Yiming Wu

TL;DR: Investigating titin expression in patients with end-stage heart failure resulting from nonischemic dilated cardiomyopathy found changes in titin isoform expression significantly impact diastolic filling by lowering myocardial stiffness and clinical correlations support the relevance of these changes for LV function.

TL;DR: Investigation of titin expression at the protein level in a wide range of mammalian species indicates that the myocardium coexpresses 2 distinct titin isoforms, and Immunofluorescence experiments with isoform-specific antibodies suggest that coexpression of these isoforms takes place at the single-myocyte level.

TL;DR: It is proposed that the PEVK segment contains E-rich motifs that render titin a calcium-dependent molecular spring that adapts to the physiological state of the cell.

TL;DR: Cardiac muscle sarcomeres contain a third filament system composed of titin, and it is demonstrated that titin is also phosphorylated by therenergic pathway, suggesting that tit in phosphorylation may modulate cardiac function in vivo.

TL;DR: Examination of titin expression and altered function during cardiac muscle development in a range of species revealed expression of fetal titin isoforms, characterized by additional spring elements both in the tandem Ig and PEVK region of the molecule.