Modulation of intracellular calcium handling in skeletal muscle cells by inhibitors of protein kinase C and phospholipase A2

Renzhi Han

doi:10.26182/5d50b26de9ab4

Modulation of intracellular calcium handling in skeletal muscle cells by inhibitors of protein kinase C and phospholipase A₂

Renzhi Han

Research output: Thesis › Doctoral Thesis

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Abstract

[Truncated] In this study, an investigation was undertaken into the regulation of excitation contraction coupling, calcium handling properties and SR function by protein kinase C (PKC) and phospholipase A₂ (PLA₂) in C2C12 myotubes, normal and mdx myotubes, and in mechanically skinned EDL muscle fibres of the rat.1. The PKC inhibitor calphostin C significantly increased the decay time of electrically induced Ca²⁺-dependent fluorescence changes but had no significant effect on the peak of the Ca²⁺-dependent fluorescence changes in C2Cl2 myotubes or the caffeine-induced Ca²⁺ release in skinned adult skeletal muscle fibres of the rat. The PKC activator PMA decreased the decay time of the Ca²⁺-dependent fluorescence changes. These results suggest that PKC is involved in the control of the SR Ca²⁺ pump function in skeletal muscle. Calphostin C also significantly increased the peak of the ATP-induced Ca²⁺ responses in C2C12 myotubes, suggesting PKC inhibition by calphostin C may modulate the phospholipase C (PLC)-inositol-(1, 4, 5) trisphosphate (IP₃)-sensitive Ca²⁺ release. Finally, calphostin C was observed to increase the cytosolic Ca²⁺ concentration within 10-15 min and caused cell shrinkage and eventual necrosis.

Original language	English
Qualification	Doctor of Philosophy
Awarding Institution	The University of Western Australia
DOIs	https://doi.org/10.26182/5d50b26de9ab4
Publication status	Unpublished - 2002

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Han_Renzhi_2002
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Cite this

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title = "Modulation of intracellular calcium handling in skeletal muscle cells by inhibitors of protein kinase C and phospholipase A2",

abstract = "[Truncated] In this study, an investigation was undertaken into the regulation of excitation contraction coupling, calcium handling properties and SR function by protein kinase C (PKC) and phospholipase A2 (PLA2) in C2C12 myotubes, normal and mdx myotubes, and in mechanically skinned EDL muscle fibres of the rat.1. The PKC inhibitor calphostin C significantly increased the decay time of electrically induced Ca2+-dependent fluorescence changes but had no significant effect on the peak of the Ca2+-dependent fluorescence changes in C2Cl2 myotubes or the caffeine-induced Ca2+ release in skinned adult skeletal muscle fibres of the rat. The PKC activator PMA decreased the decay time of the Ca2+-dependent fluorescence changes. These results suggest that PKC is involved in the control of the SR Ca2+ pump function in skeletal muscle. Calphostin C also significantly increased the peak of the ATP-induced Ca2+ responses in C2C12 myotubes, suggesting PKC inhibition by calphostin C may modulate the phospholipase C (PLC)-inositol-(1, 4, 5) trisphosphate (IP3)-sensitive Ca2+ release. Finally, calphostin C was observed to increase the cytosolic Ca2+ concentration within 10-15 min and caused cell shrinkage and eventual necrosis.",

author = "Renzhi Han",

year = "2002",

doi = "10.26182/5d50b26de9ab4",

language = "English",

school = "The University of Western Australia",

}

TY - BOOK

T1 - Modulation of intracellular calcium handling in skeletal muscle cells by inhibitors of protein kinase C and phospholipase A2

AU - Han, Renzhi

PY - 2002

Y1 - 2002

N2 - [Truncated] In this study, an investigation was undertaken into the regulation of excitation contraction coupling, calcium handling properties and SR function by protein kinase C (PKC) and phospholipase A2 (PLA2) in C2C12 myotubes, normal and mdx myotubes, and in mechanically skinned EDL muscle fibres of the rat.1. The PKC inhibitor calphostin C significantly increased the decay time of electrically induced Ca2+-dependent fluorescence changes but had no significant effect on the peak of the Ca2+-dependent fluorescence changes in C2Cl2 myotubes or the caffeine-induced Ca2+ release in skinned adult skeletal muscle fibres of the rat. The PKC activator PMA decreased the decay time of the Ca2+-dependent fluorescence changes. These results suggest that PKC is involved in the control of the SR Ca2+ pump function in skeletal muscle. Calphostin C also significantly increased the peak of the ATP-induced Ca2+ responses in C2C12 myotubes, suggesting PKC inhibition by calphostin C may modulate the phospholipase C (PLC)-inositol-(1, 4, 5) trisphosphate (IP3)-sensitive Ca2+ release. Finally, calphostin C was observed to increase the cytosolic Ca2+ concentration within 10-15 min and caused cell shrinkage and eventual necrosis.

AB - [Truncated] In this study, an investigation was undertaken into the regulation of excitation contraction coupling, calcium handling properties and SR function by protein kinase C (PKC) and phospholipase A2 (PLA2) in C2C12 myotubes, normal and mdx myotubes, and in mechanically skinned EDL muscle fibres of the rat.1. The PKC inhibitor calphostin C significantly increased the decay time of electrically induced Ca2+-dependent fluorescence changes but had no significant effect on the peak of the Ca2+-dependent fluorescence changes in C2Cl2 myotubes or the caffeine-induced Ca2+ release in skinned adult skeletal muscle fibres of the rat. The PKC activator PMA decreased the decay time of the Ca2+-dependent fluorescence changes. These results suggest that PKC is involved in the control of the SR Ca2+ pump function in skeletal muscle. Calphostin C also significantly increased the peak of the ATP-induced Ca2+ responses in C2C12 myotubes, suggesting PKC inhibition by calphostin C may modulate the phospholipase C (PLC)-inositol-(1, 4, 5) trisphosphate (IP3)-sensitive Ca2+ release. Finally, calphostin C was observed to increase the cytosolic Ca2+ concentration within 10-15 min and caused cell shrinkage and eventual necrosis.

U2 - 10.26182/5d50b26de9ab4

DO - 10.26182/5d50b26de9ab4

M3 - Doctoral Thesis