Document Detail


Fluorescent Resonance Energy Transfer Imaging of VEGFR Dimerization.
MedLine Citation:
PMID:  24778014     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Activation of vascular endothelial growth factor receptor 1 (VEGFR1/FLT1) and 2 (VEGFR2/KDR) involves receptor dimerization. Formation of VEGFR dimer has so far not been visualized in single intact cells. In the present study we describe different optical assays which can be used to observe dimerization of VEGFR1 and VEGFR2. Bimolecular fluorescence complementation (BIFC) assays confirmed homo,- and heterodimerization of transfected receptors. Fluorescence resonance energy transfer (FRET) techniques in living and fixed CHO-K1 cells allowed observation of VEGFR1 homodimer,- and VEGFR1 and VEGFR2 heterodimer formation after ligand stimulation. After inhibition of ligand binding by the VEGFA JH121 antibody VEGFR1 homodimerization was completely abolished. Under the same conditions, cells transfected by VEGFR1 and VEGFR2 maintained relevant receptor heterodimerization. These techniques to monitor VEGFR1 and VEGFR2 homo- and heterodimerization in living and fixed cells may help in the search for new angiogenesis-directed inhibitors of VEGFR dimerization.
Authors:
Zhala Ahmadova; Vugar Yagublu; Tassilo Förg; Yegana Hajiyeva; Ralf Jesenofsky; Mathias Hafner; Michael Keese
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Anticancer research     Volume:  34     ISSN:  1791-7530     ISO Abbreviation:  Anticancer Res.     Publication Date:  2014 May 
Date Detail:
Created Date:  2014-04-29     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8102988     Medline TA:  Anticancer Res     Country:  Greece    
Other Details:
Languages:  eng     Pagination:  2123-33     Citation Subset:  IM    
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