Source:http://linkedlifedata.com/resource/pubmed/id/11058082
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
2001-1-23
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| pubmed:abstractText |
Calsequestrin is the major calcium-binding protein of cardiac and skeletal muscles whose function is to sequester Ca(2+ )in the lumen of the sarcoplasmic reticulum (SR). Here we describe the identification and functional characterization of a C. elegans calsequestrin gene (csq-1). CSQ-1 shows moderate similarity (50% similarity, 30% identity) to rabbit skeletal calsequestrin. Unlike mammals, which have two different genes encoding cardiac and fast-twitch skeletal muscle isoforms, csq-1 is the only calsequestrin gene in the C. elegans genome. We show that csq-1 is highly expressed in the body-wall muscles, beginning in mid-embryogenesis and maintained through the adult stage. In body-wall muscle cells, CSQ-1 is localized to sarcoplasmic membranes surrounding sarcomeric structures, in the regions where ryanodine receptors (UNC-68) are located. Mutation in UNC-68 affects CSQ-1 localization, suggesting that the two possibly interact in vivo. Genetic analyses of chromosomal deficiency mutants deleting csq-1 show that CSQ-1 is not essential for initiation of embryonic muscle formation and contraction. Furthermore, double-stranded RNA injection resulted in animals completely lacking CSQ-1 in body-wall muscles with no observable defects in locomotion. These findings suggest that although CSQ-1 is one of the major calcium-binding proteins in the body-wall muscles of C. elegans, it is not essential for body-wall muscle formation and contraction.
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| pubmed:grant | |
| pubmed:commentsCorrections | |
| 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 |
0021-9533
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| pubmed:author |
pubmed-author:AhnnJJ,
pubmed-author:BandyopadhyayJJ,
pubmed-author:HOAKC GCG,
pubmed-author:HamadaTT,
pubmed-author:KagawaHH,
pubmed-author:KimD HDH,
pubmed-author:LUY CYC,
pubmed-author:MaryonE BEB,
pubmed-author:MouT WTW,
pubmed-author:MunkMM,
pubmed-author:ParkW JWJ,
pubmed-author:ShinJ YJY,
pubmed-author:YuJJ
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| pubmed:issnType |
Print
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| pubmed:volume |
113 ( Pt 22)
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
3947-58
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| pubmed:dateRevised |
2010-9-2
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| pubmed:meshHeading |
pubmed-meshheading:11058082-Amino Acid Sequence,
pubmed-meshheading:11058082-Animals,
pubmed-meshheading:11058082-Base Sequence,
pubmed-meshheading:11058082-Caenorhabditis elegans,
pubmed-meshheading:11058082-Calcium,
pubmed-meshheading:11058082-Calsequestrin,
pubmed-meshheading:11058082-Chromosome Mapping,
pubmed-meshheading:11058082-Cloning, Molecular,
pubmed-meshheading:11058082-Gene Deletion,
pubmed-meshheading:11058082-Genes, Helminth,
pubmed-meshheading:11058082-Humans,
pubmed-meshheading:11058082-Mammals,
pubmed-meshheading:11058082-Molecular Sequence Data,
pubmed-meshheading:11058082-Muscle, Skeletal,
pubmed-meshheading:11058082-Rabbits,
pubmed-meshheading:11058082-Recombinant Proteins,
pubmed-meshheading:11058082-Sarcoplasmic Reticulum,
pubmed-meshheading:11058082-Sequence Alignment,
pubmed-meshheading:11058082-Sequence Homology, Amino Acid
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| pubmed:year |
2000
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| pubmed:articleTitle |
Calsequestrin, a calcium sequestering protein localized at the sarcoplasmic reticulum, is not essential for body-wall muscle function in Caenorhabditis elegans.
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| pubmed:affiliation |
Department of Life Science, Kwangju Institute of Science and Technology, Kwangju, Korea.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|