Linked Life Data

17668446

Source:http://linkedlifedata.com/resource/pubmed/id/17668446

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-1-28
pubmed:abstractText
Raf kinase inhibitor protein (RKIP) regulates a number of cellular processes, including cell migration. Exploring the role of RKIP in cell adhesion, we found that overexpression of RKIP in Madin-Darby canine kidney (MDCK) epithelial cells increases adhesion to the substratum, while decreasing adhesion of the cells to one another. The level of the adherens junction protein E-cadherin declines profoundly, and there is loss of normal localization of the tight junction protein ZO-1, while expression of the cell-substratum adhesion protein beta1 integrin dramatically increases. The cells also display increased adhesion and spreading on multiple substrata, including collagen, gelatin, fibronectin and laminin. In three-dimensional culture, RKIP overexpression leads to marked cell elongation and extension of long membrane protrusions into the surrounding matrix, and the cells do not form hollow cysts. RKIP-overexpressing cells generate considerably more contractile traction force than do control cells. In contrast, RNA interference-based silencing of RKIP expression results in decreased cell-substratum adhesion in both MDCK and MCF7 human breast adenocarcinoma cells. Treatment of MDCK and MCF7 cells with locostatin, a direct inhibitor of RKIP and cell migration, also reduces cell-substratum adhesion. Silencing of RKIP expression in MCF7 cells leads to a reduction in the rate of wound closure in a scratch-wound assay, although not as pronounced as that previously reported for RKIP-knockdown MDCK cells. These results suggest that RKIP has important roles in the regulation of cell adhesion, positively controlling cell-substratum adhesion while negatively controlling cell-cell adhesion, and underscore the complex functions of RKIP in cell physiology.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1097-4644
pubmed:author
pubmed:copyrightInfo
Copyright 2007 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
972-85
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:17668446-Adherens Junctions, pubmed-meshheading:17668446-Animals, pubmed-meshheading:17668446-Antigens, CD29, pubmed-meshheading:17668446-Breast Neoplasms, pubmed-meshheading:17668446-Cadherins, pubmed-meshheading:17668446-Cell Movement, pubmed-meshheading:17668446-Cell-Matrix Junctions, pubmed-meshheading:17668446-Dogs, pubmed-meshheading:17668446-Down-Regulation, pubmed-meshheading:17668446-Epithelial Cells, pubmed-meshheading:17668446-Extracellular Matrix, pubmed-meshheading:17668446-Extracellular Matrix Proteins, pubmed-meshheading:17668446-Humans, pubmed-meshheading:17668446-Kidney Neoplasms, pubmed-meshheading:17668446-Membrane Proteins, pubmed-meshheading:17668446-Oxazolidinones, pubmed-meshheading:17668446-Phosphatidylethanolamine Binding Protein, pubmed-meshheading:17668446-Phosphoproteins, pubmed-meshheading:17668446-Protein Kinase Inhibitors, pubmed-meshheading:17668446-RNA Interference, pubmed-meshheading:17668446-Tumor Cells, Cultured, pubmed-meshheading:17668446-Up-Regulation, pubmed-meshheading:17668446-Wound Healing, pubmed-meshheading:17668446-raf Kinases
pubmed:year
2008
pubmed:articleTitle
Raf kinase inhibitor protein positively regulates cell-substratum adhesion while negatively regulating cell-cell adhesion.
pubmed:affiliation
Department of Chemistry, University of Connecticut, Storrs, Connecticut 06269, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural