Linked Life Data

21610047

Source:http://linkedlifedata.com/resource/pubmed/id/21610047

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-7-1
pubmed:abstractText
Both receptor tyrosine kinases epidermal growth factor receptors (EGFRs) and their ligands are transmembrane proteins. It has been known that ligand binding activates cytoplasmic tyrosine kinase domains of EGFRs, resulting in the transduction of signals for cell proliferation, migration, differentiation or survival. In an EGFRs-ligands system, however, signal transduction occurs not only unidirectionally but also bidirectionally, which is regulated by cell-cell contact and proteolytic cleavage. Recent studies of proteolytic cleavage 'ectodomain shedding' of EGFRs and their ligands mediated by membrane-type metalloproteinases, a disintegrin and metalloproteinases have been unveiling novel functions and molecular mechanism of their remnant peptides. In addition, the study of the remnant peptide signalling would be essential for understanding the physiological and pathological relevance of anti-shedding therapeutic strategies for diseases such as cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1756-2651
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
150
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-22
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Ectodomain shedding and remnant peptide signalling of EGFRs and their ligands.
pubmed:affiliation
Department of Cell Growth and Tumor Regulation, Proteo-Medicine Research Center (ProMRes), Ehime University, Japan. shigeki@m.ehime-u.ac.jp
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't