Authors: Nareyeck, Gordon¹; Seidler, Daniela G.¹; Troyer, David²; Rauterberg, Jürgen²; Kresse, Hans¹; Schönherr, Elke

Source: FEBS Journal, Volume 271, Number 16, August 2004 , pp. 3389-3398(10)

Publisher: Wiley-Blackwell

Abstract:

The small leucine-rich proteoglycan decorin can bind via its core protein to different types of collagens such as type I and type VI. To test whether decorin can act as a bridging molecule between these collagens, the binding properties of wild-type decorin, two full-length decorin species with single amino acid substitutions (DCN E180K, DCN E180Q), which previously showed reduced binding to collagen type I fibrils, and a truncated form of decorin (DCN Q153) to the these collagens were investigated. In a solid phase assay dissociation constants for wild-type decorin bound to methylated, therefore monomeric, triple helical type I collagen were in the order of 10⁻¹⁰ m, while dissociation constants for fibrillar type I collagen were ≈ 10⁻⁹ m. The dissociation constant for type VI was ≈ 10⁻⁷ m. Using real-time analysis for a more detailed investigation DCN E180Q and DCN E180K exhibited lower association and higher dissociation constants to type I collagen, compared to wild-type decorin, deviating by at least one order of magnitude. In contrast, the affinities of these mutants to type VI collagen were 10 times higher than the affinity of wild-type decorin (K_D ≈ 10⁻⁸ m). Further investigations verified that complexes of type VI collagen and decorin bound type I collagen and that the affinity of collagen type VI to type I was increased by the presence of decorin. These data show that decorin not only can regulate collagen fibril formation but that it also can act as an intermediary between type I and type VI collagen and that these two types of collagen interact via different binding sites.

Keywords: collagen type I; collagen type VI; decorin; surface plasmon resonance measurements

Document Type: Research article

DOI: http://dx.doi.org/10.1111/j.1432-1033.2004.04273.x

Affiliations: 1: Departement of Physiological Chemistry and Pathobiochemistry, University Hospital of Münster, Germany 2: Institute of Arteriosclerosis Research, University of Münster, Germany

Publication date: 2004-08-01

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• In this Subject: Anatomy & Physiology ,  Biology ,  Chemistry (General) ,  Biochemistry
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