Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi

The presence of Ca2+/calmodulin (Ca2+/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...

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Autor principal: Ogueta, S.B
Otros Autores: Macintosh, G.C, Téllez-Iñon, M.T
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: Blackwell Publishing Inc. 1998
Acceso en línea:Registro en Scopus
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024 7 |2 scopus  |a 2-s2.0-0032127976 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
030 |a JEMIE 
100 1 |a Ogueta, S.B. 
245 1 0 |a Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi 
260 |b Blackwell Publishing Inc.  |c 1998 
270 1 0 |m Ogueta, S.B.; Jules Stein Eye Institute, University of California, Los Angeles, CA 90095, United States; email: ogueta@jsei.ucla.edu 
506 |2 openaire  |e Política editorial 
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504 |a Orr, G.A., Tanowitz, H.B., Wittner, M., Trypanosoma cruzi: Stage expression of calmodulin-binding proteins (1992) Exp. Parasitol., 74, pp. 127-133 
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504 |a Tokumitsu, H., Chijiwa, T., Hagiwara, M., Mizutani, A., Teresawa, M., Hidaka, H., KN-62, 1-[N,O-Bis(5-isoquinolinesulfonyl)-N-methyl-L -tyrosyl]-4-phenylpiperazine, a specific inhibitor of Ca2+/calmodulin-dependent protein kinase II (1990) J. Biol. Chem., 265, pp. 4315-4320 
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520 3 |a The presence of Ca2+/calmodulin (Ca2+/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.  |l eng 
593 |a Inst. Invest. Ing. Genet. Biol. M., Fac. de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina 
593 |a Jules Stein Eye Institute, University of California, Los Angeles, CA 90095, United States 
593 |a Michigan State University, Department of Energy, Michigan State University, East Lansing, MI 48824, United States 
690 1 0 |a AMASTIGOTES 
690 1 0 |a DIFFERENTIATION 
690 1 0 |a EPIMASTIGOTES 
690 1 0 |a TRYPANOSOMATIDS 
690 1 0 |a TRYPOMASTIGOTES 
690 1 0 |a CALCIUM 
690 1 0 |a CALMODULIN 
690 1 0 |a DEVELOPMENTAL CYCLE 
690 1 0 |a ENZYME ACTIVATION 
690 1 0 |a IDENTIFICATION 
690 1 0 |a MORPHOGENESIS 
690 1 0 |a PHOSPHORYLATION 
690 1 0 |a POLYCLONAL ANTIBODY 
690 1 0 |a PROTEIN KINASE 
690 1 0 |a WESTERN BLOTTING 
690 1 0 |a TRYPANOSOMA CRUZI 
700 1 |a Macintosh, G.C. 
700 1 |a Téllez-Iñon, M.T. 
773 0 |d Blackwell Publishing Inc., 1998  |g v. 45  |h pp. 392-396  |k n. 4  |p J. Eukaryotic Microbiol.  |x 10665234  |t Journal of Eukaryotic Microbiology 
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