Browsing by Author "Jinha, Azim"
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- ItemOpen AccessAnalyses of muscle force predictions based on optimization(2002) Jinha, Azim; Herzog, Walter
- ItemOpen AccessAre titin properties reflected in single myofibrils?(Journal of Biomechanics, 2012-07-26) Herzog, Jens A.; Leonard, Timothy R.; Jinha, Azim; Herzog, WalterTitin is a structural protein in muscle that spans the half sarcomere from Z-band to M-line. Although there are selected studies on titin's mechanical properties from tests on isolated molecules or titin fragments, little is known about its behavior within the structural confines of a sarcomere. Here, we tested the hypothesis that titin properties might be reflected well in single myofibrils. Single myofibrils from rabbit psoas were prepared for measurement of passive stretch-shortening cycles at lengths where passive titin forces occur. Three repeat stretch-shortening cycles with magnitudes between 1.0 and 3.0μm/sarcomere were performed at a speed of 0.1μm/s·sarcomere and repeated after a ten minute rest at zero force. These tests were performed in a relaxation solution (passive) and an activation solution (active) where cross-bridge attachment was inhibited with 2,3 butanedionemonoxime. Myofibrils behaved viscoelastically producing an increased efficiency with repeat stretch-shortening cycles, but a decreased efficiency with increasing stretch magnitudes. Furthermore, we observed a first distinct inflection point in the force-elongation curve at an average sarcomere length of 3.5μm that was associated with an average force of 68±5nN/mm. This inflection point was thought to reflect the onset of Ig domain unfolding and was missing after a ten minute rest at zero force, suggesting a lack of spontaneous Ig domain refolding. These passive myofibrillar properties observed here are consistent with those observed in isolated titin molecules, suggesting that the mechanics of titin are well preserved in isolated myofibrils, and thus, can be studied readily in myofibrils, rather than in the extremely difficult and labile single titin preparations.
- ItemOpen AccessEffect of Vastus Medialis Loss on Rabbit Patellofemoral Joint Contact Pressure Distribution(2020-08) Han, Seong-won; Sawatsky, Andrew; Jinha, Azim; Herzog, WalterVastus medialis (VM) weakness is thought to alter patellar tracking, thereby changing the loading of the patellofemoral joint (PFJ), resulting in patellofemoral pain. However, it is challenging to measure VM force and weakness in human studies, nor is it possible to measure the associated mechanical changes in the PFJ. To obtain fundamental insight into VM weakness and its effects on PFJ mechanics, the authors determined PFJ loading in the presence of experimentally simulated VM weakness. Skeletally mature New Zealand White rabbits were used (n = 6), and the vastus lateralis, VM, and rectus femoris were stimulated individually through 3 custom-built nerve cuff electrodes. Muscle torque and PFJ pressure distribution were measured while activating all muscles simultaneously, or when the vastus lateralis and rectus femoris were activated, while VM was not, to simulate a quadriceps muscle strength imbalance. For a given muscular joint torque, peak pressures were greater and joint contact areas were smaller when simulating VM weakness compared with the condition where all muscles were activated simultaneously. The results in the rabbit model support that VM weakness results in altered PFJ loading, which may cause patellofemoral pain, often associated with a strength imbalance of the knee extensor muscle group.
- ItemOpen AccessOn sarcomere length stability during isometric contractions before and after active stretching(2019-11-27) Johnston, Kaleena; Moo, Engkuan; Jinha, Azim; Herzog, WalterSarcomere length (SL) instability and SL non-uniformity have been used to explain fundamental properties of skeletal muscles, such as creep, force depression following active muscle shortening and residual force enhancement following active stretching of muscles. Regarding residual force enhancement, it has been argued that active muscle stretching causes SL instability, thereby increasing SL non-uniformity. However, we recently showed that SL non-uniformity is not increased by active muscle stretching, but it remains unclear if SL stability is affected by active stretching. Here, we used single myofibrils of rabbit psoas muscle and measured SL non-uniformity and SL instability during isometric contractions and for isometric contractions following active stretching at average SLs corresponding to the descending limb of the force-length relationship. We defined isometric contractions as contractions during which mean SL remained constant. SL instability was quantified by the rate of change of individual SLs over the course of steady-state isometric force and SL non-uniformity was defined as deviations of SLs from the mean SL at an instant of time. We found that whereas the mean SL remained constant during isometric contraction, by definition, individual SLs did not. SLs were more stable in the force-enhanced, isometric state following active stretching compared with the isometric reference state. We also found that SL instability was not correlated with the rate of change of SL non-uniformity. Also, SL non-uniformity was not different in the isometric and the post-stretch isometric contractions. We conclude that since SL is more stable but similarly non-uniform in the force-enhanced compared with the corresponding isometric reference contraction, it appears unlikely that either SL instability or SL non-uniformity contribute to the residual force enhancement property of skeletal muscle.
- ItemOpen AccessSarcomere length measurement reliability in single myofibrils(Elsevier, 2021-07-12) Schmidt, Jonas; Jinha, Azim; Herzog, WalterSarcomere length non-uniformities occur at all structural levels of skeletal muscles and have been associated with important mechanical properties. Changes in sarcomere length non-uniformities in the nano- and sub-nanometer range have been used to explain muscle properties and contractile mechanisms. Typically, these measurements rely on light microscopy with a limited spatial resolution. One critical aspect in sarcomere length determination is the relatively arbitrary choice of intensity thresholds used to delineate sarcomere structures, such as A-bands or Z-lines. In experiments, these structures are typically distorted, intensity profiles vary, and baselines drift, resulting in asymmetric intensity patterns, causing changes in the centroid location of these structures depending on threshold choice, resulting in changes of sarcomere lengths. The purpose of this study was to determine the changes in (half-) sarcomere lengths associated with small changes in the A-band threshold choice. Sarcomere and half-sarcomere length changes for minute variations in A-band threshold were 28 nm (± 28 nm) and 18 nm (± 22 nm), respectively, and for the entire feasible range of thresholds across A-bands were 123 nm (± 88 nm) and 99 nm (± 105 nm), respectively. We conclude from these results that (half-) sarcomere lengths in the nanometer range obtained with light microcopy are noise, and the functional implications associated with such data should be discarded. We suggest that a functional resolution for sarcomere length of 100 nm (0.1 µm) is reasonable and 50 nm (0.05 µm) might be possible under ideal conditions.