Sphingomyelinase activity of trichomonas vaginalis extract and subfractions

Francisco González-Salazar, Jesús N. Garza-González, Carlos E. Hernandez-Luna, Benito David Mata-Cárdenas, Pilar Carranza-Rosales, Jorge Enrique Castro-Garza, Magda Elizabeth Hernández-García, Javier Vargas-Villarreal

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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. © 2013 Francisco González-Salazar et al.
Original languageEnglish
JournalBioMed Research International
DOIs
Publication statusPublished - 23 Sep 2013
Externally publishedYes

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Sphingomyelin Phosphodiesterase
Trichomonas vaginalis
Ceramides
Apoptosis
Trophozoites
Signal transduction
Phosphorylcholine
Sphingomyelins
Cell proliferation
Second Messenger Systems
Manganese
Sexually Transmitted Diseases
Microorganisms
Cell Differentiation
Hydrolysis
Monolayers
Signal Transduction
Mucous Membrane
Parasites
Cell Proliferation

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Cite this

González-Salazar, F., Garza-González, J. N., Hernandez-Luna, C. E., Mata-Cárdenas, B. D., Carranza-Rosales, P., Castro-Garza, J. E., ... Vargas-Villarreal, J. (2013). Sphingomyelinase activity of trichomonas vaginalis extract and subfractions. BioMed Research International. https://doi.org/10.1155/2013/679365
González-Salazar, Francisco ; Garza-González, Jesús N. ; Hernandez-Luna, Carlos E. ; Mata-Cárdenas, Benito David ; Carranza-Rosales, Pilar ; Castro-Garza, Jorge Enrique ; Hernández-García, Magda Elizabeth ; Vargas-Villarreal, Javier. / Sphingomyelinase activity of trichomonas vaginalis extract and subfractions. In: BioMed Research International. 2013.
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abstract = "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. {\circledC} 2013 Francisco Gonz{\'a}lez-Salazar et al.",
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González-Salazar, F, Garza-González, JN, Hernandez-Luna, CE, Mata-Cárdenas, BD, Carranza-Rosales, P, Castro-Garza, JE, Hernández-García, ME & Vargas-Villarreal, J 2013, 'Sphingomyelinase activity of trichomonas vaginalis extract and subfractions', BioMed Research International. https://doi.org/10.1155/2013/679365

Sphingomyelinase activity of trichomonas vaginalis extract and subfractions. / González-Salazar, Francisco; Garza-González, Jesús N.; Hernandez-Luna, Carlos E.; Mata-Cárdenas, Benito David; Carranza-Rosales, Pilar; Castro-Garza, Jorge Enrique; Hernández-García, Magda Elizabeth; Vargas-Villarreal, Javier.

In: BioMed Research International, 23.09.2013.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Sphingomyelinase activity of trichomonas vaginalis extract and subfractions

AU - González-Salazar, Francisco

AU - Garza-González, Jesús N.

AU - Hernandez-Luna, Carlos E.

AU - Mata-Cárdenas, Benito David

AU - Carranza-Rosales, Pilar

AU - Castro-Garza, Jorge Enrique

AU - Hernández-García, Magda Elizabeth

AU - Vargas-Villarreal, Javier

PY - 2013/9/23

Y1 - 2013/9/23

N2 - 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. © 2013 Francisco González-Salazar et al.

AB - 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. © 2013 Francisco González-Salazar et al.

U2 - 10.1155/2013/679365

DO - 10.1155/2013/679365

M3 - Article

JO - BioMed Research International

JF - BioMed Research International

SN - 2314-6133

ER -

González-Salazar F, Garza-González JN, Hernandez-Luna CE, Mata-Cárdenas BD, Carranza-Rosales P, Castro-Garza JE et al. Sphingomyelinase activity of trichomonas vaginalis extract and subfractions. BioMed Research International. 2013 Sep 23. https://doi.org/10.1155/2013/679365