Quantitative analysis of myofilament protein phosphorylation in small cardiac biopsies

Ruud Zaremba; Daphne Merkus; Nazha Hamdani; Jos M.J. Lamers; Walter J. Paulus; Cris dos Remedios; Dirk J. Duncker; Ger J.M. Stienen; Jolanda van der Velden

doi:https://doi.org/10.1002/prca.200600891

Quantitative analysis of myofilament protein phosphorylation in small cardiac biopsies

Ruud Zaremba, Daphne Merkus, Nazha Hamdani, Jos M.J. Lamers, Walter J. Paulus, Cris dos Remedios, Dirk J. Duncker, Ger J.M. Stienen, Jolanda van der Velden

Physiology (VUmc)

Research output: Contribution to journal › Article › Academic › peer-review

62 Citations (Scopus)

Abstract

Phosphorylation of cardiac myofilament proteins represents one of the main post-translational mechanisms that regulate cardiac pump function. Human studies are often limited by the amount of available tissue as biopsies taken during cardiac catheterization weigh only 1 mg (dry weight). Similarly, investigation of time- (or dose-) dependent changes in protein phosphorylation in animal studies is often hampered by tissue availability. The present study describes quantitative analysis of phosphorylation status of multiple myofilament proteins by 2-DE and Pro-Q® Diamond stained gradient gels using minor amounts (-0.5 mg dry weight) of human and pig cardiac tissue.

Original language	English
Pages (from-to)	1285-1290
Number of pages	6
Journal	Proteomics - Clinical Applications
Volume	1
Issue number	10
DOIs	https://doi.org/10.1002/prca.200600891
Publication status	Published - 1 Oct 2007

Keywords

2-DE
Cardiac tissue
Pro-Q® Diamond stain
Protein phosphorylation
TCA

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abstract = "Phosphorylation of cardiac myofilament proteins represents one of the main post-translational mechanisms that regulate cardiac pump function. Human studies are often limited by the amount of available tissue as biopsies taken during cardiac catheterization weigh only 1 mg (dry weight). Similarly, investigation of time- (or dose-) dependent changes in protein phosphorylation in animal studies is often hampered by tissue availability. The present study describes quantitative analysis of phosphorylation status of multiple myofilament proteins by 2-DE and Pro-Q{\textregistered} Diamond stained gradient gels using minor amounts (-0.5 mg dry weight) of human and pig cardiac tissue.",

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AU - Zaremba, Ruud

AU - Merkus, Daphne

AU - Hamdani, Nazha

AU - Lamers, Jos M.J.

AU - Paulus, Walter J.

AU - dos Remedios, Cris

AU - Duncker, Dirk J.

AU - Stienen, Ger J.M.

AU - van der Velden, Jolanda

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AB - Phosphorylation of cardiac myofilament proteins represents one of the main post-translational mechanisms that regulate cardiac pump function. Human studies are often limited by the amount of available tissue as biopsies taken during cardiac catheterization weigh only 1 mg (dry weight). Similarly, investigation of time- (or dose-) dependent changes in protein phosphorylation in animal studies is often hampered by tissue availability. The present study describes quantitative analysis of phosphorylation status of multiple myofilament proteins by 2-DE and Pro-Q® Diamond stained gradient gels using minor amounts (-0.5 mg dry weight) of human and pig cardiac tissue.

KW - 2-DE

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Quantitative analysis of myofilament protein phosphorylation in small cardiac biopsies

Abstract

Keywords

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