Source:http://linkedlifedata.com/resource/pubmed/id/17638863
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
2007-7-19
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pubmed:abstractText |
Prostatic acid phosphatase (PAP) is currently evaluated as a target for vaccine immunotherapy of prostate cancer. This is based on the previous knowledge about secretory PAP and its high prostatic expression. We describe a novel PAP spliced variant mRNA encoding a type I transmembrane (TM) protein with the extracellular NH(2)-terminal phosphatase activity and the COOH-terminal lysosomal targeting signal (YxxPhi). TM-PAP is widely expressed in nonprostatic tissues like brain, kidney, liver, lung, muscle, placenta, salivary gland, spleen, thyroid, and thymus. TM-PAP is also expressed in fibroblast, Schwann, and LNCaP cells, but not in PC-3 cells. In well-differentiated human prostate cancer tissue specimens, the expression of secretory PAP, but not TM-PAP, is significantly decreased. TM-PAP is localized in the plasma membrane-endosomal-lysosomal pathway and is colocalized with the lipid raft marker flotillin-1. No cytosolic PAP is detected. We conclude that the wide expression of TM-PAP in, for instance, neuronal and muscle tissues must be taken into account in the design of PAP-based immunotherapy approaches.
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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 |
Jul
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pubmed:issn |
0008-5472
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pubmed:author |
pubmed-author:AraujoCésar LCL,
pubmed-author:EskelinenEeva-LiisaEL,
pubmed-author:HellströmPekka APA,
pubmed-author:HerralaAnnakaisa MAM,
pubmed-author:HirvikoskiPasi PPP,
pubmed-author:JokitaloEijaE,
pubmed-author:PulkkaAnitta EAE,
pubmed-author:QuinteroIleana BIB,
pubmed-author:TuominenHannu JHJ,
pubmed-author:VihkoPirkko TPT,
pubmed-author:WirkkalaRiikka SRS
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6549-54
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17638863-Amino Acid Sequence,
pubmed-meshheading:17638863-Cell Line, Tumor,
pubmed-meshheading:17638863-Cell Membrane,
pubmed-meshheading:17638863-Cytosol,
pubmed-meshheading:17638863-Humans,
pubmed-meshheading:17638863-Male,
pubmed-meshheading:17638863-Membrane Microdomains,
pubmed-meshheading:17638863-Membrane Proteins,
pubmed-meshheading:17638863-Molecular Sequence Data,
pubmed-meshheading:17638863-Prostate,
pubmed-meshheading:17638863-Protein Structure, Tertiary,
pubmed-meshheading:17638863-Protein Tyrosine Phosphatases,
pubmed-meshheading:17638863-Sequence Homology, Amino Acid,
pubmed-meshheading:17638863-Tissue Distribution
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pubmed:year |
2007
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pubmed:articleTitle |
Prostatic acid phosphatase is not a prostate specific target.
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pubmed:affiliation |
Research Center for Molecular Endocrinology and WHO Collaborating Centre, Biocenter Oulu, University of Oulu, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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