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VEGF-A is a glycoprotein, which belongs to the vascular endothelial growth factor family. The human VEGF-A gene is composed of 8 exons, separated by 7 introns and is localized in chromosome 6p21.3. Alternative exon splicing of a single VEGF gene results in the generation of the ten different isoforms known as 121, 138, 145, 148, 162, 162b, 165, 183, 189 and 206. VEGF-A binds to two tyrosine kinase receptors Flt-1 and Flk-1. Activation of the receptors leads to a rapid recruitment of the adaptor proteins Shc, Grb2, Nic, Nck, Crk, protein tyrosine phosphatases SHP-1 i SHP-2 as well as Akt/PKB serine/threonine kinase, phospholipase Cγ (PLCγ), focal adhesion kinase FAK and PI-3 kinase. Oxygen tension is a key regulator of VEGF gene expression. Hypoxia-inducible transcription of VEGF is media- ted, at least in part, by the binding of hypoxia-inducible factor 1 HIF-1 to an HIF-1 binding site located in the VEGF promoter. VEGF-A plays very important roles in the organism of which angiogenesis is the most significant. The understanding of the mechanisms of angiogenesis can create the basis of new methods of treatment of some diseases with accompanying angiogenesis disturbances, such as antiangio- genic cancer therapy, and therapeutic angiogenesis in case of cardiac, brain and limb ischemia.

The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

Editorial address:
Katedra i Zakład Histologii i Embriologii Uniwersytetu Medycznego w Poznaniu, ul. Święcickiego 6, 60-781 Poznań, tel. +48 61 8546453, fax. +48 61 8546440, email:

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