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M212224200v1
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Papers In Press, published online ahead of print February 21, 2003
J. Biol. Chem, 10.1074/jbc.M212224200
Submitted on December 2, 2002
Revised on February 21, 2003
Accepted on February 21, 2003

VEGF162 : A new heparin binding VEGF splice form that is expressed in transformed human cells

Tali Lange, Noga Gutman-Raviv, Limor Baruch, Marcelle Machluf, and Gera Neufeld

Department of Cell biology and Anatomy, Technion, Israel Institute of Technology, Haifa 31096

Corresponding Author: gera{at}tx.technion.ac.il

The splice forms of vascular endothelial growth factor (VEGF) differ in biological properties such as the receptor types which they recognize and their interaction with heparan sulfate proteoglycans. We have identified a new VEGF mRNA splice form encoding a VEGF species containing 162 amino-acids (VEGF162) in human A431 ovarian carcinoma cells. This novel mRNA contains the peptides encoded by exons 1-5, 6A, 6B and 8 of the VEGF gene. Recombinant VEGF162 is biologically active. It induces proliferation of endothelial cells in-vitro and angiogenesis in-vivo as determined by the alginate beads assay. VEGF162 binds less efficiently than VEGF145, but more efficiently than VEGF165, to a natural basement membrane produced by corneal endothelial cells. VEGF138, an artificial VEGF form that contains exon 6B but lacks exons 6A and 7, did not bind to this basement membrane at all indicating that exon-6b probably interferes with the interaction of exon-6A with heparin and heparan sulfate proteoglycans.


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