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Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation.

Cardiovascular research

Vikhorev PG, Vikhoreva NN, Yeung W, Li A, Lal S, Dos Remedios CG, Blair CA, Guglin M, Campbell KS, Yacoub MH, de Tombe P, Marston SB.
PMID: 33135063
Cardiovasc Res. 2022 Jan 07;118(1):241-253. doi: 10.1093/cvr/cvaa316.

AIMS : Dilated cardiomyopathy (DCM) is associated with mutations in many genes encoding sarcomere proteins. Truncating mutations in the titin gene TTN are the most frequent. Proteomic and functional characterizations are required to elucidate the origin of the disease...

Cite
Vikhorev PG, Vikhoreva NN, Yeung W, et al. Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation. Cardiovasc Res. 2022;118(1):241-253doi: 10.1093/cvr/cvaa316.
Vikhorev, P. G., Vikhoreva, N. N., Yeung, W., Li, A., Lal, S., Dos Remedios, C. G., Blair, C. A., Guglin, M., Campbell, K. S., Yacoub, M. H., de Tombe, P., & Marston, S. B. (2022). Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation. Cardiovascular research, 118(1), 241-253. https://doi.org/10.1093/cvr/cvaa316
Vikhorev, Petr G, et al. "Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation." Cardiovascular research vol. 118,1 (2022): 241-253. doi: https://doi.org/10.1093/cvr/cvaa316
Vikhorev PG, Vikhoreva NN, Yeung W, Li A, Lal S, Dos Remedios CG, Blair CA, Guglin M, Campbell KS, Yacoub MH, de Tombe P, Marston SB. Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation. Cardiovasc Res. 2022 Jan 07;118(1):241-253. doi: 10.1093/cvr/cvaa316. PMID: 33135063.
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Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I.

Frontiers in physiology

Siddiqui JK, Tikunova SB, Walton SD, Liu B, Meyer M, de Tombe PP, Neilson N, Kekenes-Huskey PM, Salhi HE, Janssen PM, Biesiadecki BJ, Davis JP.
PMID: 28066265
Front Physiol. 2016 Dec 21;7:632. doi: 10.3389/fphys.2016.00632. eCollection 2016.

Control of calcium binding to and dissociation from cardiac troponin C (TnC) is essential to healthy cardiac muscle contraction/relaxation. There are numerous aberrant post-translational modifications and mutations within a plethora of contractile, and even non-contractile, proteins that appear to...

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Siddiqui JK, Tikunova SB, Walton SD, et al. Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I. Front Physiol. 2016;7:632doi: 10.3389/fphys.2016.00632.
Siddiqui, J. K., Tikunova, S. B., Walton, S. D., Liu, B., Meyer, M., de Tombe, P. P., Neilson, N., Kekenes-Huskey, P. M., Salhi, H. E., Janssen, P. M., Biesiadecki, B. J., & Davis, J. P. (2016). Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I. Frontiers in physiology, 7632. https://doi.org/10.3389/fphys.2016.00632
Siddiqui, Jalal K, et al. "Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I." Frontiers in physiology vol. 7 (2016): 632. doi: https://doi.org/10.3389/fphys.2016.00632
Siddiqui JK, Tikunova SB, Walton SD, Liu B, Meyer M, de Tombe PP, Neilson N, Kekenes-Huskey PM, Salhi HE, Janssen PM, Biesiadecki BJ, Davis JP. Myofilament Calcium Sensitivity: Consequences of the Effective Concentration of Troponin I. Front Physiol. 2016 Dec 21;7:632. doi: 10.3389/fphys.2016.00632. eCollection 2016. PMID: 28066265; PMCID: PMC5175494.
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Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway.

Scientific reports

Lertwanakarn T, Suntravat M, Sánchez EE, Wolska BM, Solaro RJ, de Tombe PP, Tachampa K.
PMID: 34707114
Sci Rep. 2021 Oct 27;11(1):21154. doi: 10.1038/s41598-021-00282-x.

Beta-cardiotoxin (β-CTX) from the king cobra venom (Ophiophagus hannah) was previously proposed as a novel β-adrenergic blocker. However, the involvement of β-adrenergic signaling by this compound has never been elucidated. The objectives of this study were to investigate the...

Cite
Lertwanakarn T, Suntravat M, Sánchez EE, et al. Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway. Sci Rep. 2021;11(1):21154doi: 10.1038/s41598-021-00282-x.
Lertwanakarn, T., Suntravat, M., Sánchez, E. E., Wolska, B. M., Solaro, R. J., de Tombe, P. P., & Tachampa, K. (2021). Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway. Scientific reports, 11(1), 21154. https://doi.org/10.1038/s41598-021-00282-x
Lertwanakarn, Tuchakorn, et al. "Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway." Scientific reports vol. 11,1 (2021): 21154. doi: https://doi.org/10.1038/s41598-021-00282-x
Lertwanakarn T, Suntravat M, Sánchez EE, Wolska BM, Solaro RJ, de Tombe PP, Tachampa K. Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway. Sci Rep. 2021 Oct 27;11(1):21154. doi: 10.1038/s41598-021-00282-x. PMID: 34707114; PMCID: PMC8551325.
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Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation.

Cardiovascular research

Vikhorev PG, Vikhoreva NN, Yeung W, Li A, Lal S, Dos Remedios CG, Blair CA, Guglin M, Campbell KS, Yacoub MH, de Tombe P, Marston SB.
PMID: 33135063
Cardiovasc Res. 2022 Jan 07;118(1):241-253. doi: 10.1093/cvr/cvaa316.

AIMS : Dilated cardiomyopathy (DCM) is associated with mutations in many genes encoding sarcomere proteins. Truncating mutations in the titin gene TTN are the most frequent. Proteomic and functional characterizations are required to elucidate the origin of the disease...

Cite
Vikhorev PG, Vikhoreva NN, Yeung W, et al. Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation. Cardiovasc Res. 2022;118(1):241-253doi: 10.1093/cvr/cvaa316.
Vikhorev, P. G., Vikhoreva, N. N., Yeung, W., Li, A., Lal, S., Dos Remedios, C. G., Blair, C. A., Guglin, M., Campbell, K. S., Yacoub, M. H., de Tombe, P., & Marston, S. B. (2022). Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation. Cardiovascular research, 118(1), 241-253. https://doi.org/10.1093/cvr/cvaa316
Vikhorev, Petr G, et al. "Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation." Cardiovascular research vol. 118,1 (2022): 241-253. doi: https://doi.org/10.1093/cvr/cvaa316
Vikhorev PG, Vikhoreva NN, Yeung W, Li A, Lal S, Dos Remedios CG, Blair CA, Guglin M, Campbell KS, Yacoub MH, de Tombe P, Marston SB. Titin-truncating mutations associated with dilated cardiomyopathy alter length-dependent activation and its modulation via phosphorylation. Cardiovasc Res. 2022 Jan 07;118(1):241-253. doi: 10.1093/cvr/cvaa316. PMID: 33135063; PMCID: PMC8752363.
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Cardiac myosin binding protein-C: redefining its structure and function.

Biophysical reviews

Sadayappan S, de Tombe PP.
PMID: 22707987
Biophys Rev. 2012 Jun 01;4(2):93-106. doi: 10.1007/s12551-012-0067-x.

Mutations of cardiac myosin binding protein-C (cMyBP-C) are inherited by an estimated 60 million people worldwide, and the protein is the target of several kinases. Recent evidence further suggests that cMyBP-C mutations alter Ca(2+) transients, leading to electrophysiological dysfunction....

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Sadayappan S, de Tombe PP. Cardiac myosin binding protein-C: redefining its structure and function. Biophys Rev. 2012;4(2):93-106doi: 10.1007/s12551-012-0067-x.
Sadayappan, S., & de Tombe, P. P. (2012). Cardiac myosin binding protein-C: redefining its structure and function. Biophysical reviews, 4(2), 93-106. https://doi.org/10.1007/s12551-012-0067-x
Sadayappan, Sakthivel, and de Tombe, Pieter P. "Cardiac myosin binding protein-C: redefining its structure and function." Biophysical reviews vol. 4,2 (2012): 93-106. doi: https://doi.org/10.1007/s12551-012-0067-x
Sadayappan S, de Tombe PP. Cardiac myosin binding protein-C: redefining its structure and function. Biophys Rev. 2012 Jun 01;4(2):93-106. doi: 10.1007/s12551-012-0067-x. PMID: 22707987; PMCID: PMC3374655.
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Suppression of cardiomyocyte functions by β-CTX isolated from the Thai king cobra (.

The journal of venomous animals and toxins including tropical diseases

Lertwanakarn T, Suntravat M, Sanchez EE, Boonhoh W, Solaro RJ, Wolska BM, Martin JL, de Tombe PP, Tachampa K.
PMID: 32742278
J Venom Anim Toxins Incl Trop Dis. 2020 Jul 17;26:e20200005. doi: 10.1590/1678-9199-JVATITD-2020-0005. eCollection 2020.

BACKGROUND: Beta-cardiotoxin (β-CTX), the three-finger toxin isolated from king cobra (METHODS: β-CTX was isolated from the crude venom of the Thai king cobra using reverse-phased and cation exchange HPLC. RESULTS: Purified β-CTX was recovered from crude venom (0.53% w/w)....

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Lertwanakarn T, Suntravat M, Sanchez EE, et al. Suppression of cardiomyocyte functions by β-CTX isolated from the Thai king cobra (. J Venom Anim Toxins Incl Trop Dis. 2020;26:e20200005doi: 10.1590/1678-9199-JVATITD-2020-0005.
Lertwanakarn, T., Suntravat, M., Sanchez, E. E., Boonhoh, W., Solaro, R. J., Wolska, B. M., Martin, J. L., de Tombe, P. P., & Tachampa, K. (2020). Suppression of cardiomyocyte functions by β-CTX isolated from the Thai king cobra (. The journal of venomous animals and toxins including tropical diseases, 26e20200005. https://doi.org/10.1590/1678-9199-JVATITD-2020-0005
Lertwanakarn, Tuchakorn, et al. "Suppression of cardiomyocyte functions by β-CTX isolated from the Thai king cobra (." The journal of venomous animals and toxins including tropical diseases vol. 26 (2020): e20200005. doi: https://doi.org/10.1590/1678-9199-JVATITD-2020-0005
Lertwanakarn T, Suntravat M, Sanchez EE, Boonhoh W, Solaro RJ, Wolska BM, Martin JL, de Tombe PP, Tachampa K. Suppression of cardiomyocyte functions by β-CTX isolated from the Thai king cobra (. J Venom Anim Toxins Incl Trop Dis. 2020 Jul 17;26:e20200005. doi: 10.1590/1678-9199-JVATITD-2020-0005. eCollection 2020. PMID: 32742278; PMCID: PMC7375408.
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Which way to grow? Force over time may be the heart's .

Global cardiology science & practice

de Tombe PP, Kohl P.
PMID: 29043268
Glob Cardiol Sci Pract. 2016 Jun 30;2016(2):e201621. doi: 10.21542/gcsp.2016.21.

No abstract available.

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de Tombe PP, Kohl P. Which way to grow? Force over time may be the heart's . Glob Cardiol Sci Pract. 2016;2016(2):e201621doi: 10.21542/gcsp.2016.21.
de Tombe, P. P., & Kohl, P. (2016). Which way to grow? Force over time may be the heart's . Global cardiology science & practice, 2016(2), e201621. https://doi.org/10.21542/gcsp.2016.21
de Tombe, Pieter P, and Kohl, Peter. "Which way to grow? Force over time may be the heart's ." Global cardiology science & practice vol. 2016,2 (2016): e201621. doi: https://doi.org/10.21542/gcsp.2016.21
de Tombe PP, Kohl P. Which way to grow? Force over time may be the heart's . Glob Cardiol Sci Pract. 2016 Jun 30;2016(2):e201621. doi: 10.21542/gcsp.2016.21. PMID: 29043268; PMCID: PMC5642831.
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Exploring cardiac biophysical properties.

Global cardiology science & practice

Ait Mou Y, Bollensdorff C, Cazorla O, Magdi Y, de Tombe PP.
PMID: 26779498
Glob Cardiol Sci Pract. 2015 Apr 10;2015:10. doi: 10.5339/gcsp.2015.10. eCollection 2015.

The heart is subject to multiple sources of stress. To maintain its normal function, and successfully overcome these stresses, heart muscle is equipped with fine-tuned regulatory mechanisms. Some of these mechanisms are inherent within the myocardium itself and are...

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Ait Mou Y, Bollensdorff C, Cazorla O, et al. Exploring cardiac biophysical properties. Glob Cardiol Sci Pract. 2015;2015:10doi: 10.5339/gcsp.2015.10.
Ait Mou, Y., Bollensdorff, C., Cazorla, O., Magdi, Y., & de Tombe, P. P. (2015). Exploring cardiac biophysical properties. Global cardiology science & practice, 201510. https://doi.org/10.5339/gcsp.2015.10
Ait Mou, Younss, et al. "Exploring cardiac biophysical properties." Global cardiology science & practice vol. 2015 (2015): 10. doi: https://doi.org/10.5339/gcsp.2015.10
Ait Mou Y, Bollensdorff C, Cazorla O, Magdi Y, de Tombe PP. Exploring cardiac biophysical properties. Glob Cardiol Sci Pract. 2015 Apr 10;2015:10. doi: 10.5339/gcsp.2015.10. eCollection 2015. PMID: 26779498; PMCID: PMC4448074.
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Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway.

Scientific reports

Lertwanakarn T, Suntravat M, Sánchez EE, Wolska BM, Solaro RJ, de Tombe PP, Tachampa K.
PMID: 34707114
Sci Rep. 2021 Oct 27;11(1):21154. doi: 10.1038/s41598-021-00282-x.

Beta-cardiotoxin (β-CTX) from the king cobra venom (Ophiophagus hannah) was previously proposed as a novel β-adrenergic blocker. However, the involvement of β-adrenergic signaling by this compound has never been elucidated. The objectives of this study were to investigate the...

Cite
Lertwanakarn T, Suntravat M, Sánchez EE, et al. Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway. Sci Rep. 2021;11(1):21154doi: 10.1038/s41598-021-00282-x.
Lertwanakarn, T., Suntravat, M., Sánchez, E. E., Wolska, B. M., Solaro, R. J., de Tombe, P. P., & Tachampa, K. (2021). Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway. Scientific reports, 11(1), 21154. https://doi.org/10.1038/s41598-021-00282-x
Lertwanakarn, Tuchakorn, et al. "Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway." Scientific reports vol. 11,1 (2021): 21154. doi: https://doi.org/10.1038/s41598-021-00282-x
Lertwanakarn T, Suntravat M, Sánchez EE, Wolska BM, Solaro RJ, de Tombe PP, Tachampa K. Negative inotropic mechanisms of β-cardiotoxin in cardiomyocytes by depression of myofilament ATPase activity without activation of the classical β-adrenergic pathway. Sci Rep. 2021 Oct 27;11(1):21154. doi: 10.1038/s41598-021-00282-x. PMID: 34707114; PMCID: PMC8551325.
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Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation.

Cardiovascular research

Vikhorev PG, Vikhoreva NN, Yeung W, Li A, Lal S, Dos Remedios CG, Blair CA, Guglin M, Campbell KS, Yacoub MH, de Tombe P, Marston SB.
PMID: 33135063
Cardiovasc Res. 2020 Nov 02; doi: 10.1093/cvr/cvaa316. Epub 2020 Nov 02.

AIMS: Dilated cardiomyopathy (DCM) is associated with mutations in many genes encoding sarcomere proteins. Truncating mutations in the titin gene TTN are the most frequent. Proteomic and functional characterisations are required to elucidate the origin of the disease and...

Cite
Vikhorev PG, Vikhoreva NN, Yeung W, et al. Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation. Cardiovasc Res. 2020;doi: 10.1093/cvr/cvaa316.
Vikhorev, P. G., Vikhoreva, N. N., Yeung, W., Li, A., Lal, S., Dos Remedios, C. G., Blair, C. A., Guglin, M., Campbell, K. S., Yacoub, M. H., de Tombe, P., & Marston, S. B. (2020). Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation. Cardiovascular research, . https://doi.org/10.1093/cvr/cvaa316
Vikhorev, Petr G, et al. "Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation." Cardiovascular research vol. (2020). doi: https://doi.org/10.1093/cvr/cvaa316
Vikhorev PG, Vikhoreva NN, Yeung W, Li A, Lal S, Dos Remedios CG, Blair CA, Guglin M, Campbell KS, Yacoub MH, de Tombe P, Marston SB. Titin-Truncating Mutations Associated With Dilated Cardiomyopathy Alter Length-Dependent Activation And Its Modulation Via Phosphorylation. Cardiovasc Res. 2020 Nov 02; doi: 10.1093/cvr/cvaa316. Epub 2020 Nov 02. PMID: 33135063.
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Amino terminus of cardiac myosin binding protein-C regulates cardiac contractility.

Journal of molecular and cellular cardiology

Lynch TL, Kumar M, McNamara JW, Kuster DWD, Sivaguru M, Singh RR, Previs MJ, Lee KH, Kuffel G, Zilliox MJ, Lin BL, Ma W, Gibson AM, Blaxall BC, Nieman ML, Lorenz JN, Leichter DM, Leary OP, Janssen PML, de Tombe PP, Gilbert RJ, Craig R, Irving T, Warshaw DM, Sadayappan S.
PMID: 33781820
J Mol Cell Cardiol. 2021 Jul;156:33-44. doi: 10.1016/j.yjmcc.2021.03.009. Epub 2021 Mar 26.

Phosphorylation of cardiac myosin binding protein-C (cMyBP-C) regulates cardiac contraction through modulation of actomyosin interactions mediated by the protein's amino terminal (N')-region (C0-C2 domains, 358 amino acids). On the other hand, dephosphorylation of cMyBP-C during myocardial injury results in...

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Lynch TL, Kumar M, McNamara JW, et al. Amino terminus of cardiac myosin binding protein-C regulates cardiac contractility. J Mol Cell Cardiol. 2021;156:33-44doi: 10.1016/j.yjmcc.2021.03.009.
Lynch, T. L., Kumar, M., McNamara, J. W., Kuster, D. W. D., Sivaguru, M., Singh, R. R., Previs, M. J., Lee, K. H., Kuffel, G., Zilliox, M. J., Lin, B. L., Ma, W., Gibson, A. M., Blaxall, B. C., Nieman, M. L., Lorenz, J. N., Leichter, D. M., Leary, O. P., Janssen, P. M. L., de Tombe, P. P., Gilbert, R. J., Craig, R., Irving, T., Warshaw, D. M., & Sadayappan, S. (2021). Amino terminus of cardiac myosin binding protein-C regulates cardiac contractility. Journal of molecular and cellular cardiology, 15633-44. https://doi.org/10.1016/j.yjmcc.2021.03.009
Lynch, Thomas L, et al. "Amino terminus of cardiac myosin binding protein-C regulates cardiac contractility." Journal of molecular and cellular cardiology vol. 156 (2021): 33-44. doi: https://doi.org/10.1016/j.yjmcc.2021.03.009
Lynch TL, Kumar M, McNamara JW, Kuster DWD, Sivaguru M, Singh RR, Previs MJ, Lee KH, Kuffel G, Zilliox MJ, Lin BL, Ma W, Gibson AM, Blaxall BC, Nieman ML, Lorenz JN, Leichter DM, Leary OP, Janssen PML, de Tombe PP, Gilbert RJ, Craig R, Irving T, Warshaw DM, Sadayappan S. Amino terminus of cardiac myosin binding protein-C regulates cardiac contractility. J Mol Cell Cardiol. 2021 Jul;156:33-44. doi: 10.1016/j.yjmcc.2021.03.009. Epub 2021 Mar 26. PMID: 33781820; PMCID: PMC8217138.
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Remodelling of adult cardiac tissue subjected to physiological and pathological mechanical load in vitro.

Cardiovascular research

Pitoulis FG, Nunez-Toldra R, Xiao K, Kit-Anan W, Mitzka S, Jabbour RJ, Harding SE, Perbellini F, Thum T, de Tombe PP, Terracciano CM.
PMID: 33723566
Cardiovasc Res. 2021 Mar 16; doi: 10.1093/cvr/cvab084. Epub 2021 Mar 16.

AIMS: Cardiac remodelling is the process by which the heart adapts to its environment. Mechanical load is a major driver of remodelling. Cardiac tissue culture has been frequently employed for in vitro studies of load-induced remodelling; however, current in...

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Pitoulis FG, Nunez-Toldra R, Xiao K, et al. Remodelling of adult cardiac tissue subjected to physiological and pathological mechanical load in vitro. Cardiovasc Res. 2021;doi: 10.1093/cvr/cvab084.
Pitoulis, F. G., Nunez-Toldra, R., Xiao, K., Kit-Anan, W., Mitzka, S., Jabbour, R. J., Harding, S. E., Perbellini, F., Thum, T., de Tombe, P. P., & Terracciano, C. M. (2021). Remodelling of adult cardiac tissue subjected to physiological and pathological mechanical load in vitro. Cardiovascular research, . https://doi.org/10.1093/cvr/cvab084
Pitoulis, Fotios G, et al. "Remodelling of adult cardiac tissue subjected to physiological and pathological mechanical load in vitro." Cardiovascular research vol. (2021). doi: https://doi.org/10.1093/cvr/cvab084
Pitoulis FG, Nunez-Toldra R, Xiao K, Kit-Anan W, Mitzka S, Jabbour RJ, Harding SE, Perbellini F, Thum T, de Tombe PP, Terracciano CM. Remodelling of adult cardiac tissue subjected to physiological and pathological mechanical load in vitro. Cardiovasc Res. 2021 Mar 16; doi: 10.1093/cvr/cvab084. Epub 2021 Mar 16. PMID: 33723566.
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