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Localization of a binding site for the proteoglycan decorin on collagen XIV (undulin).

Abstract
Through its ability to bind extracellular matrix constituents and growth factors the small leucine-rich chondroitin/dermatan sulfate proteoglycan decorin which is present in many types of connective tissues may play an important biological role in remodeling and maintenance of extracellular matrices during inflammation, fibrosis, and cancer growth. In this study we investigated the known binding of decorin to human collagen XIV. This binding was unaffected when the small collagenous moiety of collagen XIV was removed with collagenase. Therefore, fragments covering the large noncollagenous domain NC3 of collagen XIV were expressed in Escherichia coli, each fused to a 26-kDa fragment of glutathione S-transferase. Using radioiodinated decorin as ligand for the immobilized fusion proteins, a binding site that interacted with the decorin core protein could be assigned to the NH2-terminal fibronectin type III repeat of collagen XIV. In addition, an auxiliary binding site located COOH-terminal to this fibronectin type III repeat interacted with the glycosaminoglycan component of decorin.
AuthorsT Ehnis, W Dieterich, M Bauer, H Kresse, D Schuppan
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 272 Issue 33 Pg. 20414-9 (Aug 15 1997) ISSN: 0021-9258 [Print] United States
PMID9252349 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • COL14A1 protein, human
  • DCN protein, human
  • Decorin
  • Extracellular Matrix Proteins
  • Glycoproteins
  • Peptide Fragments
  • Proteoglycans
  • Recombinant Fusion Proteins
  • Collagen
Topics
  • Amino Acid Sequence
  • Binding Sites
  • Collagen (metabolism)
  • Decorin
  • Extracellular Matrix Proteins
  • Glycoproteins (metabolism)
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments (metabolism)
  • Proteoglycans (metabolism)
  • Recombinant Fusion Proteins (metabolism)

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