Source:http://linkedlifedata.com/resource/pubmed/id/10730578
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
8
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| pubmed:dateCreated |
2000-5-23
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| pubmed:abstractText |
We examined the binding domains of cardiac and fast skeletal muscle troponin I (CTnI and FTnI, respectively) to myofibrils (MFs). Deletion mutants containing CTnI amino acid residues 1-79, 43-207 and 80-207 (CTnI-head, CTnI-tail-I and CTnI-tail-2, respectively) and FTnI amino acid residues 1-54 and 55-182 (FTnI-head and FTnI-tail, respectively) were transiently expressed in cardiac and fast skeletal muscle cells. To monitor the intracellular localization of these exogenously introduced truncated TnIs, epitope tagging was used. CTnI-tail-1 was incorporated into cardiac MFs specifically, but CTnI-tail-2 was not assembled onto any MFs examined. This suggests that there is no potent actin filament-binding site in CTnI-tail-2. Since CTnI-tail-1 has an amino acid extension (CTnI residues 43-79) whose sequence is longer than that of CTnI-head-2; it appears that this sequence extension is important in binding to cardiac MFs. FTnI-tail, containing the inhibitory domain of actomyosin ATPase, showed intensive and specific incorporation into fast MFs. FTnI-tail was a homologous fragment of CTnI-tail-2, but the binding patterns of these two domains differed greatly from each other. It is possible that the absence of potent binding affinity of CTnI-tail-2 corresponding to the inhibitory domain of actomyosin ATPase is advantageous for continuous cardiac muscle contraction, since a potent inhibitory activity is a serious obstacle to cardiac muscle contraction. It can be assumed that distinctive binding ability of functional domains of TnI-tails reflect unique adaptations to muscles with different physiological properties.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0142-4319
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
20
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
755-60
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:10730578-Amino Acid Sequence,
pubmed-meshheading:10730578-Animals,
pubmed-meshheading:10730578-Binding Sites,
pubmed-meshheading:10730578-Blotting, Western,
pubmed-meshheading:10730578-Cells, Cultured,
pubmed-meshheading:10730578-Chickens,
pubmed-meshheading:10730578-DNA,
pubmed-meshheading:10730578-Epitope Mapping,
pubmed-meshheading:10730578-Fluorescent Antibody Technique,
pubmed-meshheading:10730578-Gene Deletion,
pubmed-meshheading:10730578-Molecular Sequence Data,
pubmed-meshheading:10730578-Muscle, Skeletal,
pubmed-meshheading:10730578-Muscle Fibers, Fast-Twitch,
pubmed-meshheading:10730578-Mutation,
pubmed-meshheading:10730578-Myocardium,
pubmed-meshheading:10730578-Oligonucleotide Probes,
pubmed-meshheading:10730578-Protein Isoforms,
pubmed-meshheading:10730578-Transfection,
pubmed-meshheading:10730578-Troponin I
|
| pubmed:year |
1999
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| pubmed:articleTitle |
Thin-filament-binding domains of cardiac and fast skeletal muscle troponin I isoforms as studied by epitope tagging.
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| pubmed:affiliation |
Department of Anatonmy/Cell Biology, Chiba University, Japan. toyota@med.m.chiba-u.ac.jp
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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