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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
18
|
| pubmed:dateCreated |
1990-1-11
|
| pubmed:databankReference | |
| pubmed:abstractText |
The high-affinity cellular receptor for the basement membrane component laminin is differentially expressed during tumor invasion and metastasis. A cDNA clone encoding the murine laminin receptor was isolated and identified on the basis of sequence homology to the human laminin receptor [Wewer et al. (1986) Proc. Natl. Acad. Sci. U.S.A. 83, 7137-7141]. Primer extension experiments demonstrated that the clone contained the complete 5' sequence of the murine laminin receptor mRNA. RNA blot data demonstrated a single-sized laminin receptor mRNA, approximately 1400 bases long, in human, mouse, and rat. The nascent laminin receptor predicted from the cDNA sequence is 295 amino acids long, with a molecular weight of 33,000, and contains one intradisulfide bridge, a short putative transmembrane domain, and an extracellular carboxy-terminal region which has abundant glutamic acid residues and multiple repeat sequences. The precursor of the laminin receptor is apparently smaller than the 67-kilodalton protein isolated from tissue. The apparent molecular weight on SDS-polyacrylamide gels of the rabbit reticulocyte cell-free translation product of selectively hybridized laminin receptor mRNA is 37,000. Antisera to three different domains of the cDNA-predicted receptor were used to study the relationship between the 37- and 67-kilodalton polypeptides. Antisera to cDNA-deduced synthetic peptides of the receptor immunoprecipitated a 37-kilodalton band both from cell-free translation products and from pulse-labeled cell extracts. On immunoblots of cell extracts, one antisynthetic peptide antiserum recognized only the 67-kilodalton receptor, while another antiserum identified both 37- and 67-kilodalton polypeptides, suggesting a precursor-product relationship between the two polypeptides.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Laminin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
5
|
| pubmed:volume |
28
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
7476-86
|
| pubmed:dateRevised |
2004-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:2531008-Amino Acid Sequence,
pubmed-meshheading:2531008-Animals,
pubmed-meshheading:2531008-Base Sequence,
pubmed-meshheading:2531008-DNA,
pubmed-meshheading:2531008-Humans,
pubmed-meshheading:2531008-Immunoblotting,
pubmed-meshheading:2531008-Laminin,
pubmed-meshheading:2531008-Mice,
pubmed-meshheading:2531008-Molecular Sequence Data,
pubmed-meshheading:2531008-Neoplasm Metastasis,
pubmed-meshheading:2531008-Nucleic Acid Conformation,
pubmed-meshheading:2531008-Nucleic Acid Hybridization,
pubmed-meshheading:2531008-Protein Biosynthesis,
pubmed-meshheading:2531008-Protein Conformation,
pubmed-meshheading:2531008-Protein Precursors,
pubmed-meshheading:2531008-RNA, Messenger,
pubmed-meshheading:2531008-Rats,
pubmed-meshheading:2531008-Receptors, Immunologic,
pubmed-meshheading:2531008-Receptors, Laminin,
pubmed-meshheading:2531008-Restriction Mapping,
pubmed-meshheading:2531008-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2531008-Tumor Cells, Cultured
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Evidence for a precursor of the high-affinity metastasis-associated murine laminin receptor.
|
| pubmed:affiliation |
Laboratory of Pathology, National Cancer Institute, Bethesda, Maryland 20892.
|
| pubmed:publicationType |
Journal Article
|