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Quantitative analysis of myofilament protein phosphorylation in small cardiac biopsies
Author(s) -
Zaremba Ruud,
Merkus Daphne,
Hamdani Nazha,
Lamers Jos M. J.,
Paulus Walter J.,
dos Remedios Cris,
Duncker Dirk J.,
Stienen Ger J. M.,
van der Velden Jolanda
Publication year - 2007
Publication title -
proteomics – clinical applications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.948
H-Index - 54
eISSN - 1862-8354
pISSN - 1862-8346
DOI - 10.1002/prca.200600891
Subject(s) - myofilament , phosphorylation , protein phosphorylation , cardiac muscle , cardiac function curve , biology , microbiology and biotechnology , chemistry , medicine , anatomy , actin , protein kinase a , heart failure
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.