Kato, M <br/><br/>
Physiological degradation converts the soluble syndecan-1 ectodomain from an inhibitor to a potent activator of FGF-2.  [electronic resource] 

 -  Nature medicine  Jun 1998 
 - 691-7 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>1078-8956 
<br/><br/><label>Standard No.: </label>10.1038/nm0698-691  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Binding Sites--physiology<br/>Exudates and Transudates--chemistry<br/>Fibrinolytic Agents--pharmacology<br/>Fibroblast Growth Factor 2--antagonists & inhibitors<br/>Glucuronidase<br/>Glycoside Hydrolases--pharmacology<br/>Heparin--pharmacology<br/>Heparitin Sulfate--metabolism<br/>Humans<br/>Membrane Glycoproteins--drug effects<br/>Mitogens--metabolism<br/>Oligosaccharides--pharmacology<br/>Protein Binding<br/>Proteoglycans--drug effects<br/>Receptor Protein-Tyrosine Kinases<br/>Receptor, Fibroblast Growth Factor, Type 1<br/>Receptors, Fibroblast Growth Factor--metabolism<br/>Solubility<br/>Syndecan-1<br/>Syndecans<br/>Wounds and Injuries--metabolism