Document Detail

Vascular endothelial growth factor stimulates dephosphorylation of the catenins p120 and p100 in endothelial cells.
MedLine Citation:
PMID:  10657259     Owner:  NLM     Status:  MEDLINE    
Vascular endothelial growth factor (VEGF) is an endothelium-specific mitogen that induces angiogenesis and increases vascular permeability. These processes involve regulation of cell-cell adhesion, but molecular mechanisms have yet to be fully established. p120, also termed p120(ctn), and its variant p100 are catenins which associate with cadherins and localize to adherens junctions. VEGF was reported to stimulate tyrosine phosphorylation of catenins in endothelial cells. In contrast, we have found that VEGF potently stimulated a rapid and dose-dependent decrease in serine/threonine phosphorylation of p120 and p100. VEGF acted via VEGF receptor 2 to achieve this effect which was independent of activation of the extracellular-signal-regulated kinase pathway. Histamine and activators of protein kinase C had a very similar effect to that of VEGF on phosphorylation of p120 and p100, suggesting that these diverse stimuli may converge on a common signalling element regulating p120/p100 serine/threonine phosphorylation. These data raise the possibility that the dephosphorylation of p120 and p100 triggered by VEGF may contribute to mechanisms regulating permeability and/or motility through modulation of cadherin adhesiveness.
E Y Wong; L Morgan; C Smales; P Lang; S E Gubby; J M Staddon
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  346 Pt 1     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  2000 Feb 
Date Detail:
Created Date:  2000-03-30     Completed Date:  2000-03-30     Revised Date:  2010-01-29    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  209-16     Citation Subset:  IM    
Eisai London Research Laboratories Ltd., Bernard Katz Building, University College London, Gower Street, London WC1E 6BT, U.K.
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MeSH Terms
Cadherins / metabolism
Cell Adhesion Molecules / chemistry*,  genetics,  metabolism*
Cells, Cultured
Dose-Response Relationship, Drug
Electrophoresis, Polyacrylamide Gel
Endothelial Growth Factors / pharmacology*
Endothelium, Vascular / cytology,  drug effects*,  enzymology,  metabolism
Enzyme Activation / drug effects
Genetic Variation / genetics
Histidine / pharmacology
Lymphokines / pharmacology*
Mitogen-Activated Protein Kinases / metabolism
Molecular Weight
Peptide Mapping
Phorbol 12,13-Dibutyrate / pharmacology
Phosphoamino Acids / metabolism
Phosphoproteins / chemistry*,  genetics,  metabolism*
Phosphorylation / drug effects
Precipitin Tests
Protein Kinase C / metabolism
Receptor Protein-Tyrosine Kinases / metabolism
Receptors, Growth Factor / metabolism
Receptors, Vascular Endothelial Growth Factor
Signal Transduction / drug effects
Vascular Endothelial Growth Factor A
Vascular Endothelial Growth Factors
Reg. No./Substance:
0/Cadherins; 0/Cell Adhesion Molecules; 0/Endothelial Growth Factors; 0/Lymphokines; 0/Phosphoamino Acids; 0/Phosphoproteins; 0/Receptors, Growth Factor; 0/Vascular Endothelial Growth Factor A; 0/Vascular Endothelial Growth Factors; 0/delta catenin; 37558-16-0/Phorbol 12,13-Dibutyrate; 71-00-1/Histidine; EC Protein-Tyrosine Kinases; EC, Vascular Endothelial Growth Factor; EC Kinase C; EC Protein Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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