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Tenascin-C binds heparin by its fibronectin type III domain five.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1995 Mar 03; Vol. 270 (9), pp. 4619-23. - Publication Year :
- 1995
-
Abstract
- Two sites on tenascin mediate interactions with glycosaminoglycan chains of proteoglycans. One is situated on the fibrinogen-like domain, whereas the other lies within the fibronectin type III homology region (Aukhil, I., Joshi, P., Yan, Y.Z., and Erickson, H.P. (1993) J. Biol. Chem. 268, 2542-2553.). We now characterize the latter binding site more closely by means of recombinant protein fragments derived from the type III homology region of tenascin. Using a heparin-Sepharose column, we localize the second heparin binding site to the fifth fibronectin type III domain. This is confirmed in solid phase assays by incubation of fusion proteins with biotin-labeled heparin. In addition, we demonstrate the binding of heparan sulfate and dermatan sulfate to domain five. Molecular modelling of this domain reveals a conserved heparin-binding motif that we propose as the putative binding site. The fact, that different glycosaminoglycans may bind to this domain, implies that different classes of proteoglycans may in vivo compete for the same site.
- Subjects :
- Amino Acid Sequence
Animals
Biotin
Cattle
DNA, Recombinant
Fibronectins genetics
Glycosaminoglycans metabolism
Models, Molecular
Molecular Sequence Data
Protein Binding
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins metabolism
Sepharose analogs & derivatives
Sepharose metabolism
Sharks
Swine
Tenascin
Cell Adhesion Molecules, Neuronal metabolism
Extracellular Matrix Proteins metabolism
Fibronectins metabolism
Heparin metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 270
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 7533163
- Full Text :
- https://doi.org/10.1074/jbc.270.9.4619