ChloroquineV1, Main, Exploration, bibRecord, 003248

Internalization and degradation of heparin binding growth factor-I by endothelial cells

Identifieur interne : 003248 ( Main/Exploration ); précédent : 003247; suivant : 003249

Internalization and degradation of heparin binding growth factor-I by endothelial cells

Auteurs : Robert Friesel [États-Unis] ; Thomas Maciag [États-Unis]

Source :

Biochemical and Biophysical Research Communications [ 0006-291X ] ; 1988.

RBID : ISTEX:E597DD559AB8C908EC1519645DA22922BA1F0D9F

Descripteurs français

KwdFr :
- Animaux, Chloroquine (pharmacologie), Cinétique, Concentration en ions d'hydrogène, Endothélium vasculaire (), Endothélium vasculaire (métabolisme), Facteur de croissance fibroblastique de type 1, Héparine (métabolisme), Masse moléculaire, Souris, Substances de croissance (métabolisme), Vaisseaux capillaires.
MESH :
- métabolisme : Endothélium vasculaire, Héparine, Substances de croissance.
- pharmacologie : Chloroquine.
- Animaux, Cinétique, Concentration en ions d'hydrogène, Endothélium vasculaire, Facteur de croissance fibroblastique de type 1, Masse moléculaire, Souris, Vaisseaux capillaires.

English descriptors

KwdEn :
- Animals, Capillaries, Chloroquine (pharmacology), EDTA, EGF, Endothelium, Vascular (drug effects), Endothelium, Vascular (metabolism), Fibroblast Growth Factor 1, Growth Substances (metabolism), HBGF-I, HEPES, Heparin (metabolism), Hydrogen-Ion Concentration, Kinetics, Mice, Molecular Weight, PMSF.
MESH :
- chemical , metabolism : Growth Substances, Heparin.
- chemical , pharmacology : Chloroquine.
- drug effects : Endothelium, Vascular.
- metabolism : Endothelium, Vascular.
Teeft :
- Academic press, Acetic acid, Animals, Binding buffer, Biophysical, Biophysical research communications, Capillaries, Cell lysates, Cell physiol, Cell surface, Cell surface receptors, Cell types, Chloroquine, Cold binding buffer, Confluent monolayers, Electrophoretic analysis, Endothelial, Endothelial cells, Fibroblast Growth Factor 1, Friesel, Growth factor, Growth factors, Heparin, Heparin binding growth factor, Human gliomas, Hydrogen-Ion Concentration, Incubation medium, Kinetics, Leii, Leii ceils, Leii cells, Ligand, Mice, Mitogenic response, Mitogenic signal, Molecular Weight, Receptor, Specific binding.

Abstract

Summary: The fate of 125I-labeled heparin binding growth factor I (125I-HBGF-I) after binding to its cell surface receptor has been studied using murine lung capillary endothelial cells (LEII). Binding of 125I-HBGF-I to its receptor at 4°C shows pH dependence with optimal binding at pH 6.5–7.5. The majority (∼80%) of 125I-HBGF-I bound to cells at 4°C can be removed by washing with low pH medium, but rapidly becomes acid resistant upon shifting cells to 37°C, with 50% of the 125I-HBGF-I becoming acid resistant after 20 minutes. Electrophoretic analysis of internalized 125I-HBGF-I shows that degradation begins approximately 2 hours after internalization with the appearance of two major labeled fragments of Mr 15,000 and Mr 10,000. Degradation of internalized 125I-HBGF-I is inhibited by the lysosomotropic agent chloroquine. These data suggest that cell-associated 125I-HBGF-I is rapidly internalized and directed to a lysosomal cellular compartment where it is slowly degraded.

Url:

https://api.istex.fr/ark:/67375/6H6-56VRVM2J-X/fulltext.pdf

DOI: 10.1016/S0006-291X(88)80459-5

Affiliations:

États-Unis

Le document en format XML

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<front><div type="abstract" xml:lang="en">Summary: The fate of 125I-labeled heparin binding growth factor I (125I-HBGF-I) after binding to its cell surface receptor has been studied using murine lung capillary endothelial cells (LEII). Binding of 125I-HBGF-I to its receptor at 4°C shows pH dependence with optimal binding at pH 6.5–7.5. The majority (∼80%) of 125I-HBGF-I bound to cells at 4°C can be removed by washing with low pH medium, but rapidly becomes acid resistant upon shifting cells to 37°C, with 50% of the 125I-HBGF-I becoming acid resistant after 20 minutes. Electrophoretic analysis of internalized 125I-HBGF-I shows that degradation begins approximately 2 hours after internalization with the appearance of two major labeled fragments of Mr 15,000 and Mr 10,000. Degradation of internalized 125I-HBGF-I is inhibited by the lysosomotropic agent chloroquine. These data suggest that cell-associated 125I-HBGF-I is rapidly internalized and directed to a lysosomal cellular compartment where it is slowly degraded.</div>
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Serveur d'exploration Chloroquine

Internalization and degradation of heparin binding growth factor-I by endothelial cells

Internalization and degradation of heparin binding growth factor-I by endothelial cells

Source :

Descripteurs français

English descriptors

Abstract

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

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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