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The Amino Terminal Region Of Cardiac Myosin Binding Protein-C Is Necessary For Cardiac Function, Thomas Lawrence Lynch
The Amino Terminal Region Of Cardiac Myosin Binding Protein-C Is Necessary For Cardiac Function, Thomas Lawrence Lynch
Dissertations
Cardiac myosin binding protein-C (cMyBP-C) is a thick filament-associated protein that has been suggested to regulate cardiac contraction via its amino terminal (N’) region. Following ischemic injury to the heart, cMyBP-C is cleaved into a predominant N’ fragment consisting of domains C0 through C1 and the first 17 residues of the M-domain that is referred to as C0-C1f. However, the necessity of the N’-C0-C1f region of cMyBP-C in regulating cardiac function in vivo has not been elucidated. I hypothesized that the N’-C0-C1f region of cMyBP-C is critical for normal cardiac function in vivo. To test this hypothesis, transgenic (TG) mice …
Heart And Sole: The Functional Role Of Fast-Skeletal Myosin Binding Protein-C In Cardiac And Skeletal Muscle, Brian Leei Lin
Heart And Sole: The Functional Role Of Fast-Skeletal Myosin Binding Protein-C In Cardiac And Skeletal Muscle, Brian Leei Lin
Dissertations
The goal of my dissertation was to compare and contrast the function of all three major isoforms of Myosin Binding Protein-C (MyBP-C): slow-skeletal, fast-skeletal, and cardiac (ssMyBP-C, fsMyBP-C, and cMyBP-C, respectively), with a focus on the least characterized isoform, fsMyBP-C. Using a variety of ex vivo, in vitro, and in silico methods, my research demonstrated that the N-terminal region of all MyBP-C isoforms bind to actin and shift tropomyosin, thus activating the thin filament during contraction. Furthermore, each isoform differentially activated the thin filament over isoform-specific ranges of Ca2+: slow-skeletal activates at low Ca2+, fast-skeletal activates at higher Ca2+, and …