Linked Life Data

9410884

Source:http://linkedlifedata.com/resource/pubmed/id/9410884

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-12-11
pubmed:abstractText
Tissue transglutaminase (tTgase, type II) is a Ca2+-dependent GTP binding protein which crosslinks proteins via (epsilon)((gamma)-glutamyl)lysine bridges. Although essentially a cytosolic enzyme there is increasing evidence to suggest the enzyme is externalised where it may play a role in extracellular matrix organisation. To investigate the function of this enzyme in a human umbilical endothelial cell line ECV304 tTgase expression was reduced in these cells by up to 90% by stable transfection with a 1.1. kb antisense construct in the plasmid vector pSG5. Two clones showing a reduction in expression of tTgase activity of 70 and 90% have been isolated and characterised. These clones show a number of phenotypic differences when compared to the parent cell line and the transfected controls which include reduced cell spreading and a decreased adhesion of cells on different substrata as measured by their susceptibility to removal by trypsin. Reduced cell spreading in the antisense transfected clones was accompanied by a decrease in the crosslinking of fibronectin into polymeric multimers which could be correlated to the amount of tTgase externalised by cells. A novel assay was developed to measure externalised tTgase activity which is cell mediated, inhibited by preincubation of cells with anti-tTgase antibody and relies on the incorporation of biotinylated cadaverine into fibronectin. The results of these experiments suggest that externalised tTgase may play a key role in a number of cell behavioural patterns which might be related to the enzymes ability to bind and crosslink fibronectin.
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
110 ( Pt 19)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2461-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9410884-Antibodies, Monoclonal, pubmed-meshheading:9410884-Biotinylation, pubmed-meshheading:9410884-Blotting, Northern, pubmed-meshheading:9410884-Cadaverine, pubmed-meshheading:9410884-Cell Adhesion, pubmed-meshheading:9410884-Cell Line, pubmed-meshheading:9410884-Cell Membrane, pubmed-meshheading:9410884-Cell Size, pubmed-meshheading:9410884-Clone Cells, pubmed-meshheading:9410884-Endothelium, Vascular, pubmed-meshheading:9410884-Enzyme Activation, pubmed-meshheading:9410884-Fibronectins, pubmed-meshheading:9410884-GTP Phosphohydrolases, pubmed-meshheading:9410884-GTP-Binding Proteins, pubmed-meshheading:9410884-Humans, pubmed-meshheading:9410884-Polymers, pubmed-meshheading:9410884-RNA, Antisense, pubmed-meshheading:9410884-Transfection, pubmed-meshheading:9410884-Transglutaminases
pubmed:year
1997
pubmed:articleTitle
Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin.
pubmed:affiliation
Department of Life Sciences, Nottingham Trent University, Nottingham, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't