Linked Life Data

9739078

Source:http://linkedlifedata.com/resource/pubmed/id/9739078

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1998-12-22
pubmed:abstractText
Vascular endothelial cells assemble adhesive intercellular junctions comprising a unique cadherin, VE-cadherin, which is coupled to the actin cytoskeleton through cytoplasmic interactions with plakoglobin, beta-catenin and alpha -catenin. However, the potential linkage between VE-cadherin and the vimentin intermediate filament cytoskeleton is not well characterized. Recent evidence indicates that lymphatic and vascular endothelial cells express desmoplakin, a cytoplasmic desmosomal protein that attaches intermediate filaments to the plasma membrane in epithelial cells. In the present study, desmoplakin was localized to intercellular junctions in human dermal microvascular endothelial cells. To determine if VE-cadherin could associate with desmoplakin, VE-cadherin, plakoglobin, and a desmoplakin amino-terminal polypeptide (DP-NTP) were co-expressed in L-cell fibroblasts. In the presence of VE-cadherin, both plakoglobin and DP-NTP were recruited to cell-cell borders. Interestingly, beta-catenin could not substitute for plakoglobin in the recruitment of DP-NTP to cell borders, and DP-NTP bound to plakoglobin but not beta-catenin in the yeast two-hybrid system. In addition, DP-NTP colocalized at cell-cell borders with alpha-catenin in the L-cell lines, and endogenous desmoplakin and alpha-catenin colocalized in cultured dermal microvascular endothelial cells. This is in striking contrast to epithelial cells, where desmoplakin and alpha -+catenin are restricted to desmosomes and adherens junctions, respectively. These results suggest that endothelial cells assemble unique junctional complexes that couple VE-cadherin to both the actin and intermediate filament cytoskeleton.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
111 ( Pt 20)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3045-57
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9739078-Animals, pubmed-meshheading:9739078-Antigens, CD, pubmed-meshheading:9739078-COS Cells, pubmed-meshheading:9739078-Cadherins, pubmed-meshheading:9739078-Cells, Cultured, pubmed-meshheading:9739078-Cytoskeletal Proteins, pubmed-meshheading:9739078-Cytoskeleton, pubmed-meshheading:9739078-Desmoplakins, pubmed-meshheading:9739078-Endothelium, Vascular, pubmed-meshheading:9739078-Forskolin, pubmed-meshheading:9739078-Humans, pubmed-meshheading:9739078-Immunoglobulin G, pubmed-meshheading:9739078-Intercellular Junctions, pubmed-meshheading:9739078-Intermediate Filaments, pubmed-meshheading:9739078-L Cells (Cell Line), pubmed-meshheading:9739078-Mice, pubmed-meshheading:9739078-Models, Biological, pubmed-meshheading:9739078-Recombinant Proteins, pubmed-meshheading:9739078-Transfection, pubmed-meshheading:9739078-gamma Catenin
pubmed:year
1998
pubmed:articleTitle
VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: a pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions.
pubmed:affiliation
Departments of Dermatology, Pathology, and The Robert H. Lurie Cancer Center, Northwestern University Medical School, Chicago, IL, USA. akowalc@emory.edu.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't