Heparin protects heparin-binding growth factor-I from proteolytic inactivation in vitro
| Autor: | Richard E. Clark, Robert Friesel, Thomas Maciag, Todd K. Rosengart, Warren V. Johnson |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Plasmin
medicine.medical_treatment Biophysics Biochemistry Mice medicine Animals Humans Denaturation (biochemistry) Growth Substances Molecular Biology Cells Cultured Heparin Binding Growth Factor Chemistry Heparin Growth factor Proteolytic enzymes Cell Biology Trypsin Endothelial stem cell Kinetics Fibroblast Growth Factor 1 Endothelium Vascular Cell Division medicine.drug Peptide Hydrolases |
| Zdroj: | Biochemical and biophysical research communications. 152(1) |
| ISSN: | 0006-291X |
| Popis: | Heparin inhibits proteolytic digestion of heparin-binding growth factor-I (HBGF-I) by trypsin, plasmin and other proteases. This property is lost after thermal denaturation of HBGF-I, suggesting that a heparin:HBGF-I structural interaction rather than a heparin:trypsin interaction is responsible for the resistance of HBGF-I to digestion with trypsin. Heparin is also able to partially protect HBGF-I from thermal denaturation as demonstrated by the ability of heparin to protect HBGF-I from trypsin digestion. The protective effect of heparin is dependent upon the concentration of heparin as well as temperature and duration of denaturation. Autoradiography of 125I-HBGF-I incubated with human umbilical vein endothelial cells demonstrates near complete protection of HBGF-I from proteolytic modification when the incubation is performed in the presence of heparin. These data suggest that (i) the mechanism of the heparin-induced increase in human endothelial cell number at confluence involves the protection of HBGF-I by heparin against proteolytic inactivation and (ii) heparin provides conformational stability to the proteolytic growth factor which reduces the susceptibility of HBGF-I to denaturation. |
| Databáze: | OpenAIRE |
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