Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2007-4-23
pubmed:abstractText
ZO-2 is a tight junction (TJ) protein that shuttles between the plasma membrane and the nucleus. ZO-2 contains several protein binding sites that allow it to function as a scaffold that clusters integral, adaptor and signaling proteins. To gain insight into the role of ZO-2 in epithelial cells, ZO-2 was silenced in MDCK cells with small interference RNA (siRNA). ZO-2 silencing triggered: (A) changes in the gate function of the TJ, determined by an increase in dextran flow through the paracellular route of mature monolayers and achievement of lower transepithelial electrical resistance values upon TJ de novo formation; (B) changes in the fence function of the TJ manifested by a non-polarized distribution of E-cadherin on the plasma membrane; (C) altered expression of TJ and adherens junction proteins, determined by a decreased amount of occludin and E-cadherin in mature monolayers and a delayed arrival to the plasma membrane of ZO-1, occludin and E-cadherin during a calcium switch assay; and (D) an atypical monolayer architecture characterized by the appearance of widened intercellular spaces, multistratification of regions in the culture and an altered pattern of actin at the cellular borders.
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
1
pubmed:volume
313
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1533-47
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
ZO-2 silencing in epithelial cells perturbs the gate and fence function of tight junctions and leads to an atypical monolayer architecture.
pubmed:affiliation
Department of Physiology, Biophysics and Neuroscience, Center for Research and Advanced Studies (CINVESTAV), Mexico City, Mexico.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't