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10.1016/j.abb.2013.11.005 http://scihub22266oqcxt.onion/10.1016/j.abb.2013.11.005 C4028433!4028433 !24269766     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\24269766 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Arch+Biochem+Biophys 2014 ; 552-553 (ä): 83-91 Nephropedia Template TP {{tp|p=24269766 |t=2014. Titin-mediated control of cardiac myofibrillar function |pdf=|usr=}}{{24269766 }} gab.com Text Titin-mediated control of cardiac myofibrillar function JO: Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=24269766 #FOAvip According to the Frank-Starling relationship, ventricular pressure or stroke volume increases with end-diastolic volume. This is regulated, in large part, by the sarcomere length (SL) dependent changes in cardiac myofibrillar force, loaded shortening, and power. Consistent with this, both cardiac myofibrillar force and absolute power fall at shorter SL. However, when Ca(2+) activated force levels are matched between short and long SL (by increasing the activator [Ca(2+)]), short SL actually yields faster loaded shortening and greater peak normalized power output (PNPO). A potential mechanism for faster loaded shortening at short SL is that, at short SL, titin becomes less taut, which increases the flexibility of the cross-bridges, a process that may be mediated by titin's interactions with thick filament proteins. We propose a more slackened titin yields greater myosin head radial and azimuthal mobility and these flexible cross-bridges are more likely to maintain thin filament activation, which would allow more force-generating cross-bridges to work against a fixed load resulting in faster loaded shortening. We tested this idea by measuring SL-dependence of power at matched forces in rat skinned cardiac myocytes containing either N2B titin or a longer, more compliant N2BA titin. We predicted that, in N2BA titin containing cardiac myocytes, power-load curves would not be shifted upward at short SL compared to long SL (when force is matched). Consistent with this, peak normalized power was actually less at short SL versus long SL (at matched force) in N2BA-containing myocytes (N2BA titin: ?PNPO (Short SL peak power minus long SL peak power)=-0.057±0.049 (n=5) versus N2B titin: ?PNPO=+0.012±0.012 (n=5). These findings support a model whereby SL per se controls mechanical properties of cross-bridges and this process is mediated by titin. This myofibrillar mechanism may help sustain ventricular power during periods of low preloads, and perhaps a breakdown of this mechanism is involved in impaired function of failing hearts. Twit Text FOAVip Titin-mediated control of cardiac myofibrillar function ????Arch Biochem Biophys http://www.kidney.de/pget.php?&tw=1&pmid=24269766 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24269766 #FOAvip English Wikipedia <ref>{{Cite pmid|24269766 }}</ref> Titin-mediated control of cardiac myofibrillar function #MMPMID24269766 Hanft LM ; Greaser ML ; McDonald KS Arch Biochem Biophys 2014[Jun]; 552-553 (ä): 83-91 PMID24269766 show ga According to the Frank-Starling relationship, ventricular pressure or stroke volume increases with end-diastolic volume. This is regulated, in large part, by the sarcomere length (SL) dependent changes in cardiac myofibrillar force, loaded shortening, and power. Consistent with this, both cardiac myofibrillar force and absolute power fall at shorter SL. However, when Ca(2+) activated force levels are matched between short and long SL (by increasing the activator [Ca(2+)]), short SL actually yields faster loaded shortening and greater peak normalized power output (PNPO). A potential mechanism for faster loaded shortening at short SL is that, at short SL, titin becomes less taut, which increases the flexibility of the cross-bridges, a process that may be mediated by titin's interactions with thick filament proteins. We propose a more slackened titin yields greater myosin head radial and azimuthal mobility and these flexible cross-bridges are more likely to maintain thin filament activation, which would allow more force-generating cross-bridges to work against a fixed load resulting in faster loaded shortening. We tested this idea by measuring SL-dependence of power at matched forces in rat skinned cardiac myocytes containing either N2B titin or a longer, more compliant N2BA titin. We predicted that, in N2BA titin containing cardiac myocytes, power-load curves would not be shifted upward at short SL compared to long SL (when force is matched). Consistent with this, peak normalized power was actually less at short SL versus long SL (at matched force) in N2BA-containing myocytes (N2BA titin: ?PNPO (Short SL peak power minus long SL peak power)=-0.057±0.049 (n=5) versus N2B titin: ?PNPO=+0.012±0.012 (n=5). These findings support a model whereby SL per se controls mechanical properties of cross-bridges and this process is mediated by titin. This myofibrillar mechanism may help sustain ventricular power during periods of low preloads, and perhaps a breakdown of this mechanism is involved in impaired function of failing hearts. |Animals [MESH] |Cells, Cultured [MESH] |Connectin/chemistry/*metabolism [MESH] |Models, Molecular [MESH] |Myocytes, Cardiac/chemistry/cytology/*metabolism [MESH] |Myofibrils/chemistry/*metabolism [MESH] |Protein Isoforms/chemistry/metabolism [MESH] |Rats [MESH] |Rats, Inbred BN [MESH] |Rats, Inbred F344 [MESH]Titin-mediated control of cardiac myofibrillar function (epmc).pdf DeepDyve Pubget Overpricing