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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2004-4-19
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pubmed:abstractText |
The phosphorylation of the cardiac muscle isoform of the sarcoplasmic reticulum (SR) Ca(2+)-ATPase (SERCA2a) on serine 38 has been described as a regulatory event capable of very significant enhancement of enzyme activity (Hawkins, C., Xu, A., and Narayanan, N. (1994) J. Biol. Chem. 269, 31198-31206). Independent confirmation of these observations has not been forthcoming. This study has utilized a polyclonal antibody specific for the phosphorylated serine 38 epitope on the Ca(2+)-ATPase to evaluate the phosphorylation of SERCA2a in isolated sarcoplasmic reticulum vesicles and isolated rat ventricular myocytes. A quantitative Western blot approach failed to detect serine 38-phosphorylated Ca(2+)-ATPase in either kinase-treated sarcoplasmic reticulum vesicles or suitably stimulated cardiac myocytes. Calibration standards confirmed that the detection sensitivity of assays was adequate to detect Ser-38 phosphorylation if it occurred on at least 1% of Ca(2+)-ATPase molecules in SR vesicle experiments or on at least 0.1% of Ca(2+)-ATPase molecules in cardiac myocytes. The failure to detect a phosphorylated form of the Ca(2+)-ATPase in either preparation (isolated myocyte, purified sarcoplasmic reticulum vesicles) suggests that Ser-38 phosphorylation of the Ca(2+)-ATPase is not a significant regulatory feature of cardiac Ca(2+) homeostasis.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
17111-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:14766745-Amino Acid Sequence,
pubmed-meshheading:14766745-Animals,
pubmed-meshheading:14766745-Blotting, Western,
pubmed-meshheading:14766745-Calcium-Transporting ATPases,
pubmed-meshheading:14766745-Calibration,
pubmed-meshheading:14766745-Cell Membrane,
pubmed-meshheading:14766745-Cells, Cultured,
pubmed-meshheading:14766745-Dogs,
pubmed-meshheading:14766745-Dose-Response Relationship, Drug,
pubmed-meshheading:14766745-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:14766745-Epitopes,
pubmed-meshheading:14766745-Immunoblotting,
pubmed-meshheading:14766745-Male,
pubmed-meshheading:14766745-Models, Molecular,
pubmed-meshheading:14766745-Molecular Sequence Data,
pubmed-meshheading:14766745-Muscle Cells,
pubmed-meshheading:14766745-Peptides,
pubmed-meshheading:14766745-Phosphorylation,
pubmed-meshheading:14766745-Protein Conformation,
pubmed-meshheading:14766745-Protein Structure, Secondary,
pubmed-meshheading:14766745-Protein Structure, Tertiary,
pubmed-meshheading:14766745-Rabbits,
pubmed-meshheading:14766745-Rats,
pubmed-meshheading:14766745-Rats, Wistar,
pubmed-meshheading:14766745-Sarcoplasmic Reticulum,
pubmed-meshheading:14766745-Sarcoplasmic Reticulum Calcium-Transporting ATPases,
pubmed-meshheading:14766745-Sequence Homology, Amino Acid,
pubmed-meshheading:14766745-Serine,
pubmed-meshheading:14766745-Spectrometry, Mass, Electrospray Ionization
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pubmed:year |
2004
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pubmed:articleTitle |
Critical evaluation of cardiac Ca2+-ATPase phosphorylation on serine 38 using a phosphorylation site-specific antibody.
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pubmed:affiliation |
School of Biochemistry & Molecular Biology, University of Leeds, Leeds LS2 9JT, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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