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Differential interactions of decorin and decorin mutants with type I and type VI collagens

  1. Gordon Nareyeck1,
  2. Daniela G. Seidler1,
  3. David Troyer2,
  4. Jürgen Rauterberg2,
  5. Hans Kresse1,
  6. Elke Schönherr1,3

Article first published online: 26 JUL 2004

DOI: 10.1111/j.1432-1033.2004.04273.x

Issue

European Journal of Biochemistry

European Journal of Biochemistry

Volume 271, Issue 16, pages 3389–3398, August 2004

Additional Information

How to Cite

Nareyeck, G., Seidler, D. G., Troyer, D., Rauterberg, J., Kresse, H. and Schönherr, E. (2004), Differential interactions of decorin and decorin mutants with type I and type VI collagens. European Journal of Biochemistry, 271: 3389–3398. doi: 10.1111/j.1432-1033.2004.04273.x

Author Information

  1. 1

    Departement of Physiological Chemistry and Pathobiochemistry, University Hospital of Münster, Germany

  2. 2

    Institute of Arteriosclerosis Research, University of Münster, Germany

  3. 3

    Matrix Biology and Tissue Repair Research Unit, University of Wales College of Medicine, Dental School, Cardiff, UK

*E. Schönherr, Matrix Biology & Tissue Repair Research Unit, University of Wales College of Medicine, Dental School, Heath Park, Cardiff CF14 4XY, UK. Fax: + 44 29 2074 4509, Tel.: + 44 29 2074 2595, E-mail: schonherreh@cardiff.ac.uk

Publication History

  1. Issue published online: 26 JUL 2004
  2. Article first published online: 26 JUL 2004
  3. (Received 13 May 2004, accepted 30 June 2004)

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Keywords:

  • collagen type I;
  • collagen type VI;
  • decorin;
  • surface plasmon resonance measurements

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 (KD ≈ 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.

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