Linked Life Data

9177305

Source:http://linkedlifedata.com/resource/pubmed/id/9177305

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-7-10
pubmed:abstractText
A mesenchymal protein, epimorphin, is known to bind directly to the cell surface through its central portion and to act as a signaling molecule for epithelial morphogenesis. Utilizing several recombinant polypeptides and synthetic peptides, we identified the cellular recognition sequence of epimorphin in the central portion of this molecule (amino acids 105-123, NGNRTSVDLRIRRTQHSVL; termed NL-peptide sequence). Interestingly, although a model cell type bound to the NL-peptide as strong as to the full-length epimorphin, this peptide itself didn't induce the cellular functional responses so far tested. We found that the NL-peptide behaved as an antagonist for the endogenous epimorphin and severely perturbed lung branching morphogenesis in organ culture. These results not only revealed a part of the functional mechanism of epimorphin but also demonstrated that cell/ epimorphin interaction through the NL-peptide sequence is a critical step for lung epithelial morphogenesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
522-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Identification of cellular recognition sequence of epimorphin and critical role of cell/epimorphin interaction in lung branching morphogenesis.
pubmed:affiliation
Biomedical R & D Department, Sumitomo Electric Industries, Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't