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Protein kinase A activity is associated with metacyclogenesis in Leishmania amazonensis
Author(s) -
Genestra Marcelo,
CysneFinkelstein Léa,
Leon Leonor
Publication year - 2004
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1107
Subject(s) - adenylate kinase , protein kinase a , amastigote , cyclase , axenic , biochemistry , biology , cyclic adenosine monophosphate , intracellular , adenosine , enzyme , leishmania , chemistry , parasite hosting , bacteria , genetics , receptor , world wide web , computer science
Because of the importance of cell signalling processes in proliferation and differentiation, the adenylate cyclase pathway was studied, specifically the protein kinase A (PKA) in Leishmania amazonensis. The PKAs of soluble (SF) and enriched membrane fractions (MF) from infective/non‐infective promastigotes and axenic amastigotes were assayed. In order to purify the PKA molecule, fractions were chromatographed on DEAE‐cellulose columns and the phosphorylative activity was evaluated using [γ 32 P]‐ATP as the phosphate source. These experiments were performed in the presence of cyclic adenosine monophosphate (cAMP) and an inhibitor of PKA. Our data demonstrated that the PKA activity was significantly higher (about two times) in SF from promastigotes with a high concentration of metacyclic forms, when compared with the non‐infective promastigotes, suggesting an association of this activity and the metacyclogenesis process. A discrete phosphorylative activity in axenic amastigotes was observed. As the adenylate cyclase/cAMP pathway would be involved in the parasite–host interiorization, the PKA activity may constitute a good intracellular target for studies of leishmanicidal drugs. Copyright © 2004 John Wiley & Sons, Ltd.