Regular ArticlePorphyrin Induced Calcium Release from Skeletal Muscle Sarcoplasmic Reticulum
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Dynamics of a three-variable nonlinear model of vasomotion: Comparison of theory and experiment
2007, Biophysical JournalCitation Excerpt :In some simulations, therefore, the value of this coefficient was varied systematically to assess its dynamical role. Ca2+ concentrations resulting in half-maximal activation of the RyR were varied between 0.2 and 0.9 μM to encompass the range of values reported in the literature (27,28,33). No attempt was made to allow for differences in the gating characteristics of the three RyR subtypes or spatial heterogeneity in their possible subcellular location (22,26).
o-Phthalaldehyde activates the Ca<sup>2+</sup> release mechanism from skeletal muscle sarcoplasmic reticulum
2001, Archives of Biochemistry and BiophysicsSkeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators
2000, Journal of Biological ChemistryCitation Excerpt :In a similar manner, an increase in the cellular redox potential during oxidative stress (induced by fatigue, aging, or ischemia) should result in oxidation of the ryanodine receptor/Ca2+ release protein and the opening of the Ca2+ release pathway. Our previous studies have shown that oxidation induced by quinones, porphyrins and H2O2 is strongly Ca2+ dependent (8, 10, 24). A likely explanation for the Ca2+ dependence of oxidation-induced Ca2+release from SR vesicles is directly related to the measurements of redox potential described in this manuscript.
Radiosynthesis and quality control of [<sup>67</sup>Ga]-3,4-dimethoxylated porphyrin complex as a possible imaging agent
2013, Iranian Journal of Pharmaceutical Research