Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-I

Yuh-Ling Chen, Inn Ho Tsai, Tse-Ming Hong, Shu Huei Tsai

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Pm-VEGF,a novel member ofVEGF family from the venom gland of Taiwan habu (Protobothrops mucrosquamatu), is a disulfide-linked homodimer with 119 amino acid residues. Recombinant fusion Pm-VEGF was expressed in Escherichia coli, purified and refolded. Surface plasmon resonance was used to determine its binding kinetics to VEGF-receptors (VEGFR). Relative to human VEGF165, the binding affinity of Pm-VEGF to the VEGFR-1 was 1.7-fold higher while affinity to theVEGFR-2 was 17-fold lower. But it did not bind the VEGFR-3 or neuropilin-1. Pm-VEGF promoted the proliferation and tissue factor production of endothelial cells, the neovascularization in the chicken chorioallantoic membrane, and increased vascular permeability. It also stimulated tissue-factor production and human monocyte chemotaxis, in accord with its specificity for VEGFR-1. Structural comparison among VEGF-proteins from various viper venoms revealed that the two subfamilies of vipers (Crotalinae and Viperinae) have evolved with distinct receptor-specificities for VEGFR-1 and VEGFR-2, respectively. Discussion on structure-activity relationships of the VEGFs further provided insight into residues important for the receptor-binding and specificities.

Original languageEnglish
Pages (from-to)331-338
Number of pages8
JournalThrombosis and Haemostasis
Volume93
Issue number2
DOIs
Publication statusPublished - 2005 Feb 1

Fingerprint

Crotalid Venoms
Vascular Endothelial Growth Factors
Vascular Endothelial Growth Factor Receptor
Vascular Endothelial Growth Factor A
Thromboplastin
Trimeresurus
Viper Venoms
Neuropilin-1
Chorioallantoic Membrane
Surface Plasmon Resonance
Venoms
Capillary Permeability
Chemotaxis
Structure-Activity Relationship
Viperidae
Taiwan
Disulfides
Monocytes
Chickens
Endothelial Cells

All Science Journal Classification (ASJC) codes

  • Hematology

Cite this

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title = "Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-I",
abstract = "Pm-VEGF,a novel member ofVEGF family from the venom gland of Taiwan habu (Protobothrops mucrosquamatu), is a disulfide-linked homodimer with 119 amino acid residues. Recombinant fusion Pm-VEGF was expressed in Escherichia coli, purified and refolded. Surface plasmon resonance was used to determine its binding kinetics to VEGF-receptors (VEGFR). Relative to human VEGF165, the binding affinity of Pm-VEGF to the VEGFR-1 was 1.7-fold higher while affinity to theVEGFR-2 was 17-fold lower. But it did not bind the VEGFR-3 or neuropilin-1. Pm-VEGF promoted the proliferation and tissue factor production of endothelial cells, the neovascularization in the chicken chorioallantoic membrane, and increased vascular permeability. It also stimulated tissue-factor production and human monocyte chemotaxis, in accord with its specificity for VEGFR-1. Structural comparison among VEGF-proteins from various viper venoms revealed that the two subfamilies of vipers (Crotalinae and Viperinae) have evolved with distinct receptor-specificities for VEGFR-1 and VEGFR-2, respectively. Discussion on structure-activity relationships of the VEGFs further provided insight into residues important for the receptor-binding and specificities.",
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Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-I. / Chen, Yuh-Ling; Tsai, Inn Ho; Hong, Tse-Ming; Tsai, Shu Huei.

In: Thrombosis and Haemostasis, Vol. 93, No. 2, 01.02.2005, p. 331-338.

Research output: Contribution to journalArticle

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