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 :Based on arguments outlined in the literature (30–32), the steady-state [Ca2+] dependence of the RyR was generally modeled as a monotonically increasing fourth-order Hill sigmoidal (Fig. 1 A). This is consistent with the tetrameric nature of the RyR protein, although it should be noted that under different experimental conditions the degree of cooperativity implied by the Hill coefficient can lie between 2 and 7 (28,33,34). In some simulations, therefore, the value of this coefficient was varied systematically to assess its dynamical role.
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