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Ceramide synthase 2 knockdown suppresses trophozoite growth, migration, in vitro encystment and excystment of Entamoeba invadens.
Jáuregui-Wade, José Manuel; Cerbón-Solórzano, Jorge; Ávila-García, Ricardo; Ayala-Sumuano, Jorge Tonatiuh; Valdés, Jesús.
Afiliação
  • Jáuregui-Wade JM; Department of Biochemistry, CINVESTAV-IPN, P.O. Box 14-740, 07360, Ciudad de México, Mexico.
  • Cerbón-Solórzano J; Department of Biochemistry, CINVESTAV-IPN, P.O. Box 14-740, 07360, Ciudad de México, Mexico.
  • Ávila-García R; Department of Biochemistry, CINVESTAV-IPN, P.O. Box 14-740, 07360, Ciudad de México, Mexico.
  • Ayala-Sumuano JT; Idix S.A. de C.V, Querétaro, Mexico.
  • Valdés J; Department of Biochemistry, CINVESTAV-IPN, P.O. Box 14-740, 07360, Ciudad de México, Mexico. Electronic address: jvaldes@cinvestav.mx.
Biochem Biophys Res Commun ; 524(1): 135-141, 2020 03 26.
Article em En | MEDLINE | ID: mdl-31980165
Entamoeba invadens is the protozoan which causes multiple damages in reptiles and is considered a prototype for the study of the Entamoeba encystment/excystment in vitro. Here we report that EinCerS2 knockdown promoted decrease in sphingomyelin (SM) subspecies with long-chain fatty acids (24:0) down to 50% but increase sphingolipids with short-chain fatty acids (16:0) up to three times in both trophozoites and cysts of E. invadens. EinCerS2 silencing also resulted in decreased trophozoites' movement, proliferation, cysts formation, and trophozoites hatched after excystment. By immunofluorescence assays, a polyclonal antibody against EinCerS2 detected the enzyme in the cytoplasm of E. invadens trophozoites, colocalizing with Endoplasmic Reticulum-resident cognate EiSERCA. Interestingly, EinCerS2 was redistributed close to the plasma membrane during encystation, suggesting that the generation of diacylglycerol (DAG) via synthesis of sphingolipids and the activation protein kinase C might participate in the encystment process of E. invadens.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Movimento Celular / Entamoeba / Trofozoítos / Técnicas de Silenciamento de Genes Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2020 Tipo de documento: Article País de afiliação: México País de publicação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Movimento Celular / Entamoeba / Trofozoítos / Técnicas de Silenciamento de Genes Idioma: En Revista: Biochem Biophys Res Commun Ano de publicação: 2020 Tipo de documento: Article País de afiliação: México País de publicação: Estados Unidos