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Biochimie. 2015 Sep;116:1-7. doi: 10.1016/j.biochi.2015.06.011. Epub 2015 Jun 21.

Vascular endothelial growth factor from Trimeresurus jerdonii venom specifically binds to VEGFR-2.

Author information

1
Department of Forensic Biology, School of Forensic Medicine, Kunming Medical University, Kunming, Yunnan 650500, China.
2
Key Laboratory of Animal Models and Human Disease Mechanism of the Chinese Academy of Science & Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China.
3
Department of Biochemistry, Cangzhou Medical College, Cangzhou, Hebei 061001, China.
4
Key Laboratory of Animal Models and Human Disease Mechanism of the Chinese Academy of Science & Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China; Jointed Laboratory of Natural Bioactive Peptide of Kunming Institute of Zoology, Chinese Academy of Science & University of Science and Technology of China, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China.
5
Key Laboratory of Animal Models and Human Disease Mechanism of the Chinese Academy of Science & Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China; Jointed Laboratory of Natural Bioactive Peptide of Kunming Institute of Zoology, Chinese Academy of Science & University of Science and Technology of China, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China. Electronic address: lvqm@mail.kiz.ac.cn.
6
Key Laboratory of Animal Models and Human Disease Mechanism of the Chinese Academy of Science & Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China; Jointed Laboratory of Natural Bioactive Peptide of Kunming Institute of Zoology, Chinese Academy of Science & University of Science and Technology of China, Kunming Institute of Zoology, Chinese Academy of Science, Kunming, Yunnan 650223, China. Electronic address: rlai@mail.kiz.ac.cn.

Abstract

Vascular endothelial growth factors (VEGFs) play important roles in angiogenesis. In this study, a vascular endothelial growth factor named TjsvVEGF was purified from the venom of Trimeresurus jerdonii by gel filtration, affinity, ion-exchange and high-performance liquid chromatography. TjsvVEGF was a homodimer with an apparent molecular mass of 29 kDa. The cDNA encoding TjsvVEGF was obtained by PCR. The open reading frame of the cloned TjsvVEGF was composed of 432 bp coding for a signal peptide of 24 amino acid residues and a mature protein of 119 amino acid residues. Compared with other snake venom VEGFs, the nucleotide and deduced protein sequences of the cloned TjsvVEGF were conserved. TjsvVEGF showed low heparin binding activity and strong capillary permeability increasing activity. The KD of TjsvVEGF to VEFGR-2 is 413 pM. However, the binding of TjsvVEGF to VEGFR-1 is too weak to detect. Though TjsvVEGF had high sequence identities (about 90%) with Crotalinae VEGFs, the receptor preference of TjsvVEGF was similar to Viperinae VEGFs which had lower sequence identities (about 60%) with it. TjsvVEGF might serve as a useful tool for the study of structure-function relationships of VEGFs and their receptors.

KEYWORDS:

Molecular cloning; Purification; Trimeresurus jerdonii; VEGFR; Vascular endothelial growth factor

PMID:
26107411
DOI:
10.1016/j.biochi.2015.06.011
[Indexed for MEDLINE]

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