Source:http://linkedlifedata.com/resource/pubmed/id/15358244
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2004-9-14
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pubmed:abstractText |
Protein-tyrosine-phosphatases (PTP-ases), in concert with protein tyrosine kinases, control various biological activities such as cell growth and differentiation. In rodents, around 40 PTP-ases have been described. Functional orthologue for each of these PTP-ases have been identified in human, except for OST-PTP. OST-PTP is a transmembrane PTP-ase with a restricted tissue distribution. In silico analysis on public sequence databases reveals a human OST-PTP gene orthologue that encompasses 21 kb on chromosome 1q32.1. Using RT-PCR we isolated a 4 kb hOST-PTP transcript. hOST-PTP cDNA sequence exhibits numerous disablements indicating that it does not code for a PTP-ase but is rather a pseudogene with unique features. Indeed, (i) it has no "functional" parent in the human genome, (ii) it has retained an "intron-exon" structure, and (iii) it is transcribed in a regulated manner. Interestingly, we found two ESTs, from domesticated pig and from cow that exhibit ORF that would predict a functional OST-PTP orthologue in Artiodactyls. Taken together, these results indicate that OST-PTP is the only PTP-ase the function of which has been lost during the evolution process between rodents and human.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptprv protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Like Protein Tyrosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
321
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-65
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15358244-Amino Acid Sequence,
pubmed-meshheading:15358244-Animals,
pubmed-meshheading:15358244-Base Sequence,
pubmed-meshheading:15358244-Cloning, Molecular,
pubmed-meshheading:15358244-Conserved Sequence,
pubmed-meshheading:15358244-DNA Primers,
pubmed-meshheading:15358244-Exons,
pubmed-meshheading:15358244-Humans,
pubmed-meshheading:15358244-Mice,
pubmed-meshheading:15358244-Molecular Sequence Data,
pubmed-meshheading:15358244-Protein Tyrosine Phosphatases,
pubmed-meshheading:15358244-Receptor-Like Protein Tyrosine Phosphatases, Class 3,
pubmed-meshheading:15358244-Recombinant Proteins,
pubmed-meshheading:15358244-Sequence Alignment,
pubmed-meshheading:15358244-Sequence Homology, Amino Acid,
pubmed-meshheading:15358244-Species Specificity
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pubmed:year |
2004
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pubmed:articleTitle |
Cloning of hOST-PTP: the only example of a protein-tyrosine-phosphatase the function of which has been lost between rodent and human.
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pubmed:affiliation |
Institute of Signaling Developmental Biology and Cancer-UMR 6543 CNRS, Faculté des Sciences, 06108 Nice Cedex 2, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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