Distinct architecture of lymphatic vessels induced by chimeric vascular endothelial growth factor-C/vascular endothelial growth factor heparin-binding domain fusion proteins.
Identifieur interne : 007297 ( Main/Exploration ); précédent : 007296; suivant : 007298Distinct architecture of lymphatic vessels induced by chimeric vascular endothelial growth factor-C/vascular endothelial growth factor heparin-binding domain fusion proteins.
Auteurs : Tuomas Tammela [Finlande] ; Yulong He ; Johannes Lyytikk ; Michael Jeltsch ; Johanna Markkanen ; Katri Pajusola ; Seppo Yl Herttuala ; Kari Alitalo [Finlande]Source :
- Circulation research [ 1524-4571 ] ; 2007.
Descripteurs français
- KwdFr :
- Adenoviridae (génétique), Animaux, Cellules cultivées, Facteur de croissance endothéliale vasculaire de type A (métabolisme), Facteur de croissance endothéliale vasculaire de type A (pharmacologie), Facteur de croissance endothéliale vasculaire de type C (métabolisme), Facteur de croissance endothéliale vasculaire de type C (pharmacologie), Humains, Héparine (métabolisme), Lymphangiogenèse (), Protéines de fusion recombinantes (métabolisme), Protéines de fusion recombinantes (pharmacologie), Récepteur-2 au facteur croissance endothéliale vasculaire (métabolisme), Récepteur-3 au facteur croissance endothéliale vasculaire (métabolisme), Sites de fixation, Souris, Vaisseaux lymphatiques ().
- MESH :
- génétique : Adenoviridae.
- métabolisme : Facteur de croissance endothéliale vasculaire de type A, Facteur de croissance endothéliale vasculaire de type C, Héparine, Protéines de fusion recombinantes, Récepteur-2 au facteur croissance endothéliale vasculaire, Récepteur-3 au facteur croissance endothéliale vasculaire.
- pharmacologie : Facteur de croissance endothéliale vasculaire de type A, Facteur de croissance endothéliale vasculaire de type C, Protéines de fusion recombinantes.
- Animaux, Cellules cultivées, Humains, Lymphangiogenèse, Sites de fixation, Souris, Vaisseaux lymphatiques.
English descriptors
- KwdEn :
- Adenoviridae (genetics), Animals, Binding Sites, Cells, Cultured, Heparin (metabolism), Humans, Lymphangiogenesis (drug effects), Lymphatic Vessels (drug effects), Mice, Recombinant Fusion Proteins (metabolism), Recombinant Fusion Proteins (pharmacology), Vascular Endothelial Growth Factor A (metabolism), Vascular Endothelial Growth Factor A (pharmacology), Vascular Endothelial Growth Factor C (metabolism), Vascular Endothelial Growth Factor C (pharmacology), Vascular Endothelial Growth Factor Receptor-2 (metabolism), Vascular Endothelial Growth Factor Receptor-3 (metabolism).
- MESH :
- chemical , metabolism : Heparin, Recombinant Fusion Proteins, Vascular Endothelial Growth Factor A, Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor Receptor-2, Vascular Endothelial Growth Factor Receptor-3.
- drug effects : Lymphangiogenesis, Lymphatic Vessels.
- genetics : Adenoviridae.
- chemical , pharmacology : Recombinant Fusion Proteins, Vascular Endothelial Growth Factor A, Vascular Endothelial Growth Factor C.
- Animals, Binding Sites, Cells, Cultured, Humans, Mice.
Abstract
Vascular endothelial growth factor (VEGF)-C and VEGF-D are composed of the receptor-binding VEGF homology domain and a carboxy-terminal silk homology domain that requires proteolytic cleavage for growth factor activation. Here, we explored whether the C-terminal heparin-binding domain of the VEGF(165) or VEGF(189) isoform also containing neuropilin-binding sequences could substitute for the silk homology domain of VEGF-C. Such VEGF-C/VEGF-heparin-binding domain chimeras were produced and shown to activate VEGF-C receptors, and, when expressed in tissues via adenovirus or adeno-associated virus vectors, stimulated lymphangiogenesis in vivo. However, both chimeras induced a distinctly different pattern of lymphatic vessels when compared with VEGF-C. Whereas VEGF-C-induced vessels were initially a dense network of small diameter vessels, the lymphatic vessels induced by the chimeric growth factors tended to form directly along tissue borders, along basement membranes that are rich in heparan sulfate. For example, in skeletal muscle, the chimeras induced formation of lumenized lymphatic vessels more efficiently than wild-type VEGF-C. We conclude that the matrix-binding domain of VEGF can target VEGF-C activity to heparin-rich basement membrane structures. These properties may prove useful for tissue engineering and attempts to regenerate lymphatic vessels in lymphedema patients.
DOI: 10.1161/01.RES.0000269043.51272.6d
PubMed: 17478733
Affiliations:
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Finland.</nlm:affiliation><country xml:lang="fr">Finlande</country><wicri:regionArea>Molecular/Cancer Biology Laboratory and Ludwig Institute for Cancer Research, Biomedicum Helsinki, the Haartman Institute and Helsinki University Central Hospital, University of Helsinki, Helsinki</wicri:regionArea><wicri:noRegion>Helsinki</wicri:noRegion></affiliation></author><author><name sortKey="He, Yulong" sort="He, Yulong" uniqKey="He Y" first="Yulong" last="He">Yulong He</name></author><author><name sortKey="Lyytikk, Johannes" sort="Lyytikk, Johannes" uniqKey="Lyytikk J" first="Johannes" last="Lyytikk">Johannes Lyytikk</name></author><author><name sortKey="Jeltsch, Michael" sort="Jeltsch, Michael" uniqKey="Jeltsch M" first="Michael" last="Jeltsch">Michael Jeltsch</name></author><author><name sortKey="Markkanen, Johanna" sort="Markkanen, Johanna" uniqKey="Markkanen J" first="Johanna" last="Markkanen">Johanna Markkanen</name></author><author><name sortKey="Pajusola, Katri" sort="Pajusola, Katri" 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Cultured</term><term>Heparin (metabolism)</term><term>Humans</term><term>Lymphangiogenesis (drug effects)</term><term>Lymphatic Vessels (drug effects)</term><term>Mice</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Recombinant Fusion Proteins (pharmacology)</term><term>Vascular Endothelial Growth Factor A (metabolism)</term><term>Vascular Endothelial Growth Factor A (pharmacology)</term><term>Vascular Endothelial Growth Factor C (metabolism)</term><term>Vascular Endothelial Growth Factor C (pharmacology)</term><term>Vascular Endothelial Growth Factor Receptor-2 (metabolism)</term><term>Vascular Endothelial Growth Factor Receptor-3 (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adenoviridae (génétique)</term><term>Animaux</term><term>Cellules cultivées</term><term>Facteur de croissance endothéliale vasculaire de type A (métabolisme)</term><term>Facteur de croissance endothéliale vasculaire de type A (pharmacologie)</term><term>Facteur de croissance endothéliale vasculaire de type C (métabolisme)</term><term>Facteur de croissance endothéliale vasculaire de type C (pharmacologie)</term><term>Humains</term><term>Héparine (métabolisme)</term><term>Lymphangiogenèse ()</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines de fusion recombinantes (pharmacologie)</term><term>Récepteur-2 au facteur croissance endothéliale vasculaire (métabolisme)</term><term>Récepteur-3 au facteur croissance endothéliale vasculaire (métabolisme)</term><term>Sites de fixation</term><term>Souris</term><term>Vaisseaux lymphatiques ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Heparin</term><term>Recombinant Fusion Proteins</term><term>Vascular Endothelial Growth Factor A</term><term>Vascular Endothelial Growth Factor C</term><term>Vascular Endothelial Growth Factor Receptor-2</term><term>Vascular Endothelial Growth Factor Receptor-3</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Lymphangiogenesis</term><term>Lymphatic Vessels</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Adenoviridae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Adenoviridae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur de croissance endothéliale vasculaire de type A</term><term>Facteur de croissance endothéliale vasculaire de type C</term><term>Héparine</term><term>Protéines de fusion recombinantes</term><term>Récepteur-2 au facteur croissance endothéliale vasculaire</term><term>Récepteur-3 au facteur croissance endothéliale vasculaire</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Facteur de croissance endothéliale vasculaire de type A</term><term>Facteur de croissance endothéliale vasculaire de type C</term><term>Protéines de fusion recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Recombinant Fusion Proteins</term><term>Vascular Endothelial Growth Factor A</term><term>Vascular Endothelial Growth Factor C</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cells, Cultured</term><term>Humans</term><term>Mice</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules cultivées</term><term>Humains</term><term>Lymphangiogenèse</term><term>Sites de fixation</term><term>Souris</term><term>Vaisseaux lymphatiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Vascular endothelial growth factor (VEGF)-C and VEGF-D are composed of the receptor-binding VEGF homology domain and a carboxy-terminal silk homology domain that requires proteolytic cleavage for growth factor activation. Here, we explored whether the C-terminal heparin-binding domain of the VEGF(165) or VEGF(189) isoform also containing neuropilin-binding sequences could substitute for the silk homology domain of VEGF-C. Such VEGF-C/VEGF-heparin-binding domain chimeras were produced and shown to activate VEGF-C receptors, and, when expressed in tissues via adenovirus or adeno-associated virus vectors, stimulated lymphangiogenesis in vivo. However, both chimeras induced a distinctly different pattern of lymphatic vessels when compared with VEGF-C. Whereas VEGF-C-induced vessels were initially a dense network of small diameter vessels, the lymphatic vessels induced by the chimeric growth factors tended to form directly along tissue borders, along basement membranes that are rich in heparan sulfate. For example, in skeletal muscle, the chimeras induced formation of lumenized lymphatic vessels more efficiently than wild-type VEGF-C. We conclude that the matrix-binding domain of VEGF can target VEGF-C activity to heparin-rich basement membrane structures. These properties may prove useful for tissue engineering and attempts to regenerate lymphatic vessels in lymphedema patients.</div></front></TEI><affiliations><list><country><li>Finlande</li></country><region><li>Uusimaa</li></region><settlement><li>Helsinki</li></settlement><orgName><li>Université d'Helsinki</li></orgName></list><tree><noCountry><name sortKey="He, Yulong" sort="He, Yulong" uniqKey="He Y" first="Yulong" last="He">Yulong He</name><name sortKey="Jeltsch, Michael" sort="Jeltsch, Michael" uniqKey="Jeltsch M" first="Michael" last="Jeltsch">Michael Jeltsch</name><name sortKey="Lyytikk, Johannes" sort="Lyytikk, Johannes" uniqKey="Lyytikk J" first="Johannes" last="Lyytikk">Johannes Lyytikk</name><name sortKey="Markkanen, Johanna" sort="Markkanen, Johanna" uniqKey="Markkanen J" first="Johanna" last="Markkanen">Johanna Markkanen</name><name sortKey="Pajusola, Katri" sort="Pajusola, Katri" uniqKey="Pajusola K" first="Katri" last="Pajusola">Katri Pajusola</name><name sortKey="Yl Herttuala, Seppo" sort="Yl Herttuala, Seppo" uniqKey="Yl Herttuala S" first="Seppo" last="Yl Herttuala">Seppo Yl Herttuala</name></noCountry><country name="Finlande"><noRegion><name sortKey="Tammela, Tuomas" sort="Tammela, Tuomas" uniqKey="Tammela T" first="Tuomas" last="Tammela">Tuomas Tammela</name></noRegion><name sortKey="Alitalo, Kari" sort="Alitalo, Kari" uniqKey="Alitalo K" first="Kari" last="Alitalo">Kari Alitalo</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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