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1.
FIGURE 6.

FIGURE 6. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

A, FV relationships of trabeculae that have undergone exchange with rRLC species that are hyperphosphorylated (n = 8), have control phosphorylation similar to native RLC phosphorylation (n = 6), and are dephosphorylated (n = 5). B, calculated PV relationships of trabeculae that have undergone exchange with the three species of rRLC phosphorylation. All data are plotted as mean ± S.E. (error bars). ML/s, muscle lengths/s.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.
2.
FIGURE 7.

FIGURE 7. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

Parameters from hyperbolic fits of FV and PV relationships plotted as mean ± S.E. (error bars) by RLC phosphorylation magnitude normalized to control phosphorylation. All parameters that had significant differences between phosphorylation statuses were plotted: power (A), velocity at peak power (B), and peak unloaded shortening velocity (Vmax) (C). All data sets were described with a linear fit.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.
3.
FIGURE 3.

FIGURE 3. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

A, bar plot indicating the phosphorylation level of differently phosphorylated rat rRLC species generated by incubation with kinases (Enriched), shrimp alkaline phosphatase (Reduced), or a mixture of the two mimicking native RLC phosphorylation levels (Control). Native trabecular phosphorylation level is displayed for comparison (Native). All data are plotted as mean ± S.E. (error bars), and n values are given for each preparation. B, representative Western blots of differently phosphorylated rRLC species. Arrow, direction of blot. 2P, 1P, and 0P, number of RLC sites phosphorylated.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.
4.
FIGURE 4.

FIGURE 4. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

A, confocal image of a permeabilized cardiac trabeculum after exchange with a recombinant fluorescently labeled rRLC. B, fluorescent intensity across sarcomeres measured before and after a secondary exchange with an unlabeled recombinant RLC. C, exchange efficiency calculated from integrating fluorescent intensity before and after secondary exchange. Data presented are an average ± S.E. of n = 3 separate exchange procedures on permeabilized trabeculae. D, calculated RLC phosphorylation changes after trabeculae have undergone exchange with differently phosphorylated rRLC species. Control, the native left ventricular phosphorylation level of RLC (n = 12). Control Exchange, the calculated phosphorylation level of trabeculae that have undergone exchange with rRLC that is similarly phosphorylated to native RLC. Enriched RLC Phos, the RLC phosphorylation after exchange with enriched rRLC species. Depleted RLC Phos, the effect on trabecular phosphorylation after exchange with dephosphorylated rRLC species. Error bars are calculated from S.E. values of exchange efficiencies.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.
5.
FIGURE 5.

FIGURE 5. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

A, FV relationships of untreated trabeculae (n = 8) compared with trabeculae that have undergone control exchange (n = 6) with rRLC species of similar to native levels of RLC phosphorylation. Force was measured during the plateau phase for the individual fixed shortening velocity. Relations are fit with Hill's hyperbolic equation. All points are means of force produced during shortening ± S.E. (error bars). B, PV relations calculated from FV relations of untreated trabeculae (n = 8) compared with control exchange (n = 6). All data are presented as power ± S.E. This fitting procedure fits the relationship between force during shortening and shortening velocity in muscle lengths (ML)/s. Microsoft Excel solver was used to minimize the sum of the squared error between observed and expected values of force. The Vmax measurements obtained by the slack test method constrain the fitting procedure.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.
6.
FIGURE 2.

FIGURE 2. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

Top, SDS-PAGE Phos-tagTM analysis of cRLC phosphorylation level in mol of phosphate/mol of cRLC. cRLC phosphorylation was measured in left ventricular tissue from porcine, human, and rat samples. Samples from human left ventricular tissue taken from patients were categorized as moderate (NYHA I or II (n = 5)) or severe heart failure (NYHA III or IV (n = 5)) or normal donor (Human Non-failing LV, n = 5). Normal rat left ventricular tissue (Healthy Rat LV, n = 12) was compared with rat LV 4 weeks post-chronic MI (Rat post-MI LVH, n = 5) and 20 weeks post-chronic MI (Rat post-MI HF, n = 4). All data are displayed as mean ± S.E. (error bars). *, significance of p < 0.05 compared with control. Bottom, representative Western blots showing the ratio of phosphorylation and the amount of phosphorylation sites in each organism. Arrow, direction of blot. 2P, 1P, and 0P, the number of RLC sites phosphorylated for each band.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.
7.
FIGURE 1.

FIGURE 1. From: Myosin Regulatory Light Chain (RLC) Phosphorylation Change as a Modulator of Cardiac Muscle Contraction in Disease.

A, representative tension trace during a temperature jump activation between 0.5 and 20 °C of a permeabilized trabeculum. Force rises to a isometric plateau. 3 s after the temperature jump, the muscle is rapidly released and shortened at a fixed velocity for 50 ms, and then force recovers at the shortened sarcomere length. Muscle is then restretched to the original length and relaxed in a low calcium solution at 4 s. B, tension traces during two slack test (ST) measurements encompassing a 10% rapid release (black trace) and 12% rapid release (red trace). Time zero (T = 0) is reset to mark the time of the onset of the release. The time taken for tension to deviate from zero “slack force” (F = 0) in each slack length test is used to calculate peak unloaded shortening velocity (Vmax). Shown are tension traces during a range of fixed velocities (C) and the corresponding motor traces showing the release lengths and ramp velocities of each maneuver (D). kN, kilonewtons. ML, muscle lengths.

Christopher Toepfer, et al. J Biol Chem. 2013 May 10;288(19):13446-13454.

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