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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1996-9-4
|
| pubmed:databankReference | |
| pubmed:abstractText |
DNA sequences encoding a novel member of the receptor protein tyrosine phosphatase (R-PTP) family, termed PCP-2, were identified in a human pancreatic adenocarcinoma cDNA library. Human PCP-2 cDNA predicts a protein of 1430 amino acids with a calculated Mr of 160 kDa. The predicted PCP-2 enzyme consists of a 740 amino acid extracellular region, a single transmembrane domain, and a 666 amino acid intracellular portion. The extracellular sequence contains a MAM (meprin/A5/PTPmu) domain, an immunoglobulin-like domain and four fibronectin type III-like repeats, suggesting that it is a member of the PTPkappa and PTPmu subfamily. The intracellular region contains two tandemly-repeated protein tyrosine phosphatase domains. Northern blot analyses revealed a single transcript of 5.5 kilobases, which is expressed at different levels in many human tissues except spleen and placenta. Upon transfection of PCP-2 cDNA into human embryonic kidney fibroblast 293 cells, a protein with an apparent Mr of 180 000 was detected by immunoblot analysis. This size was reduced to the predicted Mr upon treatment with endoglycosidase F, indicating that PCP-2 is glycosylated and, hence, expressed at the cell surface. A potential role of PCP-2 in cell-cell recognition and adhesion is supported by its co-localization with cell adhesion molecules, such as catenin and E-cadherin, at sites of cell-cell contact.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/mammary carcinoma antigen
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0950-9232
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
12
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2555-62
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8700514-Adenocarcinoma,
pubmed-meshheading:8700514-Amino Acid Sequence,
pubmed-meshheading:8700514-Antigens, Neoplasm,
pubmed-meshheading:8700514-Base Sequence,
pubmed-meshheading:8700514-Cadherins,
pubmed-meshheading:8700514-Cell Adhesion,
pubmed-meshheading:8700514-Cloning, Molecular,
pubmed-meshheading:8700514-Cytoskeletal Proteins,
pubmed-meshheading:8700514-Humans,
pubmed-meshheading:8700514-Molecular Sequence Data,
pubmed-meshheading:8700514-Pancreatic Neoplasms,
pubmed-meshheading:8700514-Protein Tyrosine Phosphatases,
pubmed-meshheading:8700514-RNA, Messenger,
pubmed-meshheading:8700514-Sequence Homology, Amino Acid,
pubmed-meshheading:8700514-Tissue Distribution,
pubmed-meshheading:8700514-Trans-Activators,
pubmed-meshheading:8700514-Tumor Cells, Cultured,
pubmed-meshheading:8700514-beta Catenin
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Characterization of PCP-2, a novel receptor protein tyrosine phosphatase of the MAM domain family.
|
| pubmed:affiliation |
Department of Molecular Biology, Max-Planck-Institute für Biochemie, Germany.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|