The Inhibition of Differentiation Caused by TGFβ in Fetal Myoblasts Is Dependent upon Selective Expression of PKCθ: A Possible Molecular Basis for Myoblast Diversification during Limb Histogenesis
Identifieur interne : 000200 ( Istex/Curation ); précédent : 000199; suivant : 000201The Inhibition of Differentiation Caused by TGFβ in Fetal Myoblasts Is Dependent upon Selective Expression of PKCθ: A Possible Molecular Basis for Myoblast Diversification during Limb Histogenesis
Auteurs : Fabrizio Zappelli [Italie] ; Daniela Willems [Italie] ; Shin-Ichi Osada [Japon] ; Shigeo Ohno [Japon] ; William C. Wetsel [États-Unis] ; Mario Molinaro [Italie] ; Giulio Cossu [Italie] ; Marina Bouché [Italie]Source :
- Developmental Biology [ 0012-1606 ] ; 1996.
English descriptors
- Teeft :
- Academic press, Angelis, Bers, Biol, Bouche, Cdna, Cell biol, Cell proliferation, Copyright, Cos1 cells, Cossu, Different isoforms, Differential expression, Differential response, Differential sensitivity, Differentiation, Embryo, Embryo limbs, Embryonic, Embryonic myoblasts, Expression vectors, Fetal, Fetal muscle, Fetal myoblasts, Growth factor, Growth factors, High levels, Histogenesis, Isoform, Isoforms, Kinase, Limb, Molinaro, Mouse embryos, Muscle histogenesis, Myoblast, Myoblasts, Myogenic, Myogenic cells, Myogenic differentiation, Myosin, Myotubes, Osada, Overexpression, Pkcu, Pkcu expression, Positive control, Possible role, Protein kinase, Satellite cells, Signal transduction, Skeletal muscle, Tgfb, Tgfb sensitivity, Total protein lysates, Transduction, Transfected, Western blot, Western blot analysis, Wetsel.
Abstract
Embryonic and fetal skeletal myoblasts are responsible for the formation of primary and secondary fibers in mammals, but the mechanism which diversifies their fate is unknown.In vitro,embryonic myoblasts are resistant to the differentiation inhibitory effects of transforming growth factor β and phorbol esters. Thus, differential expression of specific molecules involved in the transduction of extracellular signals may contribute to the different phenotypes. We report here that protein kinase C θ, but none of the other known protein kinase C isoforms, is selectively expressed in fetal and postnatal muscle cells (at both the myoblast and myotube stage)in vitroandin vivo.By contrast, embryonic myoblasts and myotubes do not express protein kinase C θin vitroorin vivo.This difference is causally related to a differential response to transforming growth factor β, since overexpression of protein kinase C θ, but not of protein kinase C α or ζ, in embryonic myoblasts makes these cells sensitive to transforming growth factor β. These data demonstrate for the first time that a protein kinase C isoform is a key component of the signal transduction cascade which follows exposure of myoblasts to transforming growth factor β. They also suggest a specific role for protein kinase C θ in determining the fate of different myoblasts during muscle histogenesis.
Url:
DOI: 10.1006/dbio.1996.0292
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Wetsel</name><affiliation wicri:level="2"><mods:affiliation>Laboratory of Cellular and Molecular Pharmacology, National Institute of Environmental Health Sciences, North Carolina</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Laboratory of Cellular and Molecular Pharmacology, National Institute of Environmental Health Sciences</wicri:cityArea></affiliation></author><author><name sortKey="Molinaro, Mario" sort="Molinaro, Mario" uniqKey="Molinaro M" first="Mario" last="Molinaro">Mario Molinaro</name><affiliation wicri:level="1"><mods:affiliation>Institute of Histology and General Embryology, University of Rome “La Sapienza,” 00161, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Histology and General Embryology, University of Rome “La Sapienza,” 00161</wicri:regionArea></affiliation></author><author><name sortKey="Cossu, Giulio" sort="Cossu, Giulio" uniqKey="Cossu G" first="Giulio" last="Cossu">Giulio Cossu</name><affiliation wicri:level="1"><mods:affiliation>Institute of Histology and General Embryology, University of Rome “La Sapienza,” 00161, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Histology and General Embryology, University of Rome “La Sapienza,” 00161</wicri:regionArea></affiliation></author><author><name sortKey="Bouche, Marina" sort="Bouche, Marina" uniqKey="Bouche M" first="Marina" last="Bouché">Marina Bouché</name><affiliation wicri:level="1"><mods:affiliation>Institute of Histology and General Embryology, University of Rome “La Sapienza,” 00161, Italy</mods:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Histology and General Embryology, University of Rome “La Sapienza,” 00161</wicri:regionArea></affiliation></author></analytic><monogr></monogr><series><title level="j">Developmental Biology</title><title level="j" type="abbrev">YDBIO</title><idno type="ISSN">0012-1606</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1996">1996</date><biblScope unit="volume">180</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="156">156</biblScope><biblScope unit="page" to="164">164</biblScope></imprint><idno type="ISSN">0012-1606</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0012-1606</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Angelis</term><term>Bers</term><term>Biol</term><term>Bouche</term><term>Cdna</term><term>Cell biol</term><term>Cell proliferation</term><term>Copyright</term><term>Cos1 cells</term><term>Cossu</term><term>Different isoforms</term><term>Differential expression</term><term>Differential response</term><term>Differential sensitivity</term><term>Differentiation</term><term>Embryo</term><term>Embryo limbs</term><term>Embryonic</term><term>Embryonic myoblasts</term><term>Expression vectors</term><term>Fetal</term><term>Fetal muscle</term><term>Fetal myoblasts</term><term>Growth factor</term><term>Growth factors</term><term>High levels</term><term>Histogenesis</term><term>Isoform</term><term>Isoforms</term><term>Kinase</term><term>Limb</term><term>Molinaro</term><term>Mouse embryos</term><term>Muscle histogenesis</term><term>Myoblast</term><term>Myoblasts</term><term>Myogenic</term><term>Myogenic cells</term><term>Myogenic differentiation</term><term>Myosin</term><term>Myotubes</term><term>Osada</term><term>Overexpression</term><term>Pkcu</term><term>Pkcu expression</term><term>Positive control</term><term>Possible role</term><term>Protein kinase</term><term>Satellite cells</term><term>Signal transduction</term><term>Skeletal muscle</term><term>Tgfb</term><term>Tgfb sensitivity</term><term>Total protein lysates</term><term>Transduction</term><term>Transfected</term><term>Western blot</term><term>Western blot analysis</term><term>Wetsel</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Embryonic and fetal skeletal myoblasts are responsible for the formation of primary and secondary fibers in mammals, but the mechanism which diversifies their fate is unknown.In vitro,embryonic myoblasts are resistant to the differentiation inhibitory effects of transforming growth factor β and phorbol esters. Thus, differential expression of specific molecules involved in the transduction of extracellular signals may contribute to the different phenotypes. We report here that protein kinase C θ, but none of the other known protein kinase C isoforms, is selectively expressed in fetal and postnatal muscle cells (at both the myoblast and myotube stage)in vitroandin vivo.By contrast, embryonic myoblasts and myotubes do not express protein kinase C θin vitroorin vivo.This difference is causally related to a differential response to transforming growth factor β, since overexpression of protein kinase C θ, but not of protein kinase C α or ζ, in embryonic myoblasts makes these cells sensitive to transforming growth factor β. These data demonstrate for the first time that a protein kinase C isoform is a key component of the signal transduction cascade which follows exposure of myoblasts to transforming growth factor β. They also suggest a specific role for protein kinase C θ in determining the fate of different myoblasts during muscle histogenesis.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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