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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1998-6-18
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pubmed:abstractText |
Using RNA fingerprinting (RAP) strategy and Northern blot analysis, we identified a differentially expressed sequence DOC-2 which is detectable in all normal human ovarian surface epithelial (HOSE) cell cultures but not in ovarian cancer cell lines and tissues. Subsequent cloning of DOC-2 from a cDNA library generated from the HOSE cells was carried out using the 3' and 5' RACE approach. A 3268 base pair full length cDNA of DOC-2 was isolated and sequenced. The predicted protein has a length of 770 amino acids. Homology search of all NCBI sequences indicated that the amino acid sequence of DOC-2 shares 93% homology with the mouse p96/mDab2 phosphoprotein and has a phosphotyrosine interacting domain (PID) and multiple SH3 binding motifs. Chromosomal localization by FISH showed that the DOC-2 gene is located on 5p13. Western blot analysis showed that the 105 kDa DOC-2 protein was down-regulated in all the carcinoma cell lines. In-situ immunohistochemistry performed on normal ovaries, and benign, borderline and invasive ovarian tumor tissues showed down regulation of DOC-2 protein particularly in serous ovarian tumor tissues. When DOC-2 was transfected into the ovarian carcinoma cell line SKOV3, the stable transfectants showed significantly reduced growth rate and ability to form tumors in nude mice. These data suggest that down-regulation of DOC-2 may play an important role in ovarian carcinogenesis.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Vesicular...,
http://linkedlifedata.com/resource/pubmed/chemical/DAB2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Neoplasm
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0950-9232
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2381-7
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9620555-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:9620555-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:9620555-Amino Acid Sequence,
pubmed-meshheading:9620555-Chromosomes, Human, Pair 5,
pubmed-meshheading:9620555-Female,
pubmed-meshheading:9620555-Genes, Tumor Suppressor,
pubmed-meshheading:9620555-Humans,
pubmed-meshheading:9620555-Molecular Sequence Data,
pubmed-meshheading:9620555-Neoplasms, Glandular and Epithelial,
pubmed-meshheading:9620555-Ovarian Neoplasms,
pubmed-meshheading:9620555-Proteins,
pubmed-meshheading:9620555-RNA, Neoplasm,
pubmed-meshheading:9620555-Sequence Homology, Amino Acid,
pubmed-meshheading:9620555-Transfection,
pubmed-meshheading:9620555-Tumor Cells, Cultured
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pubmed:year |
1998
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pubmed:articleTitle |
DOC-2, a candidate tumor suppressor gene in human epithelial ovarian cancer.
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pubmed:affiliation |
Department of Obstetrics, Gynecology and Reproductive Biology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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