Localization of heparin- and neuropilin-1-recognition sites of viral VEGFs |
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Authors: | Tokunaga Yuko Yamazaki Yasuo Morita Takashi |
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Institution: | Department of Biochemistry, Meiji Pharmaceutical University, 2-522-1, Noshio, Kiyose, Tokyo 204-8588, Japan. |
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Abstract: | VEGF-A165 plays a central role in neovascularization. The biological activities of VEGF-A165 are largely mediated through KDR. VEGF-A165 also binds to cellular coreceptors, neuropilin-1 (NP-1), and heparin, via its C-terminal domain, resulting in functional modulation. Parapoxvirus-encoded VEGFs (PV-VEGFs), which recognize KDR, possess basic amino acid clusters in their C-terminal regions. Some PV-VEGFs may interact with NP-1; however, the NP-1- and heparin-binding properties have not been fully characterized. Here, we demonstrate that the heparin- and NP-1-binding region of PV-VEGFs is located in its C-terminal tail. Furthermore, the two arginine residues adjacent to the C-terminus greatly contribute to both interactions. |
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Keywords: | VEGF Viral VEGF Heparin Neuropilin-1 Parapoxvirus Synthetic peptide |
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