Linked Life Data

10601632

Source:http://linkedlifedata.com/resource/pubmed/id/10601632

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2000-2-3
pubmed:abstractText
T-cadherin (T-cad) is an unusual glycosylphosphatidylinositol-anchored member of the cadherin family of cell adhesion molecules. Binding of low density lipoproteins (LDLs) to T-cad can be demonstrated on Western blots of smooth muscle cell lysates, membranes and purified proteins. Using HEK293 cells transfected with human T-cad cDNA (T-cad+), we have investigated the adhesion properties of expressed mature and precursor proteins and examined the postulate that LDL represents a physiologically relevant ligand for T-cad. T-cad+ exhibits an increased Ca(2+)-dependent aggregation (vs. control) that was reduced by selective proteolytic cleavage of precursor T-cad and abolished after either proteolytic or phosphatidylinositol-specific phospholipase C (PI-PLC) cleavage of both mature and precursor proteins, indicating that both proteins function in intercellular adhesion. T-cad+ exhibited a significantly increased specific cell surface-binding of [(125)I]-LDL that was sensitive to PI-PLC pre-treatment of cells. Ca(2+)-dependent intercellular adhesion of T-cad+ was significantly inhibited by LDL. Our results support the suggestion that LDL is a physiologically relevant ligand for T-cad.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
463
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
29-34
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10601632-Cadherins, pubmed-meshheading:10601632-Calcium, pubmed-meshheading:10601632-Cell Adhesion, pubmed-meshheading:10601632-Cell Line, pubmed-meshheading:10601632-Dose-Response Relationship, Drug, pubmed-meshheading:10601632-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10601632-Humans, pubmed-meshheading:10601632-Immunoblotting, pubmed-meshheading:10601632-Kinetics, pubmed-meshheading:10601632-Lipoproteins, LDL, pubmed-meshheading:10601632-Phosphatidylinositol Diacylglycerol-Lyase, pubmed-meshheading:10601632-Phosphoinositide Phospholipase C, pubmed-meshheading:10601632-Protein Binding, pubmed-meshheading:10601632-Signal Transduction, pubmed-meshheading:10601632-Time Factors, pubmed-meshheading:10601632-Transfection, pubmed-meshheading:10601632-Type C Phospholipases
pubmed:year
1999
pubmed:articleTitle
LDL binds to surface-expressed human T-cadherin in transfected HEK293 cells and influences homophilic adhesive interactions.
pubmed:affiliation
Laboratory for Cardiovascular Research, Department of Research, Basel University Hospital, CH 4031, Basel, Switzerland. therese-j.resink@unibas.ch
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't