Leishmania amazonensis: Biological and biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities.

dc.creatorPinheiro, Carla Monica
dc.creatorDuarte, Erica dos Santos Martins
dc.creatorFerraro, Rodrigo Barbosa
dc.creatorSouza, André Luíz Fonseca de
dc.creatorGomes, Marta T
dc.creatorLopes, Angela H.C.S
dc.creatorSantos, Marcos André Vannier dos
dc.creatorSantos, André L.S
dc.creatorFernandes, José Roberto Meyer
dc.date2015-09-29T16:08:29Z
dc.date2015-09-29T16:08:29Z
dc.date2006
dc.date.accessioned2023-09-26T22:30:41Z
dc.date.available2023-09-26T22:30:41Z
dc.identifierPINHEIRO, C. M. et al. Leishmania amazonensis: Biological and biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities. Experimental Parasitology, v. 114, n. 1, p. 16-25, 2006.
dc.identifier0014-4894
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/11842
dc.identifier10.1016/j.exppara.2006.02.007
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8880162
dc.descriptionThe presence of Leishmania amazonensis ecto-nucleoside triphosphate triphosphohydrolase activities was demonstrated using antibodies against different NTPDase members by Western blotting, flow cytometry, and immunoelectron microscopy analysis. Living promastigote cells sequentially hydrolyzed the ATP molecule generating ADP, AMP, and adenosine, indicating that this surface enzyme may play a role in the salvage of purines from the extracellular medium. The L. amazonensis ecto-NTPDase activities were insensitive to Triton X-100, but they were enhanced by divalent cations, such as Mg(2+). In addition, the ecto-NTPDase activities decreased with time for 96 h when promastigotes were grown in vitro. On the other hand, these activities increased considerably when measured in living amastigote forms. Furthermore, the treatment with adenosine, a mediator of several relevant biological phenomena, induced a decrease in the reactivity with anti-CD39 antibody, raised against mammalian E-NTPDase, probably because of down regulation in the L. amazonensis ecto-NTPDase expression. Also, adenosine and anti-NTPDase antibodies induced a significant diminishing in the interaction between promastigotes of L. amazonensis and mouse peritoneal macrophages.
dc.formatapplication/pdf
dc.languageeng
dc.publisherElsevier
dc.rightsopen access
dc.subjectLeishmania amazonensis
dc.subjectEcto-ATPase
dc.subjectAdenosine
dc.subjectE-NTPDase
dc.subjectAdenosina Trifosfatases/metabolismo
dc.subjectLeishmania mexicana/enzimologia
dc.subjectDifosfato de Adenosina/metabolismo
dc.subjectMonofosfato de Adenosina/metabolismo
dc.subjectTrifosfato de Adenosina/metabolismo
dc.subjectAnimais
dc.subjectAntígenos CD/metabolismo
dc.subjectApirase/metabolismo
dc.subjectWestern Blotting
dc.subjectFeminino
dc.subjectCitometria de Fluxo
dc.subjectHumanos
dc.subjectLeishmaniose Cutânea/parasitologia
dc.subjectMacrófagos Peritoneais/parasitologia
dc.subjectCamundongos
dc.subjectMicroscopia Imunoeletrônica
dc.subjectPirofosfatases/metabolismo
dc.titleLeishmania amazonensis: Biological and biochemical characterization of ecto-nucleoside triphosphate diphosphohydrolase activities.
dc.typeArticle


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