Internalization and degradation of heparin binding growth factor-I by endothelial cells
Identifieur interne : 002010 ( Istex/Checkpoint ); précédent : 002009; suivant : 002011Internalization 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.
English descriptors
- KwdEn :
- Teeft :
- Academic press, Acetic acid, Binding buffer, Biophysical, Biophysical research communications, Cell lysates, Cell physiol, Cell surface, Cell surface receptors, Cell types, Chloroquine, Cold binding buffer, Confluent monolayers, Electrophoretic analysis, Endothelial, Endothelial cells, Friesel, Growth factor, Growth factors, Heparin, Heparin binding growth factor, Human gliomas, Incubation medium, Leii, Leii ceils, Leii cells, Ligand, Mitogenic response, Mitogenic signal, 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:
DOI: 10.1016/S0006-291X(88)80459-5
Affiliations:
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<wicri:regionArea>Laboratory of Molecular Biology Jerome H. Holland Laboratory for the Biomedical Sciences American Red Cross 15601 Crabbs Branch Way Rockville, Maryland 20855</wicri:regionArea>
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<author><name sortKey="Maciag, Thomas" sort="Maciag, Thomas" uniqKey="Maciag T" first="Thomas" last="Maciag">Thomas Maciag</name>
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<term>EGF</term>
<term>HBGF-I</term>
<term>HEPES</term>
<term>PMSF</term>
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<keywords scheme="Teeft" xml:lang="en"><term>Academic press</term>
<term>Acetic acid</term>
<term>Binding buffer</term>
<term>Biophysical</term>
<term>Biophysical research communications</term>
<term>Cell lysates</term>
<term>Cell physiol</term>
<term>Cell surface</term>
<term>Cell surface receptors</term>
<term>Cell types</term>
<term>Chloroquine</term>
<term>Cold binding buffer</term>
<term>Confluent monolayers</term>
<term>Electrophoretic analysis</term>
<term>Endothelial</term>
<term>Endothelial cells</term>
<term>Friesel</term>
<term>Growth factor</term>
<term>Growth factors</term>
<term>Heparin</term>
<term>Heparin binding growth factor</term>
<term>Human gliomas</term>
<term>Incubation medium</term>
<term>Leii</term>
<term>Leii ceils</term>
<term>Leii cells</term>
<term>Ligand</term>
<term>Mitogenic response</term>
<term>Mitogenic signal</term>
<term>Receptor</term>
<term>Specific binding</term>
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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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