The Kinetics of Cross-bridge Turnover

1976 ◽  
pp. 53-68 ◽  
Author(s):  
R. J. Podolsky
Keyword(s):  
Cross Bridge ◽  
Kinetics Of

Single Molecule Detection Approach to Muscle Study: Kinetics of a Single Cross-Bridge During Contraction of Muscle

2012 ◽  
pp. 311-334 ◽  
Author(s):  
Julian Borejdo ◽  
Danuta Szczesna-Cordary ◽  
Priya Muthu ◽  
Prasad Metticolla ◽  
Rafal Luchowski ◽  
...  
Keyword(s):  
Single Molecule ◽  
Single Molecule Detection ◽  
Cross Bridge ◽  
Detection Approach ◽  
Single Cross ◽  
Kinetics Of

The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment

1997 ◽  
Vol 273 (5) ◽  
pp. H2428-H2435 ◽  
Author(s):  
Thomas Wannenburg ◽  
Paul M. L. Janssen ◽  
Dongsheng Fan ◽  
Pieter P. De Tombe
Keyword(s):  
Cardiac Muscle ◽  
Maximum Rate ◽  
Sarcomere Length ◽  
Myosin Head ◽  
Isometric Force ◽  
Force Development ◽  
Cross Bridge ◽  
Average Slope ◽  
The Cross ◽  
Kinetics Of

We tested the hypothesis that the Frank-Starling relationship is mediated by changes in the rate of cross-bridge detachment in cardiac muscle. We simultaneously measured isometric force development and the rate of ATP consumption at various levels of Ca2+ activation in skinned rat cardiac trabecular muscles at three sarcomere lengths (2.0, 2.1, and 2.2 μm). The maximum rate of ATP consumption was 1.5 nmol ⋅ s−1 ⋅ μl fiber vol−1, which represents an estimated adenosinetriphosphatase (ATPase) rate of ∼10 s−1 per myosin head at 24°C. The rate of ATP consumption was tightly and linearly coupled to the level of isometric force development, and changes in sarcomere length had no effect on the slope of the force-ATPase relationships. The average slope of the force-ATPase relationships was 15.5 pmol ⋅ mN−1 ⋅ mm−1. These results suggest that the mechanisms that underlie the Frank-Starling relationship in cardiac muscle do not involve changes in the kinetics of the apparent detachment step in the cross-bridge cycle.

scholarly journals Kinetics of a Ca(2+)-sensitive cross-bridge state transition in skeletal muscle fibers. Effects due to variations in thin filament activation by extraction of troponin C.

1991 ◽  
Vol 98 (2) ◽  
pp. 233-248 ◽  
Author(s):  
J M Metzger ◽  
R L Moss
Keyword(s):  
Steady State ◽  
Direct Effect ◽  
Thin Filament ◽  
Near Neighbor ◽  
Troponin C ◽  
Isometric Tension ◽  
Cross Bridge ◽  
Filament Activation ◽  
Kinetics Of ◽  
Partial Extraction

The rate constant of tension redevelopment (ktr; 1986. Proc. Natl. Acad. Sci. USA. 83:3542-3546) was determined at various levels of thin filament activation in skinned single fibers from mammalian fast twitch muscles. Activation was altered by (a) varying the concentration of free Ca2+ in the activating solution, or (b) extracting various amounts of troponin C (TnC) from whole troponin complexes while keeping the concentration of Ca2+ constant. TnC was extracted by bathing the fiber in a solution containing 5 mM EDTA, 10 mM HEPES, and 0.5 mM trifluoperazine dihydrochloride. Partial extraction of TnC resulted in a decrease in the Ca2+ sensitivity of isometric tension, presumably due to disruption of near-neighbor molecular cooperativity between functional groups (i.e., seven actin monomers plus associated troponin and tropomyosin) within the thin filament. Altering the level of thin filament activation by partial extraction of TnC while keeping Ca2+ concentration constant tested whether the Ca2+ sensitivity of ktr results from a direct effect of Ca2+ on cross-bridge state transitions or, alternatively, an indirect effect of Ca2+ on these transitions due to varying extents of thin filament activation. Results showed that the ktr-pCa relation was unaffected by partial extraction of TnC, while steady-state isometric tension exhibited the expected reduction in Ca2+ sensitivity. This finding provides evidence for a direct effect of Ca2+ on an apparent rate constant that limits the formation of force-bearing cross-bridge states in muscle fibers. Further, the kinetics of this transition are unaffected by disruption of near-neighbor thin filament cooperativity subsequent to extraction of TnC. Finally, the results support the idea that the steepness of the steady-state isometric tension-calcium relationship is at least in part due to mechanisms involving molecular cooperativity among thin filament regulatory proteins.

scholarly journals The Influence of Myosin Converter and Relay Domains on Cross-Bridge Kinetics of Drosophila Indirect Flight Muscle

2010 ◽  
Vol 99 (5) ◽  
pp. 1546-1555 ◽  
Author(s):  
Chaoxing Yang ◽  
Charlotte N. Kaplan ◽  
Maria L. Thatcher ◽  
Douglas M. Swank
Keyword(s):  
Flight Muscle ◽  
Indirect Flight Muscle ◽  
Cross Bridge ◽  
Kinetics Of

scholarly journals Phosphate binding induced force-reversal occurs via slow backward cycling of cross-bridges

2020 ◽  
Author(s):  
R Stehle
Keyword(s):  
Rate Constant ◽  
Force Generation ◽  
Phosphate Binding ◽  
Reversible Process ◽  
Cross Bridge ◽  
Force Relation ◽  
The Cross ◽  
Cross Bridges ◽  
Bridge Models ◽  
Kinetics Of

ABSTRACTThe release of inorganic phosphate (Pi) from the cross-bridge is a pivotal step in the cross-bridge ATPase cycle leading to force generation. It is well known that Pi release and the force-generating step are reversible, thus increase of [Pi] decreases isometric force by product inhibition and increases the rate constant kTR of mechanically-induced force redevelopment due to the reversible redistribution of cross-bridges among non-force-generating and force-generating states. The experiments on cardiac myofibrils from guinea pig presented here show that increasing [Pi] increases kTR almost reciprocally to force, i.e., kTR ≈ 1/force. To elucidate which cross-bridge models can explain the reciprocal kTR-force relation, simulations were performed for models varying in sequence and kinetics of 1) the Pi release-rebinding equilibrium, 2) the force-generating step and its reversal, and 3) the transitions limiting forward and backward cycling of cross-bridges between non-force-generating and force-generating states. Models consisting of fast reversible force generation before/after rapid Pi release-rebinding fail to describe the kTR–force relation observed in experiments. Models consistent with the experimental kTR-force relation have in common that Pi binding and/or force-reversal are/is intrinsically slow, i.e., either Pi binding or force-reversal or both limit backward cycling of cross-bridges from force-generating to non-force-generating states.STATEMENT OF SIGNIFICANCEPrevious mechanical studies on muscle fibers, myofibrils and myosin interacting with actin revealed that force production associated to phosphate release from myosin’s active site presents a reversible process in the cross-bridge cycle. The correlation of this reversible process to the process(es) limiting kinetics of backward cycling from force-generating to non-force-generating states remained unclear.Experimental data of cardiac myofibrils and model simulations show that the combined effects of [Pi] on force and the rate constant of force redevelopment (kTR) are inconsistent with fast reversible force generation before/after rapid Pi release-rebinding. The minimum requirement in sequential models for successfully describing the experimentally observed nearly reciprocal change of force and kTR is that either the Pi binding or the force-reversal step limit backward cycling.

scholarly journals Kinetics of a single cross-bridge in familial hypertrophic cardiomyopathy heart muscle measured by reverse Kretschmann fluorescence

2010 ◽  
Vol 15 (1) ◽  
pp. 017011 ◽  
Author(s):  
Prasad Mettikolla ◽  
Nils Calander ◽  
Rafal Luchowski ◽  
Ignacy Gryczynski ◽  
Zygmunt Gryczynski ◽  
...  
Keyword(s):  
Hypertrophic Cardiomyopathy ◽  
Heart Muscle ◽  
Familial Hypertrophic Cardiomyopathy ◽  
Cross Bridge ◽  
Single Cross ◽  
Kinetics Of

scholarly journals 2-Deoxyadenosine triphosphate restores the contractile function of cardiac myofibril from adult dogs with naturally occurring dilated cardiomyopathy

2016 ◽  
Vol 310 (1) ◽  
pp. H80-H91 ◽  
Author(s):  
Yuanhua Cheng ◽  
Kaley A. Hogarth ◽  
M. Lynne O'Sullivan ◽  
Michael Regnier ◽  
W. Glen Pyle
Keyword(s):  
Dilated Cardiomyopathy ◽  
Contractile Function ◽  
Systolic Function ◽  
Major Type ◽  
Slow Phase ◽  
Phase Relaxation ◽  
Cross Bridge ◽  
Naturally Occurring ◽  
Deoxyadenosine Triphosphate ◽  
Kinetics Of

Dilated cardiomyopathy (DCM) is a major type of heart failure resulting from loss of systolic function. Naturally occurring canine DCM is a widely accepted experimental paradigm for studying human DCM. 2-Deoxyadenosine triphosphate (dATP) can be used by myosin and is a superior energy substrate over ATP for cross-bridge formation and increased systolic function. The objective of this study was to evaluate the beneficial effect of dATP on contractile function of cardiac myofibrils from dogs with naturally occurring DCM. We measured actomyosin NTPase activity and contraction/relaxation properties of isolated myofibrils from nonfailing (NF) and DCM canine hearts. NTPase assays indicated replacement of ATP with dATP significantly increased myofilament activity in both NF and DCM samples. dATP significantly improved maximal tension of DCM myofibrils to the NF sample level. dATP also restored Ca2+ sensitivity of tension that was reduced in DCM samples. Similarly, dATP increased the kinetics of contractile activation (kACT), with no impact on the rate of cross-bridge tension redevelopment (kTR). Thus, the activation kinetics (kACT/kTR) that were reduced in DCM samples were restored for dATP to NF sample levels. dATP had little effect on relaxation. The rate of early slow-phase relaxation was slightly reduced with dATP, but its duration was not, nor was the fast-phase relaxation or times to 50 and 90% relaxation. Our findings suggest that myosin utilization of dATP improves cardiac myofibril contractile properties of naturally occurring DCM canine samples, restoring them to NF levels, without compromising relaxation. This suggests elevation of cardiac dATP is a promising approach for the treatment of DCM.

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