Priority of the Discovery

F t Biotechnology discovery Fu

Citation: Wang Q, Li T, Wu Z, Wu Q, Ke X, Luo D, et al. (2013) Novel VEGF Decoy Receptor Fusion Protein Conbercept Targeting Multiple VEGF Isoforms Provide Remarkable Anti-Angiogenesis Effect In Vivo. PLoS ONE 8(8): e70544. doi:10.1371/journal.pone.0070544

Editor: Bhaskar Saha, National Center for Cell Science, India

Copyright: © 2013 Wang et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Funding: The authors are thankful for support from the National Natural Science Foundation of China (grant Nos. 81072677 and 31201352), the National Basic Research Program of China (973 Program No. 2011CB510200), and the National Grand Program of China (2008 ZX10004-015). The funders had no role in the design of experiments, data collection and analysis, decision to publish, or preparation of the paper.

Competing interests: All authors of the paper declare that there are no competing commercial interests in relation to the present work. Although one or more of the authors are employed by Chengdu Kanghong Biotechnology Co. Ltd., this does not alter the authors' adherence to all of the PLOS ONE policies on sharing data and materials.

Introduction

The pathological angiogenesis is a critical hallmark of human diseases such as the cancer and the wet form of age-related macular degeneration (AMD) – the leading cause of blindness in the elderly population. Compelling evidences have demonstrated that vascular endothelial growth factor (VEGF) plays a pivotal role in the abnormal angiogenesis process . Therefore VEGF has become a key target in antiangiogenic therapy . There are five members in VEGF family: VEGF-A, -B, -C, -D and placental growth factor (PlGF) . Among them, VEGF-A is the first discovered and the most well-studied member . Alternative exon splicing and proteolytic cleavage generated several distinct VEGF-A isoforms, respectively named VEGF121, VEGF165, and VEGF162. VEGF-A isoforms are all active as dimers, differing principally in their size and ability to bind heparin or neuropilins. Isoforms of VEGF-B and PlGF, which differ in their capacity to bind heparin, are also produced by alternative splicing.

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