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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Publicado:	1998
Materias:	Amastigotes Differentiation Epimastigotes Trypanosomatids Trypomastigotes calcium calmodulin developmental cycle enzyme activation identification morphogenesis phosphorylation polyclonal antibody protein kinase Western blotting Trypanosoma cruzi
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v45_n4_p392_Ogueta http://hdl.handle.net/20.500.12110/paper_10665234_v45_n4_p392_Ogueta
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_10665234_v45_n4_p392_Ogueta
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spelling	paper:paper_10665234_v45_n4_p392_Ogueta2023-06-08T16:04:17Z Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi Amastigotes Differentiation Epimastigotes Trypanosomatids Trypomastigotes calcium calmodulin developmental cycle enzyme activation identification morphogenesis phosphorylation polyclonal antibody protein kinase Western blotting 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 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. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v45_n4_p392_Ogueta http://hdl.handle.net/20.500.12110/paper_10665234_v45_n4_p392_Ogueta
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Amastigotes Differentiation Epimastigotes Trypanosomatids Trypomastigotes calcium calmodulin developmental cycle enzyme activation identification morphogenesis phosphorylation polyclonal antibody protein kinase Western blotting Trypanosoma cruzi
spellingShingle	Amastigotes Differentiation Epimastigotes Trypanosomatids Trypomastigotes calcium calmodulin developmental cycle enzyme activation identification morphogenesis phosphorylation polyclonal antibody protein kinase Western blotting Trypanosoma cruzi Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi
topic_facet	Amastigotes Differentiation Epimastigotes Trypanosomatids Trypomastigotes calcium calmodulin developmental cycle enzyme activation identification morphogenesis phosphorylation polyclonal antibody protein kinase Western blotting Trypanosoma cruzi
description	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.
title	Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi
title_short	Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi
title_full	Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi
title_fullStr	Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi
title_full_unstemmed	Stage-specific substrate phosphorylation by a Ca2+/calmodulin-dependent protein kinase in Trypanosoma cruzi
title_sort	stage-specific substrate phosphorylation by a ca2+/calmodulin-dependent protein kinase in trypanosoma cruzi
publishDate	1998
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10665234_v45_n4_p392_Ogueta http://hdl.handle.net/20.500.12110/paper_10665234_v45_n4_p392_Ogueta
_version_	1768545474480963584

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

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