Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1989-8-29
pubmed:abstractText
Multidomain proteins of the extracellular matrix (ECM) play an important role in development and maintenance of cellular organization and in tissue repair. Several ECM proteins such as laminin, tenascin and thrombospondin contain domains with homology to epidermal growth factor (EGF) and exhibit growth promoting activity. The mitogenic activity of laminin is restricted to a fragment which consists of about 25 repeating domains with partial homology to EGF and comprises the rod-like inner regions of the three short arms of the four armed molecule. The mitogenic activity does not correlate with promotion of cell attachment and neurite outgrowth for which major functional sites have been found in other regions of the laminin molecule. It is suggested that EGF-like domains in laminin, in other ECM proteins and in the extracellular portions of some membrane proteins are signals for cellular growth and differentiation. Because they are integral parts of large molecules and often of supramolecular assemblies these domains are well suited to stimulate neighboring cells in a specific and vectorial way. This concept of localized growth or differentiation signals offers an attractive mechanism for the regulation of cellular development.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation?
pubmed:affiliation
Abteilung für Biophysikalische Chemie, Biozentrum der Universität, Basal, Switzerland.
pubmed:publicationType
Journal Article, Comparative Study, Review