrichomonas vaginalisExtract and Subfractions

González-Salazar

Garza-González

Hernández-Luna

et al. 2013

BioMed Research International

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Trichomoniasis is one of the most common acute sexually transmitted curable diseases, and it is disseminated worldwide generating more than 170 million cases annually. Trichomonas vaginalis is the parasite that causes trichomoniasis and has the ability to destroy cell monolayers of the vaginal mucosa in vitro. Sphingomyelinases (SMase) are enzymes that catalyze the hydrolysis of sphingomyelin into ceramide and phosphorylcholine. Ceramide appears to be a second messenger lipid in programmed apoptosis, cell differentiation, and cell proliferation. Sphingomyelinase is probably a major source of ceramide in cells. Signal transduction mediated by ceramide leads cells to produce cytokine induced apoptosis during several inflammatory responses. SMase are also relevant toxins in several microorganisms. The main objective of this research is to identify SMase activity of T. vaginalis in the total extract (TE), P30, and S30 subfractions from brooked trophozoites. It was found that these fractions of T. vaginalis have SMase activity, which comes principally from P30 subfraction and was mainly type C. Enzymatic activity of SMase increased linearly with time and is pH dependent with two peaks by pH 5.5 and pH 7.5. The addition of manganese to the reaction mixture increased the SMase activity by 1.97.

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“…We have demonstrated the presence of phospholipases in Trichomonas [21], amoeba [46], and giardia [47]. But the presence of sphingomyelinases has not been described in T. vaginalis.…”

Section: Discussionmentioning

confidence: 99%

Sphingomyelinase Activity ofTrichomonas vaginalisExtract and Subfractions

González-Salazar

Garza-González

Hernández-Luna

et al. 2013

BioMed Research International

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“…The synthesis of PGs is not yet well understood. The cycle of transformation begins with phospholipase A 2 , the enzyme whose presence in the lysosomes of protozoa has been established (Visvevara and Balamuth 1975; Misra et al 1983;Vargas-Villarreal et al 1995). The synthesis of PGs begins with the enzyme known as the synthase of endoperoxides of PGs (E.C.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis of prostaglandins in pathogenic and nonpathogenic strains of Acanthamoeba spp.

Hadas¹,

Mazur²

1997

Parasitology Research

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The aim of the present study was to examine the biosynthesis of prostaglandins and to investigate factors conditioning their biosynthesis in pathogenic and nonpathogenic strains of Acanthamoeba spp. We established that the activity of the synthase of prostaglandins was almost identical in pathogenic and non-pathogenic strains and that the synthesis of endoperoxide prostaglandins was similar to that of other organisms up to the point at which prostaglandin H2 was produced. The course of biosynthesis in vitro can be activated by various compounds such as glutathione, albumin, and p-chloromercuribenzoic acid (p-CMB), which are either activators or inhibitors of the enzymes. We suggest that the course of biosynthesis of prostaglandins in vivo is most probably activated by tissues or constitutional liquids surrounding the parasites.

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“…The spots belonging to PC, LPC and FFA were identified. These lipids were recovered by scalpel scraped of each sample from the plates, and their radioactivity determined (expressed as disintegrations per min, DPM) as described elsewhere (Vargas-Villarreal et al 1995). All determinations were performed in triplicate and presented as mean ± SE.…”

Section: Sequence Of T Vaginalis Phospholipase 521mentioning

confidence: 99%

“…These enzymes are important in the pathogenic mechanisms of the protozoa such as T. vaginalis , 2005, Lubick and Burgess 2004, Entamoeba histolytica (Long-Krug et al 1985;Vargas-Villarreal et al 1995González-Garza et al 2000), Trypanosoma cruzi (Wainszelbaum et al 2001), and Naegleria fowleri (Barbour and Marciano-Cabral 2001). We have previously shown that the P30 and S30 subcellular fractions of T. vaginalis incubated in presence of human or rat erythrocytes.…”

Section: Introductionmentioning

confidence: 99%

Trichomonas vaginalis acidic phospholipase A2: isolation and partial amino acid sequence

Escobedo-Guajardo

González-Salazar

Palacios-Corona

et al. 2013

Acta Parasitologica

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Sexually transmitted diseases are a major cause of acute disease worldwide, and trichomoniasis is the most common and curable disease, generating more than 170 million cases annually worldwide. Trichomonas vaginalis is the causal agent of trichomoniasis and has the ability to destroy in vitro cell monolayers of the vaginal mucosa, where the phospholipases A 2 (PLA 2 ) have been reported as potential virulence factors. These enzymes have been partially characterized from the subcellular fraction S30 of pathogenic T. vaginalis strains. The main objective of this study was to purify a phospholipase A 2 from T. vaginalis, make a partial characterization, obtain a partial amino acid sequence, and determine its enzymatic participation as hemolytic factor causing lysis of erythrocytes. Trichomonas S30, RF30 and UFF30 sub-fractions from GT-15 strain have the capacity to hydrolyze [2-14 C-PA]-PC at pH 6.0. Proteins from the UFF30 sub-fraction were separated by affinity chromatography into two eluted fractions with detectable PLA A 2 activity. The EDTA-eluted fraction was analyzed by HPLC using on-line HPLC-tandem mass spectrometry and two protein peaks were observed at 8.2 and 13 kDa. Peptide sequences were identified from the proteins present in the eluted EDTA UFF30 fraction; bioinformatic analysis using Protein Link Global Server charged with T. vaginalis protein database suggests that eluted peptides correspond a putative ubiquitin protein in the 8.2 kDa fraction and a phospholipase preserved in the 13 kDa fraction. The EDTA-eluted fraction hydrolyzed [2-14 C-PA]-PC lyses erythrocytes from Sprague-Dawley in a time and dose-dependent manner. The acidic hemolytic activity decreased by 84% with the addition of 100 µM of Rosenthal's inhibitor.

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Identification ofEntamoeba histolytica intracellular phospholipase A and lysophospholipase L1 activities

Cited by 27 publications

References 10 publications

Sphingomyelinase Activity ofTrichomonas vaginalisExtract and Subfractions

Sphingomyelinase Activity ofTrichomonas vaginalisExtract and Subfractions

Biosynthesis of prostaglandins in pathogenic and nonpathogenic strains of Acanthamoeba spp.

Trichomonas vaginalis acidic phospholipase A2: isolation and partial amino acid sequence

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