Serveur d'exploration Chloroquine

Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.

Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects

Identifieur interne : 002F69 ( Main/Exploration ); précédent : 002F68; suivant : 002F70

Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects

Auteurs : A. Bikfalvi [France, États-Unis] ; C. Sauzeau [France] ; H. Moukadiri [France] ; J. Maclouf [France] ; N. Busso [France] ; M. Bryckaert [France] ; J. Plouet [France] ; G. Tobelem [France]

Source :

RBID : ISTEX:D65D97CC8479F9BF9489CDDB588AF8E067E434AA

English descriptors

Abstract

Vasculotropin/vascular endothelial cell growth factor (VAS/VEGF) is a newly purified growth factor with a unique specificity for vascular endothelial cells. We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). 125I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (KD = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of 125I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with 125I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced 125I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. 125I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of 125I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. The angiogenic activity seems to be independent of the plasminogen activator or inhibitor system.

Url:
DOI: 10.1002/jcp.1041490108


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

<record>
<TEI wicri:istexFullTextTei="biblStruct">
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en">Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects</title>
<author>
<name sortKey="Bikfalvi, A" sort="Bikfalvi, A" uniqKey="Bikfalvi A" first="A." last="Bikfalvi">A. Bikfalvi</name>
</author>
<author>
<name sortKey="Sauzeau, C" sort="Sauzeau, C" uniqKey="Sauzeau C" first="C." last="Sauzeau">C. Sauzeau</name>
</author>
<author>
<name sortKey="Moukadiri, H" sort="Moukadiri, H" uniqKey="Moukadiri H" first="H." last="Moukadiri">H. Moukadiri</name>
</author>
<author>
<name sortKey="Maclouf, J" sort="Maclouf, J" uniqKey="Maclouf J" first="J." last="Maclouf">J. Maclouf</name>
</author>
<author>
<name sortKey="Busso, N" sort="Busso, N" uniqKey="Busso N" first="N." last="Busso">N. Busso</name>
</author>
<author>
<name sortKey="Bryckaert, M" sort="Bryckaert, M" uniqKey="Bryckaert M" first="M." last="Bryckaert">M. Bryckaert</name>
</author>
<author>
<name sortKey="Plouet, J" sort="Plouet, J" uniqKey="Plouet J" first="J." last="Plouet">J. Plouet</name>
</author>
<author>
<name sortKey="Tobelem, G" sort="Tobelem, G" uniqKey="Tobelem G" first="G." last="Tobelem">G. Tobelem</name>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:D65D97CC8479F9BF9489CDDB588AF8E067E434AA</idno>
<date when="1991" year="1991">1991</date>
<idno type="doi">10.1002/jcp.1041490108</idno>
<idno type="url">https://api.istex.fr/ark:/67375/WNG-CDHTF6T2-B/fulltext.pdf</idno>
<idno type="wicri:Area/Istex/Corpus">000994</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000994</idno>
<idno type="wicri:Area/Istex/Curation">000994</idno>
<idno type="wicri:Area/Istex/Checkpoint">001D40</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001D40</idno>
<idno type="wicri:doubleKey">0021-9541:1991:Bikfalvi A:interaction:of:vasculotropin</idno>
<idno type="wicri:Area/Main/Merge">003036</idno>
<idno type="wicri:Area/Main/Curation">002F69</idno>
<idno type="wicri:Area/Main/Exploration">002F69</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title level="a" type="main">Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects</title>
<author>
<name sortKey="Bikfalvi, A" sort="Bikfalvi, A" uniqKey="Bikfalvi A" first="A." last="Bikfalvi">A. Bikfalvi</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 150, Hopital Lariboisière, 75010 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
<affiliation wicri:level="2">
<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Current Address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York</wicri:cityArea>
</affiliation>
<affiliation wicri:level="2">
<country xml:lang="fr">États-Unis</country>
<placeName>
<region type="state">État de New York</region>
</placeName>
<wicri:cityArea>Correspondence address: Department of Cell Biology, New York University Medical Center, 550 First Avenue, New York</wicri:cityArea>
</affiliation>
</author>
<author>
<name sortKey="Sauzeau, C" sort="Sauzeau, C" uniqKey="Sauzeau C" first="C." last="Sauzeau">C. Sauzeau</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 150, Hopital Lariboisière, 75010 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Moukadiri, H" sort="Moukadiri, H" uniqKey="Moukadiri H" first="H." last="Moukadiri">H. Moukadiri</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 86, Centre des Cordeliers, 75006 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
<affiliation wicri:level="1">
<country xml:lang="fr">France</country>
<wicri:regionArea>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse</wicri:regionArea>
<placeName>
<settlement type="city">Toulouse</settlement>
<region type="region" nuts="2">Occitanie (région administrative)</region>
<region type="old region" nuts="2">Midi-Pyrénées</region>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Maclouf, J" sort="Maclouf, J" uniqKey="Maclouf J" first="J." last="Maclouf">J. Maclouf</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 150, Hopital Lariboisière, 75010 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Busso, N" sort="Busso, N" uniqKey="Busso N" first="N." last="Busso">N. Busso</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>Laboratoires Glaxo, 91940 Les Ulis</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Les Ulis</settlement>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Bryckaert, M" sort="Bryckaert, M" uniqKey="Bryckaert M" first="M." last="Bryckaert">M. Bryckaert</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 150, Hopital Lariboisière, 75010 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Plouet, J" sort="Plouet, J" uniqKey="Plouet J" first="J." last="Plouet">J. Plouet</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 86, Centre des Cordeliers, 75006 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
<affiliation wicri:level="1">
<country xml:lang="fr">France</country>
<wicri:regionArea>Current Address: ATIP, Centre de Recherches en Biochimie et Genetique Cellulaire, 114 route de Narbonne, 3100 Toulouse</wicri:regionArea>
<placeName>
<settlement type="city">Toulouse</settlement>
<region type="region" nuts="2">Occitanie (région administrative)</region>
<region type="old region" nuts="2">Midi-Pyrénées</region>
</placeName>
</affiliation>
</author>
<author>
<name sortKey="Tobelem, G" sort="Tobelem, G" uniqKey="Tobelem G" first="G." last="Tobelem">G. Tobelem</name>
<affiliation wicri:level="3">
<country xml:lang="fr">France</country>
<wicri:regionArea>INSERM U 150, Hopital Lariboisière, 75010 Paris</wicri:regionArea>
<placeName>
<region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Paris</settlement>
</placeName>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series>
<title level="j" type="main">Journal of Cellular Physiology</title>
<title level="j" type="alt">JOURNAL OF CELLULAR PHYSIOLOGY</title>
<idno type="ISSN">0021-9541</idno>
<idno type="eISSN">1097-4652</idno>
<imprint>
<biblScope unit="vol">149</biblScope>
<biblScope unit="issue">1</biblScope>
<biblScope unit="page" from="50">50</biblScope>
<biblScope unit="page" to="59">59</biblScope>
<biblScope unit="page-count">10</biblScope>
<publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher>
<pubPlace>Hoboken</pubPlace>
<date type="published" when="1991-10">1991-10</date>
</imprint>
<idno type="ISSN">0021-9541</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt>
<idno type="ISSN">0021-9541</idno>
</seriesStmt>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="Teeft" xml:lang="en">
<term>Acad</term>
<term>Acidic</term>
<term>Acidic wash</term>
<term>Activator</term>
<term>Amino acids</term>
<term>Angiogenesis</term>
<term>Angiogenic</term>
<term>Assay</term>
<term>Basic fibroblast growth factor</term>
<term>Bfgf</term>
<term>Bikfalvi</term>
<term>Binding sites</term>
<term>Biol</term>
<term>Bovine</term>
<term>Bovine capillary</term>
<term>Cell biol</term>
<term>Cell growth factor</term>
<term>Cell surface binding</term>
<term>Chloroquine</term>
<term>Collagen type</term>
<term>Connolly</term>
<term>Degradation</term>
<term>Degraded</term>
<term>Endothelial</term>
<term>Endothelial cell mitogen</term>
<term>Endothelial cells</term>
<term>Fibroblast</term>
<term>Gospodarowicz</term>
<term>Growth factor</term>
<term>Growth factors</term>
<term>Heparin</term>
<term>Human umbilical vein</term>
<term>Huve</term>
<term>Huve cells</term>
<term>Incubation medium</term>
<term>Inhibitor</term>
<term>Internalization</term>
<term>Ligand</term>
<term>Montesano</term>
<term>Moukadiri</term>
<term>Natl</term>
<term>Ngiml</term>
<term>Orci</term>
<term>Physiol</term>
<term>Plasminogen</term>
<term>Plasminogen activator</term>
<term>Plasminogen activators</term>
<term>Plouet</term>
<term>Proc</term>
<term>Procoagulant</term>
<term>Procoagulant activity</term>
<term>Prostacyclin</term>
<term>Prostacyclin production</term>
<term>Protamin</term>
<term>Radioactivity</term>
<term>Receptor</term>
<term>Tissue factor</term>
<term>Total radioactivity</term>
<term>Umbilical</term>
<term>Unlabeled</term>
<term>Unlabeled ligand</term>
<term>Unstimulated control</term>
<term>Vascular permeability factor</term>
<term>Vasculotropin</term>
<term>Vasculotropin effect</term>
<term>Vasi vegf</term>
<term>Vasivegf</term>
<term>Vegf</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">Vasculotropin/vascular endothelial cell growth factor (VAS/VEGF) is a newly purified growth factor with a unique specificity for vascular endothelial cells. We have investigated the interactions of VAS/VEGF with human umbilical vein endothelial cells (HUVE cells). 125I‐VAS/VEGF was bound to HUVE cells in a saturable manner with a half‐maximum binding at 2.8 ng/ml. Scatchard analysis did show two classes of high‐affinity binding sites. The first class displayed a dissociation constant of 9 pM with 500 sites/cell. The dissociation constant and the number of binding sites of the second binding class were variable for different HUVE cell cultures (KD = 179 ± 101 pM, 5,850 ± 2,950 sites/cell). Half‐maximal inhibition of 125I‐VAS/VEGF occurred with a threefold excess of unlabeled ligand. Basic fibroblast growth factor (bFGF) and heparin did not compete with 125I‐VAS/VEGF binding. In contrast, suramin and protamin sulfate completely displaced 125I‐VAS/VEGF binding from HUVE cells. VAS/VEGF was shown to be internalized in HUVE cells. Maximum internalization (55% of total cell‐associated radioactivity) was observed after 30 min. 125I‐VAS/VEGF was completely degraded 2–3 hr after binding. At 3 hr, the trichloroacetic acid (TCA)‐soluble radioactivity accumulated in the medium was 60% of the total radioactivity released by HUVE cells. No degradation fragment of 125I‐VAS/VEGF was observed. Chloroquine completely inhibited degradation. VAS/VEGF was able to induce angiogenesis in vitro in HUVE cells. However, it did not significantly modulate urokinase‐type plasminogen activator (u‐PA), tissue‐type plasminogen activator (t‐PA), plasminogen activator inhibitor (PAI‐1), and tissue factor (TF). Prostacyclin production was only stimulated at very high VAS/VEGF concentrations. Taken together, these results indicate that VAS/VEGF might be a potent inducer of neovascularization resulting from a direct interaction with endothelial cells. The angiogenic activity seems to be independent of the plasminogen activator or inhibitor system.</div>
</front>
</TEI>
<affiliations>
<list>
<country>
<li>France</li>
<li>États-Unis</li>
</country>
<region>
<li>Midi-Pyrénées</li>
<li>Occitanie (région administrative)</li>
<li>État de New York</li>
<li>Île-de-France</li>
</region>
<settlement>
<li>Les Ulis</li>
<li>Paris</li>
<li>Toulouse</li>
</settlement>
</list>
<tree>
<country name="France">
<region name="Île-de-France">
<name sortKey="Bikfalvi, A" sort="Bikfalvi, A" uniqKey="Bikfalvi A" first="A." last="Bikfalvi">A. Bikfalvi</name>
</region>
<name sortKey="Bryckaert, M" sort="Bryckaert, M" uniqKey="Bryckaert M" first="M." last="Bryckaert">M. Bryckaert</name>
<name sortKey="Busso, N" sort="Busso, N" uniqKey="Busso N" first="N." last="Busso">N. Busso</name>
<name sortKey="Maclouf, J" sort="Maclouf, J" uniqKey="Maclouf J" first="J." last="Maclouf">J. Maclouf</name>
<name sortKey="Moukadiri, H" sort="Moukadiri, H" uniqKey="Moukadiri H" first="H." last="Moukadiri">H. Moukadiri</name>
<name sortKey="Moukadiri, H" sort="Moukadiri, H" uniqKey="Moukadiri H" first="H." last="Moukadiri">H. Moukadiri</name>
<name sortKey="Plouet, J" sort="Plouet, J" uniqKey="Plouet J" first="J." last="Plouet">J. Plouet</name>
<name sortKey="Plouet, J" sort="Plouet, J" uniqKey="Plouet J" first="J." last="Plouet">J. Plouet</name>
<name sortKey="Sauzeau, C" sort="Sauzeau, C" uniqKey="Sauzeau C" first="C." last="Sauzeau">C. Sauzeau</name>
<name sortKey="Tobelem, G" sort="Tobelem, G" uniqKey="Tobelem G" first="G." last="Tobelem">G. Tobelem</name>
</country>
<country name="États-Unis">
<region name="État de New York">
<name sortKey="Bikfalvi, A" sort="Bikfalvi, A" uniqKey="Bikfalvi A" first="A." last="Bikfalvi">A. Bikfalvi</name>
</region>
<name sortKey="Bikfalvi, A" sort="Bikfalvi, A" uniqKey="Bikfalvi A" first="A." last="Bikfalvi">A. Bikfalvi</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/ChloroquineV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002F69 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002F69 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    ChloroquineV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     ISTEX:D65D97CC8479F9BF9489CDDB588AF8E067E434AA
   |texte=   Interaction of vasculotropin/vascular endothelial cell growth factor with human umbilical vein endothelial cells: Binding, internalization, degradation, and biological effects
}}

Wicri

This area was generated with Dilib version V0.6.33.
Data generation: Wed Mar 25 22:43:59 2020. Site generation: Sun Jan 31 12:44:45 2021