The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Phosphorylation of Troponin I by Protein Kinase A Accelerates Relaxation and Crossbridge Cycle Kinetics in Mouse Ventricular Muscle
Open accessAbstract
Abstract —Phosphorylation of cardiac myofibrils by cAMP-dependent protein kinase (PKA) can increase the intrinsic rate of myofibrillar relaxation, which may contribute to the shortening of the cardiac twitch during β-adrenoceptor stimulation. However, it is not known whether the acceleration of myofibrillar relaxation is due to phosphorylation of troponin I (TnI) or of myosin binding protein-C (MyBP-C). To distinguish between these possibilities, we used transgenic mice that overexpress the nonphosphorylatable, slow skeletal isoform of TnI in the myocardium and do not express the normal, phosphorylatable cardiac TnI. The intrinsic rate of relaxation of myofibrils from wild-type and transgenic mice was measured using flash photolysis of diazo-2 to rapidly decrease the [Ca 2+ ] within skinned muscles from the mouse ventricles. Incubation with PKA nearly doubled the intrinsic rate of myofibrillar relaxation in muscles from wild-type mice (relaxation half-time fell from ≈150 to ≈90 ms at 22°C) but had no effect on the relaxation rate of muscles from the transgenic mice. In parallel studies with intact muscles, we assessed crossbridge kinetics indirectly by determining f min (the frequency for minimum dynamic stiffness) during tetanic contractions. Stimulation of β-adrenoceptors with isoproterenol increased f min from 1.9 to 3.1 Hz in muscles from wild-type mice but had no effect on f min in muscles from transgenic mice. We conclude that the acceleration of myofibrillar relaxation rate by PKA is due to phosphorylation of TnI, rather than MyBP-C, and that this may be due, at least in part, to faster crossbridge cycle kinetics.
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Cites
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Excitation-Contraction Coupling and Cardiac Contractile Force
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Self-citationCardiac Troponin I Phosphorylation Increases the Rate of Cardiac Muscle Relaxation
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Phosphorylation of C-protein, troponin I and phospholamban in isolated rabbit hearts
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Regulation of cardiac contractile function by troponin I phosphorylation
LAYLAND, J., SOLARO, R., & SHAH, A. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.12.022 · Cited by 385
Self-citationHerron, T. J., Rocha, A. M. D., Campbell, K. F., Ponce-Balbuena, D., Willis, B. C., Guerrero-Serna, G., Liu, Q., Klos, M., Musa, H., Zarzoso, M., et al. (2016) · Circulation: Arrhythmia and Electrophysiology · doi:10.1161/circep.113.003638 · Cited by 257
The sarcomeric Z-disc: a nodal point in signalling and disease
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CaMKII induces permeability transition through Drp1 phosphorylation during chronic β-AR stimulation
Xu, S., Wang, P., Zhang, H., Gong, G., Gutierrez Cortes, N., Zhu, W., Yoon, Y., Tian, R., & Wang, W. (2016) · Nature Communications · doi:10.1038/ncomms13189 · Cited by 218
Augmented Phosphorylation of Cardiac Troponin I in Hypertensive Heart Failure
Dong, X., Sumandea, C. A., Chen, Y.-C., Garcia-Cazarin, M. L., Zhang, J., Balke, C. W., Sumandea, M. P., & Ge, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.293258 · Cited by 99
Metadata
- Authors
- Kentish, J. C., McCloskey, D. T., Layland, J., Palmer, S., Leiden, J. M., Martin, A. F., & Solaro, R. J.
- Venue
- Circulation Research
- Published
- 2001-05-25
- Volume
- 88
- Issue
- 10
- Pages
- 1059-1065
- ISSN
- 0009-7330 (ISSN-L)
- 1524-4571
- OpenAlex
- W2014534876
- Cited by
- 337
- References
- 26
- FWCI
- 11.79
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Kentish, J. C., McCloskey, D. T., Layland, J., Palmer, S., Leiden, J. M., Martin, A. F., & Solaro, R. J. (2001). Phosphorylation of Troponin I by Protein Kinase A Accelerates Relaxation and Crossbridge Cycle Kinetics in Mouse Ventricular Muscle. Circulation Research. https://doi.org/10.1161/hh1001.091640
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