Source:http://linkedlifedata.com/resource/pubmed/id/17482382
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
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| pubmed:dateCreated |
2007-7-2
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| pubmed:abstractText |
Whole genome sequence data permit the study of protein families regulating cellular homeostasis during development. Here we present a study of the sea urchin Ca(2+)-ATPases made possible by the Sea Urchin Genome Sequencing Project. This is of potential interest because adult sea urchins, their gametes and embryos live in the relatively high Ca(2+) concentration of 10 mM. Three Ca(2+)-ATPases regulate Ca(2+) levels in animal cells: plasma membrane Ca(2+)-ATPase (PMCA), sarcoplasmic/endoplasmic reticulum Ca(2+)-ATPase (SERCA) and secretory pathway Ca(2+)-ATPase (SPCA). The primary structures of Sp-PMCA and Sp-SERCA in the sea urchin, Strongylocentrotus purpuratus (Sp), have been published. Here, we present the primary structure of Sp-SPCA, which is 912 amino acids and has 66% identity and 80% similarity to human SPCA1. Southern blots and genome analysis show that Sp-SPCA is a single copy gene. Each Sp Ca(2+)-ATPase is highly conserved when compared to its human ortholog, indicating that human and sea urchin share structurally similar energy driven Ca(2+) homeostasis mechanisms that have been maintained throughout the course of deuterostome evolution. Annotation using the assembled sea urchin genome reveals that Sp-SPCA, Sp-PMCA and Sp-SERCA have 23, 17 and 24 exons. RT-Q-PCR shows that transcripts of Sp-SPCA are at low levels compared to Sp-PMCA and Sp-SERCA. Gradual increases in Sp-PMCA and Sp-SERCA mRNA begin at the 18 hour hatched blastula stage and peak 4-5-fold higher by 25 h at the mid to late blastulae stage.
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| pubmed:grant | |
| 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 |
Aug
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| pubmed:issn |
0378-1119
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
1
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| pubmed:volume |
397
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
67-75
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| pubmed:dateRevised |
2010-11-18
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| pubmed:meshHeading |
pubmed-meshheading:17482382-Amino Acid Sequence,
pubmed-meshheading:17482382-Animals,
pubmed-meshheading:17482382-Base Sequence,
pubmed-meshheading:17482382-Calcium-Transporting ATPases,
pubmed-meshheading:17482382-Cloning, Molecular,
pubmed-meshheading:17482382-DNA, Complementary,
pubmed-meshheading:17482382-Gene Expression Regulation, Developmental,
pubmed-meshheading:17482382-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:17482382-Humans,
pubmed-meshheading:17482382-Male,
pubmed-meshheading:17482382-Molecular Sequence Data,
pubmed-meshheading:17482382-Multigene Family,
pubmed-meshheading:17482382-Phylogeny,
pubmed-meshheading:17482382-Plasma Membrane Calcium-Transporting ATPases,
pubmed-meshheading:17482382-Protein Structure, Tertiary,
pubmed-meshheading:17482382-Sarcoplasmic Reticulum Calcium-Transporting ATPases,
pubmed-meshheading:17482382-Sequence Homology, Amino Acid,
pubmed-meshheading:17482382-Strongylocentrotus purpuratus
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| pubmed:year |
2007
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| pubmed:articleTitle |
Sequence, annotation and developmental expression of the sea urchin Ca(2+) -ATPase family.
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| pubmed:affiliation |
Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093-0202, USA. jayantha_gunaratne@etc.a-star.edu.sg
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, N.I.H., Extramural
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