Linked Life Data

9233779

Source:http://linkedlifedata.com/resource/pubmed/id/9233779

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-8-19
pubmed:abstractText
Normal human breast epithelial (HBE) cells which reached confluence ceased growth and tightly adhered to each other, forming a monolayer. In quiescent cells thus arrested by density, E-cadherin colocalized and coimmunoprecipitated with alpha- and beta-catenins in the boundary region between adjacent cells. By contrast, immunocytostaining and Western blot analyses revealed that E-cadherin colocalized and coprecipitated with beta-catenin but not with alpha-catenin in exponentially growing cells at low density. As a comparable amount of alpha-catenin was detected in the total cell lysate of cells at different densities, it is suggested that alpha-catenin is present but dissociates from the E-cadherin-beta-catenin complex in growing cells. beta-Catenin was tyrosine phosphorylated in growing cells at low density but not in quiescent cells at confluence. Tyrosine phosphorylation of beta-catenin was concomitantly induced with association of beta-catenin with EGF receptor (EGFR) when quiescent cells at confluence were dissociated into single cells by tryptic digestion, being accompanied by dissociation of alpha-catenin from E-cadherin. Both tyrosine phosphorylation and association of beta-catenin with EGFR were inhibited by tyrphostin, a specific inhibitor of the EGFR tyrosine kinase, whereas dissociation of alpha-catenin from E-cadherin was not. The results suggest that tyrosine phosphorylation of beta-catenin is achieved by EGFR upon tryptic digestion of cells and concurrent with but independent of dissociation of alpha-catenin from E-cadherin. beta-Catenin thus phosphorylated at tyrosine is suggested to play the role in preventing alpha-catenin once dissociated from reassociating with E-cadherin until cells reach confluence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
71-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Induction of tyrosine phosphorylation and association of beta-catenin with EGF receptor upon tryptic digestion of quiescent cells at confluence.
pubmed:affiliation
Department of Biochemistry, Kanagawa Cancer Center Research Institute, Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't