Source:http://linkedlifedata.com/resource/pubmed/id/11414767
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2001-6-20
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| pubmed:databankReference | |
| pubmed:abstractText |
Acid phosphatases are enzymes capable of hydrolyzing orthophosphoric acid esters in an acid medium. Prostatic acid phosphatase has served as a tumor marker for metastatic prostate cancer for many years. We have cloned a new human acid phosphatase gene (named testicular acid phosphatase, ACPT), which is expressed mainly in testis and to a lower extent in the prostate, trachea, and other tissues. This gene maps to chromosome 19q13.4, in an area that harbors many cancer-related genes. The testicular acid phosphatase gene is composed of 11 exons, and the protein is predicted to have a luminal domain, a transmembrane domain, and a cytoplasmic domain. The N-terminal end of the protein encodes a signal peptide. The protein has approximately 50% homology with both the prostatic and the lysosomal acid phosphatases, and the position of the cysteine residues, the N-glycosylation sites, and the histidine catalytic site are conserved among the three proteins. The testicular acid phosphatase gene is up-regulated by androgens and is down-regulated by estrogens in the prostate cancer cell line LNCaP. Our preliminary results indicate that this gene exhibits a lower level of expression in testicular cancer tissues than in their normal counterparts.
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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 |
Jun
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| pubmed:issn |
0888-7543
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
74
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
385-95
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| pubmed:dateRevised |
2004-11-17
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| pubmed:meshHeading |
pubmed-meshheading:11414767-Acid Phosphatase,
pubmed-meshheading:11414767-Alternative Splicing,
pubmed-meshheading:11414767-Amino Acid Sequence,
pubmed-meshheading:11414767-Base Sequence,
pubmed-meshheading:11414767-Chromosome Mapping,
pubmed-meshheading:11414767-Chromosomes, Human, Pair 19,
pubmed-meshheading:11414767-Cloning, Molecular,
pubmed-meshheading:11414767-DNA,
pubmed-meshheading:11414767-Exons,
pubmed-meshheading:11414767-Female,
pubmed-meshheading:11414767-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11414767-Humans,
pubmed-meshheading:11414767-Introns,
pubmed-meshheading:11414767-Male,
pubmed-meshheading:11414767-Molecular Sequence Data,
pubmed-meshheading:11414767-Phylogeny,
pubmed-meshheading:11414767-RNA, Messenger,
pubmed-meshheading:11414767-Sequence Alignment,
pubmed-meshheading:11414767-Sequence Analysis, DNA,
pubmed-meshheading:11414767-Sequence Homology, Amino Acid,
pubmed-meshheading:11414767-Testicular Neoplasms,
pubmed-meshheading:11414767-Testis,
pubmed-meshheading:11414767-Tissue Distribution,
pubmed-meshheading:11414767-Tumor Cells, Cultured
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| pubmed:year |
2001
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| pubmed:articleTitle |
Molecular cloning of a novel human acid phosphatase gene (ACPT) that is highly expressed in the testis.
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| pubmed:affiliation |
Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto, Ontario, M5G 1X5, Canada.
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| pubmed:publicationType |
Journal Article
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