Mechanically Driven Contour-Length Adjustment in Rat Cardiac Titin’s Unique N2B Sequence
نویسندگان
چکیده
منابع مشابه
Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes.
beta-Adrenergic stimulation of cardiac muscle activates protein kinase A (PKA), which is known to phosphorylate proteins on the thin and thick filaments of the sarcomere. Cardiac muscle sarcomeres contain a third filament system composed of titin, and here we demonstrate that titin is also phosphorylated by the beta-adrenergic pathway. Titin phosphorylation was observed after beta-receptor stim...
متن کاملProtein Kinase A Phosphorylates Cardiac-Specific N2B Domain of Titin and Reduces Passive Tension in Rat Cardiac Myocytes
b-Adrenergic stimulation of cardiac muscle activates protein kinase A (PKA), which is known to phosphorylate proteins on the thin and thick filaments of the sarcomere. Cardiac muscle sarcomeres contain a third filament system composed of titin, and in this study, we demonstrate that titin is also phosphorylated by the b-adrenergic pathway. Titin phosphorylation was observed after b-receptor sti...
متن کاملDeletion of the titin N2B region accelerates myofibrillar force development but does not alter relaxation kinetics.
Cardiac titin is the main determinant of sarcomere stiffness during diastolic relaxation. To explore whether titin stiffness affects the kinetics of cardiac myofibrillar contraction and relaxation, we used subcellular myofibrils from the left ventricles of homozygous and heterozygous N2B-knockout mice which express truncated cardiac titins lacking the unique elastic N2B region. Compared with my...
متن کاملMolecular mechanics of cardiac titin's PEVK and N2B spring elements.
Titin is a giant elastic protein that is responsible for the majority of passive force generated by the myocardium. Titin's force is derived from its extensible I-band region, which, in the cardiac isoform, comprises three main extensible elements: tandem Ig segments, the PEVK domain, and the N2B unique sequence (N2B-Us). Using atomic force microscopy, we characterized the single molecule force...
متن کاملSeries of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity.
Titins are megadalton-sized filamentous polypeptides of vertebrate striated muscle. The I-band region of titin underlies the myofibrillar passive tension response to stretch. Here, we show how titins with highly diverse I-band structures and elastic properties are expressed from a single gene. The differentially expressed tandem-Ig, PEVK, and N2B spring elements of titin are coded by 158 exons,...
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ژورنال
عنوان ژورنال: Circulation Research
سال: 1999
ISSN: 0009-7330,1524-4571
DOI: 10.1161/01.res.84.11.1339