Localization of the ganglioside-binding site of fibronectin
It has been demonstrated via biological assays that fibronectin possesses a receptor for gangliosides that is involved in cell adhesion and restoration of the normal morphology of transformed cells. In this study, fluorescence polarization has been employed to monitor the binding of ganglioside olig...
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| Veröffentlicht in: | The Journal of biological chemistry 1986-04, Vol.261 (11), p.5209-5214 |
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| container_issue | 11 |
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| container_title | The Journal of biological chemistry |
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| creator | Thompson, L K Horowitz, P M Bentley, K L Thomas, D D Alderete, J F Klebe, R J |
| description | It has been demonstrated via biological assays that fibronectin possesses a receptor for gangliosides that is involved in cell adhesion and restoration of the normal morphology of transformed cells. In this study, fluorescence polarization has been employed to monitor the binding of ganglioside oligosaccharide to fibronectin. Parameters involved in ganglioside oligosaccharide binding to fibronectin are described and compared to the interaction of heparin with fibronectin. A Kd of 1.4 X 10(-8) mol/liter has been calculated, and it is demonstrated that labeled ganglioside oligosaccharides can be eluted from fibronectin with either unlabeled ganglioside oligosaccharides or 4 M urea. Using the fluorescence polarization assay developed in this study for measurement of ganglioside binding to fibronectin, it is demonstrated that gangliosides bind to the 31,000-dalton amino terminal heparin-binding domain of fibronectin. A ganglioside-Sepharose affinity column has been constructed which specifically binds the 31,000-dalton amino terminal fragment of fibronectin. The localization of the ganglioside receptor to the amino terminal domain of fibronectin indicates that the ganglioside receptor is distinct from the putative fibronectin cell surface receptor which is located near the center of the fibronectin molecule. |
| doi_str_mv | 10.1016/S0021-9258(19)89235-9 |
| format | Article |
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In this study, fluorescence polarization has been employed to monitor the binding of ganglioside oligosaccharide to fibronectin. Parameters involved in ganglioside oligosaccharide binding to fibronectin are described and compared to the interaction of heparin with fibronectin. A Kd of 1.4 X 10(-8) mol/liter has been calculated, and it is demonstrated that labeled ganglioside oligosaccharides can be eluted from fibronectin with either unlabeled ganglioside oligosaccharides or 4 M urea. Using the fluorescence polarization assay developed in this study for measurement of ganglioside binding to fibronectin, it is demonstrated that gangliosides bind to the 31,000-dalton amino terminal heparin-binding domain of fibronectin. A ganglioside-Sepharose affinity column has been constructed which specifically binds the 31,000-dalton amino terminal fragment of fibronectin. The localization of the ganglioside receptor to the amino terminal domain of fibronectin indicates that the ganglioside receptor is distinct from the putative fibronectin cell surface receptor which is located near the center of the fibronectin molecule.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)89235-9</identifier><identifier>PMID: 3957921</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Analytical, structural and metabolic biochemistry ; Binding Sites ; Biological and medical sciences ; Fibronectins - metabolism ; Fluoresceins ; Fluorescence Polarization ; Fluorescent Dyes ; Fundamental and applied biological sciences. 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The localization of the ganglioside receptor to the amino terminal domain of fibronectin indicates that the ganglioside receptor is distinct from the putative fibronectin cell surface receptor which is located near the center of the fibronectin molecule.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Fibronectins - metabolism</subject><subject>Fluoresceins</subject><subject>Fluorescence Polarization</subject><subject>Fluorescent Dyes</subject><subject>Fundamental and applied biological sciences. 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In this study, fluorescence polarization has been employed to monitor the binding of ganglioside oligosaccharide to fibronectin. Parameters involved in ganglioside oligosaccharide binding to fibronectin are described and compared to the interaction of heparin with fibronectin. A Kd of 1.4 X 10(-8) mol/liter has been calculated, and it is demonstrated that labeled ganglioside oligosaccharides can be eluted from fibronectin with either unlabeled ganglioside oligosaccharides or 4 M urea. Using the fluorescence polarization assay developed in this study for measurement of ganglioside binding to fibronectin, it is demonstrated that gangliosides bind to the 31,000-dalton amino terminal heparin-binding domain of fibronectin. A ganglioside-Sepharose affinity column has been constructed which specifically binds the 31,000-dalton amino terminal fragment of fibronectin. The localization of the ganglioside receptor to the amino terminal domain of fibronectin indicates that the ganglioside receptor is distinct from the putative fibronectin cell surface receptor which is located near the center of the fibronectin molecule.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>3957921</pmid><doi>10.1016/S0021-9258(19)89235-9</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1986-04, Vol.261 (11), p.5209-5214 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76758096 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Fibronectins - metabolism Fluoresceins Fluorescence Polarization Fluorescent Dyes Fundamental and applied biological sciences. Psychology Gangliosides - metabolism Heparin - metabolism Humans Hydrogen-Ion Concentration Inorganic compounds Kinetics Oligosaccharides - metabolism Osmolar Concentration Other biological molecules Peptide Fragments - metabolism Temperature |
| title | Localization of the ganglioside-binding site of fibronectin |
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