Yu Ting Zheng

TL;DR: It is hypothesized that protein-protein interactions between PKC&egr; and mitochondrial pore components may serve as a signaling mechanism to modulate pore function and thus engender cardioprotection, and in vitro studies demonstrated that PKC &egr ; can directly bind and phosphorylate VDAC1.

TL;DR: Together, data show that PKCepsilon forms subcellular-targeted signaling modules with ERKs, leading to the activation of mitochondrialERKs.

TL;DR: The results support the concept that, in conscious rabbits, 2 specific members of the Src family of tyrosine kinases, Src and Lck, play an important role in the genesis of late PC by serving as downstream elements of PKC-mediated signal transduction.

TL;DR: It is demonstrated that ischemic PC activates p46 and p54 JNKs via a PKC-ε-dependent signaling pathway and that there are important differences between p 46 and p 54 J NKs with respect to the subcellular compartment and the mechanism of their activation after ischeMIC PC.

TL;DR: These findings are the first to demonstrate increased NO bioavailability with attenuation of ROS by direct measurement of these reactive species (EPR, reactive fluorescent dyes with cardiac-specific ecSOD expression) and the first indication that the predominantly extracellular SOD isoform is capable of cytosolic localization that affects myocardial intracellular signal transduction and function.