Abstract:
:cDNA encoding VEGF and Ig-like extracellular domains 2-4 of VEGFR-1 (sFlt-1(2-4)) were cloned into prokaryotic expression vectors pET32a and pQE60. Recombinant proteins were purified (metal affinity chromatography) and renatured. Chemiluminescent study for the interaction of recombinant VEGF and sFlt-1(2-4) showed that biotinylated VEGF specifically binds to the polystyrene-immobilized receptor extracellular fragment. Biotinylated recombinant sFlt-1 interacts with immobilized VEGF. Analysis of the interaction of immobilized recombinant VEGFR-1 and VEGF with C6 glioma cells labeled with CFDA-SE (vital fluorescent dye) showed that recombinant VEGFR-1 also binds to native membrane-associated VEGF. Recombinant VEGF was shown to bind to specific receptors expressed on the surface of C6 glioma cells. Functional activity of these proteins was confirmed by ligand-receptor assay for VEGF and VEGFR-1 (sFlt-1) and quantitative chemiluminescent detection.
journal_name
Bull Exp Biol Medjournal_title
Bulletin of experimental biology and medicineauthors
Leopol'd AV,Baklaushev VP,Korchagina AA,Shein SA,Grinenko NF,Pavlov KA,Ryabukhin IA,Chekhonin VPdoi
10.1007/s10517-012-1612-0subject
Has Abstractpub_date
2012-04-01 00:00:00pages
707-11issue
6eissn
0007-4888issn
1573-8221journal_volume
152pub_type
杂志文章abstract::During left-ventricular myocardial ischemia, the decrease in the venous return is determined by reduction of cardiac output, which results from heart rate deceleration and decrease in left-ventricular stroke volume. The latter is related to a decrease in myocardial contractility and blood storage in the pulmonary circ...
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