Source:http://linkedlifedata.com/resource/pubmed/id/15711751
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2005-2-15
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| pubmed:databankReference | |
| pubmed:abstractText |
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 toVEGF-receptors (VEGFR). Relative to human VEGF165, the binding affinity of Pm-VEGF to the VEGFR-1 was 1.7-fold higher while affinity to the VEGFR-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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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Crotalid Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/Thromboplastin,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor A,
http://linkedlifedata.com/resource/pubmed/chemical/Vascular Endothelial Growth Factor...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0340-6245
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
93
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
331-8
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:15711751-Amino Acid Sequence,
pubmed-meshheading:15711751-Animals,
pubmed-meshheading:15711751-Cells, Cultured,
pubmed-meshheading:15711751-Chemotaxis, Leukocyte,
pubmed-meshheading:15711751-Cloning, Molecular,
pubmed-meshheading:15711751-Crotalid Venoms,
pubmed-meshheading:15711751-Endothelium, Vascular,
pubmed-meshheading:15711751-Humans,
pubmed-meshheading:15711751-Kinetics,
pubmed-meshheading:15711751-Molecular Sequence Data,
pubmed-meshheading:15711751-Monocytes,
pubmed-meshheading:15711751-Neovascularization, Physiologic,
pubmed-meshheading:15711751-Protein Binding,
pubmed-meshheading:15711751-Sequence Alignment,
pubmed-meshheading:15711751-Surface Plasmon Resonance,
pubmed-meshheading:15711751-Thromboplastin,
pubmed-meshheading:15711751-Umbilical Veins,
pubmed-meshheading:15711751-Vascular Endothelial Growth Factor A,
pubmed-meshheading:15711751-Vascular Endothelial Growth Factor Receptor-1
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| pubmed:year |
2005
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| pubmed:articleTitle |
Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-1. Characterization of Protobothrops mucrosquamatus venom VEGF.
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| pubmed:affiliation |
Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan, Republic of China.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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