title: Interaction of the small proteoglycan decorin with fibronectin. Involvement of the sequence NKISK of the core protein.
abstract: Decorin, an interstitial small proteoglycan, was shown to interact with fibronectin via its core protein. In a solid-phase assay, both high-affinity (KD values between 10 and 20 nM) and low-affinity (KD values between 110 and 130 nM) binding sites were found. The central position of decorin core protein is made up of several repeats containing NKISK in positions 85-89 and similar sequences in other repeats. The pentapeptide inhibited, albeit not completely, the high-affinity interaction between decorin and fibronectin in a specific charge-independent manner. Half-maximal inhibition occurred at a peptide concentration of 10 microM. Core-protein-derived peptides that had been produced by endoproteinase Lys-C digestion were not inhibitory, but endoproteinase Arg-C-generated peptides served as inhibitors of binding. These results suggest that NKISK as a component of repetitive sequences of decorin is involved in the interaction between the proteoglycan and fibronectin.
authors.affiliation: Institute of Physiological Chemistry and Pathobiochemistry, University of Münster, Federal Republic of Germany.
authors.forename: G
authors.initials: G
authors.lastname: Schmidt
authors.forename: H
authors.initials: H
authors.lastname: Hausser
authors.forename: H
authors.initials: H
authors.lastname: Kresse
mesh_terms: D000595:Amino Acid Sequence; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D058575:Decorin; D004797:Enzyme-Linked Immunosorbent Assay; D016326:Extracellular Matrix Proteins; D005353:Fibronectins / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000494:pharmacology; D011509:Proteoglycans / Q000378:metabolism*
chemical_list: C546878:DCN protein, human; D058575:Decorin; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D009842:Oligopeptides; D011509:Proteoglycans