Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture

Regulation of muscle cell Ca2+ metabolism by 1,25-dihydroxy-vitamin D3 [1,25(OH)2D3] is mediated by the classic nuclear mechanism and a fast, nongenomic mode of action that activates signal transduction pathways. The role of individual protein kinase C (PKC) isoforms in the regulation of intracellul...

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Detalles Bibliográficos
Publicado: 2000
Materias:
1,25 (OH)2-vitamin D3
Development
Intracellular Ca2+
Muscle cells
Nongenomic effects
PKC isoforms
Protein kinase C
calcitriol
protein kinase C
animal cell
article
calcium cell level
calcium metabolism
cell culture
cell maturation
chicken
enzyme activity
hormonal regulation
nonhuman
priority journal
signal transduction
skeletal muscle
Animals
Calcitriol
Calcium
Calcium Signaling
Cell Differentiation
Cell Division
Cells, Cultured
Chick Embryo
Diglycerides
Enzyme Inhibitors
Intracellular Fluid
Isoenzymes
Muscle, Skeletal
Protein Kinase C
Subcellular Fractions
Animalia
Gallus gallus
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07302312_v77_n2_p200_Capiati
http://hdl.handle.net/20.500.12110/paper_07302312_v77_n2_p200_Capiati
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_07302312_v77_n2_p200_Capiati
record_format dspace
spelling paper:paper_07302312_v77_n2_p200_Capiati2023-06-08T15:43:46Z Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture 1,25 (OH)2-vitamin D3 Development Intracellular Ca2+ Muscle cells Nongenomic effects PKC isoforms Protein kinase C calcitriol protein kinase C animal cell article calcium cell level calcium metabolism cell culture cell maturation chicken enzyme activity hormonal regulation nonhuman priority journal signal transduction skeletal muscle Animals Calcitriol Calcium Calcium Signaling Cell Differentiation Cell Division Cells, Cultured Chick Embryo Diglycerides Enzyme Inhibitors Intracellular Fluid Isoenzymes Muscle, Skeletal Protein Kinase C Subcellular Fractions Animalia Gallus gallus Regulation of muscle cell Ca2+ metabolism by 1,25-dihydroxy-vitamin D3 [1,25(OH)2D3] is mediated by the classic nuclear mechanism and a fast, nongenomic mode of action that activates signal transduction pathways. The role of individual protein kinase C (PKC) isoforms in the regulation of intracellular Ca2+ levels ([Ca2+](i)) by the hormone was investigated in cultured proliferating (myoblasts) and differentiated (myotubes) chick skeletal muscle cells. 1,25(OH)2D3 (10-9 M) induced a rapid (30- to 60-s) and sustained (>5-min) increase in [Ca2+](i) which was markedly higher in myotubes than in myoblasts. The effect was suppressed by the PKC inhibitor calphostin C. In differentiated cells, PKC activity increased in the particulate fraction and decreased in cytosol to a greater extent than in proliferating cells after 5-min treatment with 1,25(OH)2D3. By Western blot analysis, these changes were correlated to translocation of the PKC α isoform from cytosol to the particulate fraction, which was more pronounced in myotubes than in myoblasts. Specific inhibition of PKC α activity using antibodies against this isoform decreased the 1,25(OH)2D3-induced [Ca2+](i) sustained response associated with Ca2+ influx through voltage- dependent calcium channels. Neomycin, a phospholipase C (PLC) inhibitor, blocked its effects on [Ca2+](i), PKC activity, and translocation of PKC α. Exposure of myotubes to 1,2-dioleyl-rac-glycerol (1,2-diolein), also increased [Ca2+](i), PKC activity, and the amount of PKC α associated with the particulate fraction. Changes in [Ca2+](i) induced by diolein were inhibited by calphostin C and nifedipine. The results indicate that PKC α activation via PLC-catalyzed phosphoinositide hydrolysis is part of the mechanism by which 1,25(OH)2D3 regulates muscle intracellular Ca2+ through modulation of the Ca2+ influx pathway of the Ca2+ response to the sterol. (C) 2000 Wiley-Liss, Inc. 2000 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07302312_v77_n2_p200_Capiati http://hdl.handle.net/20.500.12110/paper_07302312_v77_n2_p200_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 1,25 (OH)2-vitamin D3
Development
Intracellular Ca2+
Muscle cells
Nongenomic effects
PKC isoforms
Protein kinase C
calcitriol
protein kinase C
animal cell
article
calcium cell level
calcium metabolism
cell culture
cell maturation
chicken
enzyme activity
hormonal regulation
nonhuman
priority journal
signal transduction
skeletal muscle
Animals
Calcitriol
Calcium
Calcium Signaling
Cell Differentiation
Cell Division
Cells, Cultured
Chick Embryo
Diglycerides
Enzyme Inhibitors
Intracellular Fluid
Isoenzymes
Muscle, Skeletal
Protein Kinase C
Subcellular Fractions
Animalia
Gallus gallus
spellingShingle 1,25 (OH)2-vitamin D3
Development
Intracellular Ca2+
Muscle cells
Nongenomic effects
PKC isoforms
Protein kinase C
calcitriol
protein kinase C
animal cell
article
calcium cell level
calcium metabolism
cell culture
cell maturation
chicken
enzyme activity
hormonal regulation
nonhuman
priority journal
signal transduction
skeletal muscle
Animals
Calcitriol
Calcium
Calcium Signaling
Cell Differentiation
Cell Division
Cells, Cultured
Chick Embryo
Diglycerides
Enzyme Inhibitors
Intracellular Fluid
Isoenzymes
Muscle, Skeletal
Protein Kinase C
Subcellular Fractions
Animalia
Gallus gallus
Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture
topic_facet 1,25 (OH)2-vitamin D3
Development
Intracellular Ca2+
Muscle cells
Nongenomic effects
PKC isoforms
Protein kinase C
calcitriol
protein kinase C
animal cell
article
calcium cell level
calcium metabolism
cell culture
cell maturation
chicken
enzyme activity
hormonal regulation
nonhuman
priority journal
signal transduction
skeletal muscle
Animals
Calcitriol
Calcium
Calcium Signaling
Cell Differentiation
Cell Division
Cells, Cultured
Chick Embryo
Diglycerides
Enzyme Inhibitors
Intracellular Fluid
Isoenzymes
Muscle, Skeletal
Protein Kinase C
Subcellular Fractions
Animalia
Gallus gallus
description Regulation of muscle cell Ca2+ metabolism by 1,25-dihydroxy-vitamin D3 [1,25(OH)2D3] is mediated by the classic nuclear mechanism and a fast, nongenomic mode of action that activates signal transduction pathways. The role of individual protein kinase C (PKC) isoforms in the regulation of intracellular Ca2+ levels ([Ca2+](i)) by the hormone was investigated in cultured proliferating (myoblasts) and differentiated (myotubes) chick skeletal muscle cells. 1,25(OH)2D3 (10-9 M) induced a rapid (30- to 60-s) and sustained (>5-min) increase in [Ca2+](i) which was markedly higher in myotubes than in myoblasts. The effect was suppressed by the PKC inhibitor calphostin C. In differentiated cells, PKC activity increased in the particulate fraction and decreased in cytosol to a greater extent than in proliferating cells after 5-min treatment with 1,25(OH)2D3. By Western blot analysis, these changes were correlated to translocation of the PKC α isoform from cytosol to the particulate fraction, which was more pronounced in myotubes than in myoblasts. Specific inhibition of PKC α activity using antibodies against this isoform decreased the 1,25(OH)2D3-induced [Ca2+](i) sustained response associated with Ca2+ influx through voltage- dependent calcium channels. Neomycin, a phospholipase C (PLC) inhibitor, blocked its effects on [Ca2+](i), PKC activity, and translocation of PKC α. Exposure of myotubes to 1,2-dioleyl-rac-glycerol (1,2-diolein), also increased [Ca2+](i), PKC activity, and the amount of PKC α associated with the particulate fraction. Changes in [Ca2+](i) induced by diolein were inhibited by calphostin C and nifedipine. The results indicate that PKC α activation via PLC-catalyzed phosphoinositide hydrolysis is part of the mechanism by which 1,25(OH)2D3 regulates muscle intracellular Ca2+ through modulation of the Ca2+ influx pathway of the Ca2+ response to the sterol. (C) 2000 Wiley-Liss, Inc.
title Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture
title_short Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture
title_full Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture
title_fullStr Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture
title_full_unstemmed Role of protein kinase C in 1,25(OH)2-vitamin D3 modulation of intracellular calcium during development of skeletal muscle cells in culture
title_sort role of protein kinase c in 1,25(oh)2-vitamin d3 modulation of intracellular calcium during development of skeletal muscle cells in culture
publishDate 2000
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_07302312_v77_n2_p200_Capiati
http://hdl.handle.net/20.500.12110/paper_07302312_v77_n2_p200_Capiati
_version_ 1768542181641945088

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