The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish

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Standard

The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish. / Berchtold, Martin Werner; Zacharias, Triantafyllos; Kulej, Katarzyna; Wang, Kevin; Torggler, Raffaela; Jespersen, Thomas; Chen, Jau Nian; Larsen, Martin R.; la Cour, Jonas Marstrand.

I: Journal of Biological Chemistry, Bind 291, Nr. 52, 2016, s. 26636-26646.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Berchtold, MW, Zacharias, T, Kulej, K, Wang, K, Torggler, R, Jespersen, T, Chen, JN, Larsen, MR & la Cour, JM 2016, 'The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish', Journal of Biological Chemistry, bind 291, nr. 52, s. 26636-26646. https://doi.org/10.1074/jbc.M116.758680

APA

Berchtold, M. W., Zacharias, T., Kulej, K., Wang, K., Torggler, R., Jespersen, T., Chen, J. N., Larsen, M. R., & la Cour, J. M. (2016). The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish. Journal of Biological Chemistry, 291(52), 26636-26646. https://doi.org/10.1074/jbc.M116.758680

Vancouver

Berchtold MW, Zacharias T, Kulej K, Wang K, Torggler R, Jespersen T o.a. The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish. Journal of Biological Chemistry. 2016;291(52):26636-26646. https://doi.org/10.1074/jbc.M116.758680

Author

Berchtold, Martin Werner ; Zacharias, Triantafyllos ; Kulej, Katarzyna ; Wang, Kevin ; Torggler, Raffaela ; Jespersen, Thomas ; Chen, Jau Nian ; Larsen, Martin R. ; la Cour, Jonas Marstrand. / The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish. I: Journal of Biological Chemistry. 2016 ; Bind 291, Nr. 52. s. 26636-26646.

Bibtex

@article{24cbd7c88dfc4cb48069039498105019,
title = "The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish",
abstract = "Calmodulin (CaM) is a Ca2+ binding protein modulating multiple targets, several of which are associated with cardiac pathophysiology. Recently, CaM mutations were linked to heart arrhythmia. CaM is crucial for cell growth and viability, yet the effect of the arrhythmogenic CaM mutations on cell viability, as well as heart rhythm, remains unknown, and only a few targets with relevance for heart physiology have been analyzed for their response to mutant CaM. We show that the arrhythmia-associated CaM mutants support growth and viability of DT40 cells in the absence of WT CaM except for the long QT syndrome mutant CaM D129G. Of the six CaM mutants tested (N53I, F89L, D95V, N97S, D129G, and F141L), three showed a decreased activation of Ca2+/CaM-dependent kinase II, most prominently the D129G CaM mutation, which was incapable of stimulating Thr286 autophosphorylation. Furthermore, the CaM D129G mutation led to bradycardia in zebrafish and an arrhythmic phenotype in a subset of the analyzed zebrafish.",
author = "Berchtold, {Martin Werner} and Triantafyllos Zacharias and Katarzyna Kulej and Kevin Wang and Raffaela Torggler and Thomas Jespersen and Chen, {Jau Nian} and Larsen, {Martin R.} and {la Cour}, {Jonas Marstrand}",
year = "2016",
doi = "10.1074/jbc.M116.758680",
language = "English",
volume = "291",
pages = "26636--26646",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "52",

}

RIS

TY - JOUR

T1 - The arrhythmogenic calmodulin mutation D129G dysregulates cell growth, calmodulin-dependent kinase II activity, and cardiac function in zebrafish

AU - Berchtold, Martin Werner

AU - Zacharias, Triantafyllos

AU - Kulej, Katarzyna

AU - Wang, Kevin

AU - Torggler, Raffaela

AU - Jespersen, Thomas

AU - Chen, Jau Nian

AU - Larsen, Martin R.

AU - la Cour, Jonas Marstrand

PY - 2016

Y1 - 2016

N2 - Calmodulin (CaM) is a Ca2+ binding protein modulating multiple targets, several of which are associated with cardiac pathophysiology. Recently, CaM mutations were linked to heart arrhythmia. CaM is crucial for cell growth and viability, yet the effect of the arrhythmogenic CaM mutations on cell viability, as well as heart rhythm, remains unknown, and only a few targets with relevance for heart physiology have been analyzed for their response to mutant CaM. We show that the arrhythmia-associated CaM mutants support growth and viability of DT40 cells in the absence of WT CaM except for the long QT syndrome mutant CaM D129G. Of the six CaM mutants tested (N53I, F89L, D95V, N97S, D129G, and F141L), three showed a decreased activation of Ca2+/CaM-dependent kinase II, most prominently the D129G CaM mutation, which was incapable of stimulating Thr286 autophosphorylation. Furthermore, the CaM D129G mutation led to bradycardia in zebrafish and an arrhythmic phenotype in a subset of the analyzed zebrafish.

AB - Calmodulin (CaM) is a Ca2+ binding protein modulating multiple targets, several of which are associated with cardiac pathophysiology. Recently, CaM mutations were linked to heart arrhythmia. CaM is crucial for cell growth and viability, yet the effect of the arrhythmogenic CaM mutations on cell viability, as well as heart rhythm, remains unknown, and only a few targets with relevance for heart physiology have been analyzed for their response to mutant CaM. We show that the arrhythmia-associated CaM mutants support growth and viability of DT40 cells in the absence of WT CaM except for the long QT syndrome mutant CaM D129G. Of the six CaM mutants tested (N53I, F89L, D95V, N97S, D129G, and F141L), three showed a decreased activation of Ca2+/CaM-dependent kinase II, most prominently the D129G CaM mutation, which was incapable of stimulating Thr286 autophosphorylation. Furthermore, the CaM D129G mutation led to bradycardia in zebrafish and an arrhythmic phenotype in a subset of the analyzed zebrafish.

U2 - 10.1074/jbc.M116.758680

DO - 10.1074/jbc.M116.758680

M3 - Journal article

C2 - 27815504

AN - SCOPUS:85007308077

VL - 291

SP - 26636

EP - 26646

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 52

ER -

ID: 171653388