|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2005-1-24
|
|
pubmed:abstractText |
A natural fragment of an enzyme that catalyzes the first step of protein synthesis-human tryptophanyl-tRNA synthetase (T2-TrpRS) has potent anti-angiogenic activity. A cellular receptor through which T2-TrpRS exerts its anti-angiogenic activity has not previously been identified. Here T2-TrpRS was shown to bind at intercellular junctions of endothelial cells (ECs). Using genetic knock-outs, binding was established to depend on VE-cadherin, a calcium-dependent adhesion molecule, which is selectively expressed in ECs, concentrated at adherens junctions, and is essential for normal vascular development. In contrast, T2-TrpRS binding to EC junctions was not dependent on platelet endothelial cell adhesion molecule type-1, another adhesion molecule found at EC junctions. Pull-down assays confirmed direct complex formation between T2-TrpRS and VE-cadherin. Binding of T2-TrpRS inhibited VEGF-induced ERK activation and EC migration. Thus, a VE-cadherin-dependent pathway is proposed to link T2-TrpRS to inhibition of new blood vessel formation.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acyl-tRNA Synthetases,
http://linkedlifedata.com/resource/pubmed/chemical/Angiogenesis Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokines,
http://linkedlifedata.com/resource/pubmed/chemical/Extracellular Signal-Regulated MAP...,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan-tRNA Ligase,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A,
http://linkedlifedata.com/resource/pubmed/chemical/cadherin 5
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
28
|
|
pubmed:volume |
280
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2405-8
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:15579907-Amino Acyl-tRNA Synthetases,
pubmed-meshheading:15579907-Angiogenesis Inhibitors,
pubmed-meshheading:15579907-Animals,
pubmed-meshheading:15579907-Antigens, CD,
pubmed-meshheading:15579907-Aorta,
pubmed-meshheading:15579907-Blotting, Western,
pubmed-meshheading:15579907-Cadherins,
pubmed-meshheading:15579907-Cattle,
pubmed-meshheading:15579907-Cell Movement,
pubmed-meshheading:15579907-Cells, Cultured,
pubmed-meshheading:15579907-Cytokines,
pubmed-meshheading:15579907-Endothelium, Vascular,
pubmed-meshheading:15579907-Enzyme Activation,
pubmed-meshheading:15579907-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:15579907-Gap Junctions,
pubmed-meshheading:15579907-Green Fluorescent Proteins,
pubmed-meshheading:15579907-Immunoprecipitation,
pubmed-meshheading:15579907-Microscopy, Confocal,
pubmed-meshheading:15579907-Microscopy, Fluorescence,
pubmed-meshheading:15579907-Neovascularization, Pathologic,
pubmed-meshheading:15579907-Protein Binding,
pubmed-meshheading:15579907-Recombinant Proteins,
pubmed-meshheading:15579907-Signal Transduction,
pubmed-meshheading:15579907-Tryptophan-tRNA Ligase,
pubmed-meshheading:15579907-Vascular Endothelial Growth Factor A
|
|
pubmed:year |
2005
|
|
pubmed:articleTitle |
VE-cadherin links tRNA synthetase cytokine to anti-angiogenic function.
|
|
pubmed:affiliation |
Skaggs Institute for Chemical Biology, Department of Chemistry and Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA. etzima@scripps.edu
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
