Selective Binding of Endostatin Peptide 4 to Recombinant VEGF Receptor 3 In Vitro.
Identifieur interne : 001581 ( Main/Exploration ); précédent : 001580; suivant : 001582Selective Binding of Endostatin Peptide 4 to Recombinant VEGF Receptor 3 In Vitro.
Auteurs : Kyu-Yeon Han ; Michael Chang ; Hong-Yu Ying ; Hyun Lee ; Yu-Hui Huang ; Jin-Hong Chang [États-Unis] ; Dimitri T. AzarSource :
- Protein and peptide letters [ 1875-5305 ] ; 2015.
Descripteurs français
- KwdFr :
- Collagène de type XVIII, Données de séquences moléculaires, Endostatines (), Endostatines (métabolisme), Liaison aux protéines, Protéines recombinantes (), Protéines recombinantes (métabolisme), Récepteur-3 au facteur croissance endothéliale vasculaire (), Récepteur-3 au facteur croissance endothéliale vasculaire (métabolisme), Séquence d'acides aminés.
- MESH :
- métabolisme : Endostatines, Protéines recombinantes, Récepteur-3 au facteur croissance endothéliale vasculaire.
- Collagène de type XVIII, Données de séquences moléculaires, Endostatines, Liaison aux protéines, Protéines recombinantes, Récepteur-3 au facteur croissance endothéliale vasculaire, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Collagen Type XVIII, Endostatins (chemistry), Endostatins (metabolism), Molecular Sequence Data, Protein Binding, Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), Vascular Endothelial Growth Factor Receptor-3 (chemistry), Vascular Endothelial Growth Factor Receptor-3 (metabolism).
- MESH :
- chemical , chemistry : Endostatins, Recombinant Proteins, Vascular Endothelial Growth Factor Receptor-3.
- chemical , metabolism : Endostatins, Recombinant Proteins, Vascular Endothelial Growth Factor Receptor-3.
- chemical : Collagen Type XVIII.
- Amino Acid Sequence, Molecular Sequence Data, Protein Binding.
Abstract
We previously reported that neostatin, a proteolytic fragment of collagen XVIII that includes endostatin, inhibits basic fibroblast growth factor-induced corneal angiogenesis and lymphangiogenesis. In experiments to determine which fragments in neostatin are responsible for binding to VEGF receptors (VEGFRs), we previously showed that a 28- mer sequence at the C-terminal of endostatin, known as endostatin peptide 9, preferentially binds VEGFR3-Fc over VEGFR1-Fc and VEGFR2-Fc. In the present study, we show that a different endostatin fragment, endostatin peptide 4 (26 mers long), also selectively binds VEGFR3-Fc and not VEGFR1-Fc or VEGFR2-Fc. From surface plasmon resonance data, the KD and Chi² (RU²) values for endostatin peptide 4 binding to VEGFR3-Fc are 5.72 × 10⁻⁸ M and 0.354, respectively. In conclusion, endostatin peptides 4 and 9 may be responsible for endostatin binding to VEGFR3-Fc, and this improved understanding of endostatin peptide binding to VEGFR3-Fc may support the development of therapeutics targeting lymphangiogenic processes.
DOI: 10.2174/0929866522666150907111953
PubMed: 26343062
Affiliations:
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Le document en format XML
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<author><name sortKey="Lee, Hyun" sort="Lee, Hyun" uniqKey="Lee H" first="Hyun" last="Lee">Hyun Lee</name>
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<author><name sortKey="Chang, Jin Hong" sort="Chang, Jin Hong" uniqKey="Chang J" first="Jin-Hong" last="Chang">Jin-Hong Chang</name>
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<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Vascular Endothelial Growth Factor Receptor-3 (chemistry)</term>
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<term>Liaison aux protéines</term>
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<term>Récepteur-3 au facteur croissance endothéliale vasculaire (métabolisme)</term>
<term>Séquence d'acides aminés</term>
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<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
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<term>Données de séquences moléculaires</term>
<term>Endostatines</term>
<term>Liaison aux protéines</term>
<term>Protéines recombinantes</term>
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<front><div type="abstract" xml:lang="en">We previously reported that neostatin, a proteolytic fragment of collagen XVIII that includes endostatin, inhibits basic fibroblast growth factor-induced corneal angiogenesis and lymphangiogenesis. In experiments to determine which fragments in neostatin are responsible for binding to VEGF receptors (VEGFRs), we previously showed that a 28- mer sequence at the C-terminal of endostatin, known as endostatin peptide 9, preferentially binds VEGFR3-Fc over VEGFR1-Fc and VEGFR2-Fc. In the present study, we show that a different endostatin fragment, endostatin peptide 4 (26 mers long), also selectively binds VEGFR3-Fc and not VEGFR1-Fc or VEGFR2-Fc. From surface plasmon resonance data, the KD and Chi² (RU²) values for endostatin peptide 4 binding to VEGFR3-Fc are 5.72 × 10⁻⁸ M and 0.354, respectively. In conclusion, endostatin peptides 4 and 9 may be responsible for endostatin binding to VEGFR3-Fc, and this improved understanding of endostatin peptide binding to VEGFR3-Fc may support the development of therapeutics targeting lymphangiogenic processes.</div>
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<name sortKey="Han, Kyu Yeon" sort="Han, Kyu Yeon" uniqKey="Han K" first="Kyu-Yeon" last="Han">Kyu-Yeon Han</name>
<name sortKey="Huang, Yu Hui" sort="Huang, Yu Hui" uniqKey="Huang Y" first="Yu-Hui" last="Huang">Yu-Hui Huang</name>
<name sortKey="Lee, Hyun" sort="Lee, Hyun" uniqKey="Lee H" first="Hyun" last="Lee">Hyun Lee</name>
<name sortKey="Ying, Hong Yu" sort="Ying, Hong Yu" uniqKey="Ying H" first="Hong-Yu" last="Ying">Hong-Yu Ying</name>
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<country name="États-Unis"><region name="Illinois"><name sortKey="Chang, Jin Hong" sort="Chang, Jin Hong" uniqKey="Chang J" first="Jin-Hong" last="Chang">Jin-Hong Chang</name>
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