Binding, internalization, and degradation of basic fibroblast growth factor in human microvascular endothelial cells
- Centre National de la Recherche Scientifique UA 334, Paris (France)
- Centre National de la Recherche Scientifique UA 630, Paris (France)
- Hopital Beaujon, Clichy (France)
The binding, internalization, and degradation of basic fibroblast growth factor (bFGF) in human omental microvascular endothelial cells (HOME cells) were investigated. Binding studies of bFGF in human endothelial cells have not yet been reported. Basic FGF bound to HOME cells. The number of low-affinity binding sites was found to be variable. Washing the cells with 2 M phosphate-buffered saline removed completely {sup 125}I-bFGF bound to low-affinity binding sites but decreased also the high-affinity binding. The majority of the surface-bound {sup 125}I-bFGF was removed by washing the cells with acetic acid buffer at pH 3. At this temperature, degradation of the internalized ligand was followed after 1 hour by the appearance of three major bands of 15,000 10,000, and 8,000 Da and was inhibited by chloroquine. These results demonstrated two classes of binding sites for bFGF in HOME cells; the number of high-affinity binding sites being larger than the number reported for bovine capillary endothelial cells. The intracellular processing of bFGF in HOME cells seems to be different from that of heparin binding growth factor-1 in murine lung capillary endothelial cells and of eye-derived growth factor-1 in Chinese hamster fibroblasts.
- OSTI ID:
- 5623285
- Journal Information:
- Experimental Cell Research; (United States), Vol. 181:1; ISSN 0014-4827
- Country of Publication:
- United States
- Language:
- English
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