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During systole, Ca2+ binds to a lowaffinity binding site in the TnC N-terminal domain, causing an increased affinity between this domain and the TnI N-terminal domain. 2 Specifically, as cytosolic Ca2+ levels decrease, Ca2+ is removed from the TnC low-affinity binding site, causing TnI to dissociate from TnC and then reassociate with actin, effectively re-establishing the steric hindrance imposed by the troponin-tropomyosin complex. As discussed in detail below, the dynamic range of cardiac excitation-mechanical coupling is, in part, regulated by phosphoregulation of key ion channels and transporters, which modulate intracellular Ca2+ in addition to altering the Ca2+ sensitivity of contractile proteins.

Rentschler S, Vaidya DM, Tamaddon H, et al: Visualization and functional characterization of the developing murine cardiac conduction system, Development 128(10):1785–1792, 2001. 36. Qu J, Volpicelli FM, Garcia LI, et al: Gap junction remodeling and spironolactone-dependent reverse remodeling in the hypertrophied heart, Circ Res 104(3):365–371, 2009. 1 16 Conceptual Basis for Current Practice of Cardiac Arrhythmology 37. Shalaby FY, Levesque PC, Yang WP, et al: Dominant-negative KvLQT1 mutations underlie the LQT1 form of long QT syndrome, Circulation 96(6):1733–1736, 1997.

Specifically, unlike the first plant cell imaged by Hooke in the mid1600s, it is now known that the vertebrate myocyte is not simply a large pool of cytosol surrounded by a simple membrane. Rather, the metazoan myocyte has evolved complex membrane structures to facilitate efficient electrical activity and signaling to regulate cardiac physiology. Not surprisingly, specific cell types in the heart possess a distinct set of membrane structures based on their unique function. The ventricular cardiomyocyte plasma membrane, or sarcolemma, is divided into multiple and unique membrane structures (Figure 2-2).

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