Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts

There is evidence involving protein kinase C (PKC) in the signal transduction pathways that regulate the differentiation of myoblasts into mature multinucleated muscle cells (myotubes). In order to obtain information on the possible role of individual PKC isozymes in myogenesis, in the present work...

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Autores principales:	Capiati, D.A., Limbozzi, F., Téllez-Iñón, M.T., Boland, R.L.
Formato:	JOUR
Materias:	DNA synthesis Myoblasts Myogenesis PKC isozymes Protein kinase C creatine kinase DNA isoenzyme myosin protein kinase c animal cell article cell culture cell differentiation cell proliferation chick embryo controlled study embryo enzyme activity muscle development myoblast nonhuman priority journal protein expression Animals Cell Differentiation Cell Division Chick Embryo DNA Replication Indoles Isoenzymes Maleimides Muscle, Skeletal Naphthalenes Protein Kinase C Protein Kinase C-alpha Tetradecanoylphorbol Acetate Animalia
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_07302312_v74_n2_p292_Capiati
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_07302312_v74_n2_p292_Capiati
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spelling	todo:paper_07302312_v74_n2_p292_Capiati2023-10-03T15:37:17Z Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts Capiati, D.A. Limbozzi, F. Téllez-Iñón, M.T. Boland, R.L. DNA synthesis Myoblasts Myogenesis PKC isozymes Protein kinase C creatine kinase DNA isoenzyme myosin protein kinase c animal cell article cell culture cell differentiation cell proliferation chick embryo controlled study DNA synthesis embryo enzyme activity muscle development myoblast nonhuman priority journal protein expression Animals Cell Differentiation Cell Division Chick Embryo DNA Replication Indoles Isoenzymes Maleimides Muscle, Skeletal Naphthalenes Protein Kinase C Protein Kinase C-alpha Tetradecanoylphorbol Acetate Animalia There is evidence involving protein kinase C (PKC) in the signal transduction pathways that regulate the differentiation of myoblasts into mature multinucleated muscle cells (myotubes). In order to obtain information on the possible role of individual PKC isozymes in myogenesis, in the present work we investigated the differential expression of PKC isoforms α, β, δ, ε, and ζ during muscle cell development in vitro. Chick embryo myoblasts cultured from 1 to 6 days were used as experimental model. Morphological characterization and measurement of specific biochemical parameters in cultures, e.g., DNA synthesis, creatine kinase activity, and myosin levels, revealed a typical muscle cell developmental pattern consisting of an initial proliferation of myoblasts followed by their differentiation into myotubes. PKC activity was high at the proliferative stage, decreased as myoblasts elongated and fused, and increased again in differentiated myotubes. In proliferating myoblasts, the PKC inhibitors calphostin C and bisindolylmaleimide I decreased DNA synthesis whereas in myoblasts undergoing differentiation they exerted the opposite effect, suggesting that PKC plays a role at both stages of myogenesis. Western blot analysis of changes in the expression of PKC isoforms during muscle cell development showed high levels of PKC α in the proliferating phase which markedly decreased as myoblasts differentiated. Treatment with TPA of proliferative myoblasts inhibited DNA synthesis and selectively down-regulated PKC α, suggesting that this isozyme may have an important role in maintaining myoblast proliferation. On the other hand, an increase in the expression of PKC β, δ, and ε was detected during myogenesis, suggesting that one or more of these isoforms may participate in the differentiation process of myoblasts. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_07302312_v74_n2_p292_Capiati
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	DNA synthesis Myoblasts Myogenesis PKC isozymes Protein kinase C creatine kinase DNA isoenzyme myosin protein kinase c animal cell article cell culture cell differentiation cell proliferation chick embryo controlled study DNA synthesis embryo enzyme activity muscle development myoblast nonhuman priority journal protein expression Animals Cell Differentiation Cell Division Chick Embryo DNA Replication Indoles Isoenzymes Maleimides Muscle, Skeletal Naphthalenes Protein Kinase C Protein Kinase C-alpha Tetradecanoylphorbol Acetate Animalia
spellingShingle	DNA synthesis Myoblasts Myogenesis PKC isozymes Protein kinase C creatine kinase DNA isoenzyme myosin protein kinase c animal cell article cell culture cell differentiation cell proliferation chick embryo controlled study DNA synthesis embryo enzyme activity muscle development myoblast nonhuman priority journal protein expression Animals Cell Differentiation Cell Division Chick Embryo DNA Replication Indoles Isoenzymes Maleimides Muscle, Skeletal Naphthalenes Protein Kinase C Protein Kinase C-alpha Tetradecanoylphorbol Acetate Animalia Capiati, D.A. Limbozzi, F. Téllez-Iñón, M.T. Boland, R.L. Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts
topic_facet	DNA synthesis Myoblasts Myogenesis PKC isozymes Protein kinase C creatine kinase DNA isoenzyme myosin protein kinase c animal cell article cell culture cell differentiation cell proliferation chick embryo controlled study DNA synthesis embryo enzyme activity muscle development myoblast nonhuman priority journal protein expression Animals Cell Differentiation Cell Division Chick Embryo DNA Replication Indoles Isoenzymes Maleimides Muscle, Skeletal Naphthalenes Protein Kinase C Protein Kinase C-alpha Tetradecanoylphorbol Acetate Animalia
description	There is evidence involving protein kinase C (PKC) in the signal transduction pathways that regulate the differentiation of myoblasts into mature multinucleated muscle cells (myotubes). In order to obtain information on the possible role of individual PKC isozymes in myogenesis, in the present work we investigated the differential expression of PKC isoforms α, β, δ, ε, and ζ during muscle cell development in vitro. Chick embryo myoblasts cultured from 1 to 6 days were used as experimental model. Morphological characterization and measurement of specific biochemical parameters in cultures, e.g., DNA synthesis, creatine kinase activity, and myosin levels, revealed a typical muscle cell developmental pattern consisting of an initial proliferation of myoblasts followed by their differentiation into myotubes. PKC activity was high at the proliferative stage, decreased as myoblasts elongated and fused, and increased again in differentiated myotubes. In proliferating myoblasts, the PKC inhibitors calphostin C and bisindolylmaleimide I decreased DNA synthesis whereas in myoblasts undergoing differentiation they exerted the opposite effect, suggesting that PKC plays a role at both stages of myogenesis. Western blot analysis of changes in the expression of PKC isoforms during muscle cell development showed high levels of PKC α in the proliferating phase which markedly decreased as myoblasts differentiated. Treatment with TPA of proliferative myoblasts inhibited DNA synthesis and selectively down-regulated PKC α, suggesting that this isozyme may have an important role in maintaining myoblast proliferation. On the other hand, an increase in the expression of PKC β, δ, and ε was detected during myogenesis, suggesting that one or more of these isoforms may participate in the differentiation process of myoblasts.
format	JOUR
author	Capiati, D.A. Limbozzi, F. Téllez-Iñón, M.T. Boland, R.L.
author_facet	Capiati, D.A. Limbozzi, F. Téllez-Iñón, M.T. Boland, R.L.
author_sort	Capiati, D.A.
title	Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts
title_short	Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts
title_full	Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts
title_fullStr	Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts
title_full_unstemmed	Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts
title_sort	evidence on the participation of protein kinase c α in the proliferation of cultured myoblasts
url	http://hdl.handle.net/20.500.12110/paper_07302312_v74_n2_p292_Capiati
work_keys_str_mv	AT capiatida evidenceontheparticipationofproteinkinasecaintheproliferationofculturedmyoblasts AT limbozzif evidenceontheparticipationofproteinkinasecaintheproliferationofculturedmyoblasts AT tellezinonmt evidenceontheparticipationofproteinkinasecaintheproliferationofculturedmyoblasts AT bolandrl evidenceontheparticipationofproteinkinasecaintheproliferationofculturedmyoblasts
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Evidence on the participation of protein kinase C α in the proliferation of cultured myoblasts

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