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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1998-7-8
|
| pubmed:databankReference | |
| pubmed:abstractText |
Using the new signal sequence trap (SST) method, we isolated several clones encoding secreted and transmembrane proteins from KUSA cells, a murine osteoblast-like cell line. One isolated novel clone, termed entactin-2, exhibited a high similarity to mouse entactin/nidogen, a basement membrane protein. Although deduction of the amino acid sequence of entactin-2 revealed only 27.4% homology to entactin, many structural similarities were seen between both proteins. Entactin-2 contains five EGF-like and two thyroglobulin-like motifs, which are both cysteine-rich. Comparison of both proteins clearly revealed that entactin-2 also contains related domain structures. The rod-like domain of entactin-2, containing the RGD integrin recognition sequence, fused to glutathione-S transferase (GST), revealed a cell surface-binding activity similar to that of entactin. In addition, the tissue distribution of entactin-2 mRNA resembled that of entactin. Furthermore, mRNA expression of both genes decreased as osteoblastic differentiation progressed. These results suggest that entactin-2 is a member of the entactin gene family, may have entactin-related functions, and might act as a basement membrane component.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0014-4827
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
241
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
36-45
|
| pubmed:dateRevised |
2005-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:9633511-Amino Acid Sequence,
pubmed-meshheading:9633511-Animals,
pubmed-meshheading:9633511-Base Sequence,
pubmed-meshheading:9633511-Basement Membrane,
pubmed-meshheading:9633511-Cell Line,
pubmed-meshheading:9633511-Cloning, Molecular,
pubmed-meshheading:9633511-DNA, Complementary,
pubmed-meshheading:9633511-Eukaryotic Cells,
pubmed-meshheading:9633511-Gene Expression,
pubmed-meshheading:9633511-Genes,
pubmed-meshheading:9633511-Membrane Glycoproteins,
pubmed-meshheading:9633511-Membrane Proteins,
pubmed-meshheading:9633511-Molecular Sequence Data,
pubmed-meshheading:9633511-Protein Binding,
pubmed-meshheading:9633511-Sequence Alignment,
pubmed-meshheading:9633511-Sequence Analysis,
pubmed-meshheading:9633511-Sequence Homology, Amino Acid,
pubmed-meshheading:9633511-Tissue Distribution
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Entactin-2: a new member of basement membrane protein with high homology to entactin/nidogen.
|
| pubmed:affiliation |
Gene Search Program, Chugai Research Institute for Molecular Medicine, Ibaraki, Japan.
|
| pubmed:publicationType |
Journal Article
|