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Stage‐Specific Substrate Phosphorylation by a Ca2+/Calmodulin‐Dependent Protein Kinase in Trypanosoma cruzi
Author(s) -
Ogueta Sandra B.,
Macintosh Gustavo C.,
TéllezNo̊n Maria T.
Publication year - 1998
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1998.tb05089.x
Subject(s) - biology , trypanosoma cruzi , polyclonal antibodies , immunoprecipitation , phosphorylation , western blot , protein kinase a , protein subunit , kinase , biochemistry , microbiology and biotechnology , enzyme , antibody , parasite hosting , immunology , world wide web , computer science , gene
The presence of (Ca 2 /calmodulin (Ca 2 /CaM)‐dependent protein kinase (TcCaM K) and some stage‐specific substrates that appeared during morphogenesis of the parasite Trypanosoma cruzi were identified. Western blot analysis using a polyclonal antibody against rat brain CaM K type II recognized the same subunit composition (52, 59/62 kDa) observed for the mammalian enzyme, as well as the previously characterized TcCaM K found in epimastigote forms. Differential protein phosphorylation profiles were observed after enzyme activation in the stages of T. cruzi. Co‐immunoprecipitation of stage‐specific substrates with the TcCaM K suggested that the enzyme might be involved in the phosphorylation of a different set of proteins through the life cycle. Three phosphoproteins, pp105 and pp87 from epimastigotes and pp23 from trypomastigotes were identified as potential substrates for TcCaM K. The characterization of these endogenous stage markers might be a useful tool to understand the developmental cycles of these pathogenic protozoa.