[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.
|Qualification||Doctor of Philosophy|
|Publication status||Unpublished - 2002|
- This thesis has been made available in the UWA Profiles and Research Repository as part of a UWA Library project to digitise and make available theses completed before 2003. If you are the author of this thesis and would like it removed from the UWA Profiles and Research Repository, please contact email@example.com