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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
1998-9-14
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pubmed:databankReference | |
pubmed:abstractText |
To investigate a potential role of protein-tyrosine phosphatases (PTPases) in myocardial growth and signaling, a degenerate primer-based reverse transcription-polymerase chain reaction approach was used to isolate cDNAs for proteins that contain a PTPase catalytic domain. Among the 16 cDNA clones isolated by reverse transcription-polymerase chain reaction from total neonatal rat cardiomyocyte RNA, one, designated PTP-TD14, was unique. Subsequent isolation and sequencing of a full-length PTP-TD14 cDNA confirmed that it encodes a novel 164-kDa protein, p164(PTP-TD14). The C-terminal region contains the PTP-like domain, whereas the N-terminal region shows no homology to any known mammalian protein. However, this region is homologous to a yeast protein, BRO1, that is involved in the mitogen-activated protein kinase signaling pathway. Like BRO1, p164(PTP-TD14) contains a proline-rich region with two putative SH3-domain binding sites. By Northern blot analysis, PTP-TD14 is expressed as a 5.3-kilobase pair transcript, not only in neonatal heart but also in many adult rat tissues. When expressed in either COS-7 or NIH-3T3 cells, p164(PTP-TD14) localizes to the cytoplasm in association with vesicle-like structures. Expression of p164(PTP-TD14) in NIH-3T3 cells inhibits Ha-ras-mediated transformation more than 3-fold. This inhibitory activity is localized to the C-terminal PTPase homology domain, since no inhibition of Ha-ras-mediated focus formation was observed with a PTP-TD14 mutant, in which the putative catalytic activity was presumably inactivated by a point mutation. These findings indicate that PTP-TD14 encodes a novel protein that may be critically involved in regulating Ha-ras-dependent cell growth.
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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 |
Aug
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21077-83
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9694860-Amino Acid Sequence,
pubmed-meshheading:9694860-Animals,
pubmed-meshheading:9694860-Base Sequence,
pubmed-meshheading:9694860-Cell Transformation, Neoplastic,
pubmed-meshheading:9694860-Cells, Cultured,
pubmed-meshheading:9694860-Cloning, Molecular,
pubmed-meshheading:9694860-DNA, Complementary,
pubmed-meshheading:9694860-Genes, ras,
pubmed-meshheading:9694860-Molecular Sequence Data,
pubmed-meshheading:9694860-Mutagenesis,
pubmed-meshheading:9694860-Myocardium,
pubmed-meshheading:9694860-Protein Tyrosine Phosphatases,
pubmed-meshheading:9694860-Protein Tyrosine Phosphatases, Non-Receptor,
pubmed-meshheading:9694860-Rats,
pubmed-meshheading:9694860-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
A novel putative protein-tyrosine phosphatase contains a BRO1-like domain and suppresses Ha-ras-mediated transformation.
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pubmed:affiliation |
Victor Chang Cardiac Research Institute, St. Vincent's Hospital, Darlinghurst, NSW 2010, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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