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S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure

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S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure. / Stathopoulou, Konstantina; Wittig, Ilka; Heidler, Juliana; Piasecki, Angelika; Richter, Florian; Diering, Simon; van der Velden, Jolanda; Buck, Friedrich; Donzelli, Sonia; Schröder, Ewald; Wijnker, Paul J M; Voigt, Niels; Dobrev, Dobromir; Sadayappan, Sakthivel; Eschenhagen, Thomas; Carrier, Lucie; Eaton, Philip; Cuello, Friederike.

in: FASEB J, Jahrgang 30, Nr. 5, 05.2016, S. 1849-64.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Stathopoulou, K, Wittig, I, Heidler, J, Piasecki, A, Richter, F, Diering, S, van der Velden, J, Buck, F, Donzelli, S, Schröder, E, Wijnker, PJM, Voigt, N, Dobrev, D, Sadayappan, S, Eschenhagen, T, Carrier, L, Eaton, P & Cuello, F 2016, 'S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure', FASEB J, Jg. 30, Nr. 5, S. 1849-64. https://doi.org/10.1096/fj.201500048

APA

Stathopoulou, K., Wittig, I., Heidler, J., Piasecki, A., Richter, F., Diering, S., van der Velden, J., Buck, F., Donzelli, S., Schröder, E., Wijnker, P. J. M., Voigt, N., Dobrev, D., Sadayappan, S., Eschenhagen, T., Carrier, L., Eaton, P., & Cuello, F. (2016). S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure. FASEB J, 30(5), 1849-64. https://doi.org/10.1096/fj.201500048

Vancouver

Stathopoulou K, Wittig I, Heidler J, Piasecki A, Richter F, Diering S et al. S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure. FASEB J. 2016 Mai;30(5):1849-64. https://doi.org/10.1096/fj.201500048

Bibtex

@article{07c6a6b8a4bb437aac5bf4c262cb7479,
title = "S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure",
abstract = "Cardiac myosin-binding protein C (cMyBP-C) regulates actin-myosin interaction and thereby cardiac myocyte contraction and relaxation. This physiologic function is regulated by cMyBP-C phosphorylation. In our study, reduced site-specific cMyBP-C phosphorylation coincided with increased S-glutathiolation in ventricular tissue from patients with dilated or ischemic cardiomyopathy compared to nonfailing donors. We used redox proteomics, to identify constitutive and disease-specific S-glutathiolation sites in cMyBP-C in donor and patient samples, respectively. Among those, a cysteine cluster in the vicinity of the regulatory phosphorylation sites within the myosin S2 interaction domain C1-M-C2 was identified and showed enhanced S-glutathiolation in patients. In vitro S-glutathiolation of recombinant cMyBP-C C1-M-C2 occurred predominantly at Cys(249), which attenuated phosphorylation by protein kinases. Exposure to glutathione disulfide induced cMyBP-C S-glutathiolation, which functionally decelerated the kinetics of Ca(2+)-activated force development in ventricular myocytes from wild-type, but not those from Mybpc3-targeted knockout mice. These oxidation events abrogate protein kinase-mediated phosphorylation of cMyBP-C and therefore potentially contribute to the reduction of its phosphorylation and the contractile dysfunction observed in human heart failure.-Stathopoulou K., Wittig, I., Heidler, J., Piasecki, A., Richter, F. Diering, S., van der Velden, J., Buck, F., Donzelli, S., Schr{\"o}der, E., Wijnker, P. J. M., Voigt, N., Dobrev, D., Sadayappan, S., Eschenhagen, T., Carrier, L., Eaton, P., Cuello, F. S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.",
author = "Konstantina Stathopoulou and Ilka Wittig and Juliana Heidler and Angelika Piasecki and Florian Richter and Simon Diering and {van der Velden}, Jolanda and Friedrich Buck and Sonia Donzelli and Ewald Schr{\"o}der and Wijnker, {Paul J M} and Niels Voigt and Dobromir Dobrev and Sakthivel Sadayappan and Thomas Eschenhagen and Lucie Carrier and Philip Eaton and Friederike Cuello",
note = "{\textcopyright} FASEB.",
year = "2016",
month = may,
doi = "10.1096/fj.201500048",
language = "English",
volume = "30",
pages = "1849--64",
journal = "FASEB J",
issn = "0892-6638",
publisher = "FASEB",
number = "5",

}

RIS

TY - JOUR

T1 - S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure

AU - Stathopoulou, Konstantina

AU - Wittig, Ilka

AU - Heidler, Juliana

AU - Piasecki, Angelika

AU - Richter, Florian

AU - Diering, Simon

AU - van der Velden, Jolanda

AU - Buck, Friedrich

AU - Donzelli, Sonia

AU - Schröder, Ewald

AU - Wijnker, Paul J M

AU - Voigt, Niels

AU - Dobrev, Dobromir

AU - Sadayappan, Sakthivel

AU - Eschenhagen, Thomas

AU - Carrier, Lucie

AU - Eaton, Philip

AU - Cuello, Friederike

N1 - © FASEB.

PY - 2016/5

Y1 - 2016/5

N2 - Cardiac myosin-binding protein C (cMyBP-C) regulates actin-myosin interaction and thereby cardiac myocyte contraction and relaxation. This physiologic function is regulated by cMyBP-C phosphorylation. In our study, reduced site-specific cMyBP-C phosphorylation coincided with increased S-glutathiolation in ventricular tissue from patients with dilated or ischemic cardiomyopathy compared to nonfailing donors. We used redox proteomics, to identify constitutive and disease-specific S-glutathiolation sites in cMyBP-C in donor and patient samples, respectively. Among those, a cysteine cluster in the vicinity of the regulatory phosphorylation sites within the myosin S2 interaction domain C1-M-C2 was identified and showed enhanced S-glutathiolation in patients. In vitro S-glutathiolation of recombinant cMyBP-C C1-M-C2 occurred predominantly at Cys(249), which attenuated phosphorylation by protein kinases. Exposure to glutathione disulfide induced cMyBP-C S-glutathiolation, which functionally decelerated the kinetics of Ca(2+)-activated force development in ventricular myocytes from wild-type, but not those from Mybpc3-targeted knockout mice. These oxidation events abrogate protein kinase-mediated phosphorylation of cMyBP-C and therefore potentially contribute to the reduction of its phosphorylation and the contractile dysfunction observed in human heart failure.-Stathopoulou K., Wittig, I., Heidler, J., Piasecki, A., Richter, F. Diering, S., van der Velden, J., Buck, F., Donzelli, S., Schröder, E., Wijnker, P. J. M., Voigt, N., Dobrev, D., Sadayappan, S., Eschenhagen, T., Carrier, L., Eaton, P., Cuello, F. S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.

AB - Cardiac myosin-binding protein C (cMyBP-C) regulates actin-myosin interaction and thereby cardiac myocyte contraction and relaxation. This physiologic function is regulated by cMyBP-C phosphorylation. In our study, reduced site-specific cMyBP-C phosphorylation coincided with increased S-glutathiolation in ventricular tissue from patients with dilated or ischemic cardiomyopathy compared to nonfailing donors. We used redox proteomics, to identify constitutive and disease-specific S-glutathiolation sites in cMyBP-C in donor and patient samples, respectively. Among those, a cysteine cluster in the vicinity of the regulatory phosphorylation sites within the myosin S2 interaction domain C1-M-C2 was identified and showed enhanced S-glutathiolation in patients. In vitro S-glutathiolation of recombinant cMyBP-C C1-M-C2 occurred predominantly at Cys(249), which attenuated phosphorylation by protein kinases. Exposure to glutathione disulfide induced cMyBP-C S-glutathiolation, which functionally decelerated the kinetics of Ca(2+)-activated force development in ventricular myocytes from wild-type, but not those from Mybpc3-targeted knockout mice. These oxidation events abrogate protein kinase-mediated phosphorylation of cMyBP-C and therefore potentially contribute to the reduction of its phosphorylation and the contractile dysfunction observed in human heart failure.-Stathopoulou K., Wittig, I., Heidler, J., Piasecki, A., Richter, F. Diering, S., van der Velden, J., Buck, F., Donzelli, S., Schröder, E., Wijnker, P. J. M., Voigt, N., Dobrev, D., Sadayappan, S., Eschenhagen, T., Carrier, L., Eaton, P., Cuello, F. S-glutathiolation impairs phosphoregulation and function of cardiac myosin-binding protein C in human heart failure.

U2 - 10.1096/fj.201500048

DO - 10.1096/fj.201500048

M3 - SCORING: Journal article

C2 - 26839380

VL - 30

SP - 1849

EP - 1864

JO - FASEB J

JF - FASEB J

SN - 0892-6638

IS - 5

ER -