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J. Biol. Chem., Vol. 281, Issue 30, 21082-21095, July 28, 2006

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The Mammalian Chitinase-like Lectin, YKL-40, Binds Specifically to Type I Collagen and Modulates the Rate of Type I Collagen Fibril Formation^*

Heather F. Bigg¹, Robin Wait, Andrew D. Rowan, and Tim E. Cawston

From the Musculoskeletal Research Group, Catherine Cookson Building, The Medical School, Framlington Place, University of Newcastle-upon-Tyne, Newcastle-upon-Tyne NE2 4HH, United Kingdom and the Kennedy Institute of Rheumatology Division, Faculty of Medicine, Imperial College London, 1, Aspenlea Road, Hammersmith, London W6 8LH, United Kingdom

YKL-40 is expressed in arthritic cartilage and produced in large amounts by cultured chondrocytes, but its exact role is unclear, and the identities of its physiological ligands remain unknown. Purification of YKL-40 from resorbing bovine nasal cartilage and chondrocyte monolayers demonstrated the existence of three isoforms, a major and minor form from resorbing cartilage and a third species from chondrocytes. Affinity chromatography experiments with purified YKL-40 demonstrated specific binding of all three forms to collagen types I, II, and III, thus identifying collagens as potential YKL-40 ligands. Binding to immobilized type I collagen was inhibited by soluble native ligand, but not heat-denatured ligand, confirming a specific interaction. Binding of the chondrocyte-derived species to type I collagen was also demonstrated by surface plasmon resonance analysis, and the dissociation rate constant was calculated (3.42 x 10^-3 to 4.50 x 10^-3 s^-1). The chondrocyte-derived species was found to prevent collagenolytic cleavage of type I collagen and to stimulate the rate of type I collagen fibril formation in a concentration-dependent manner. By contrast, the cartilage major form had an inhibitory effect on type I collagen fibrillogenesis. Digestion with N-glycosidase F, endoglycosidase H and lectin blotting did not reveal any difference in the carbohydrate component of these two YKL-40 species, indicating that this does not account for the opposing effects on fibril formation rate.

Received for publication, February 7, 2006 , and in revised form, May 10, 2006.

^* This work was supported by the Arthritis Research Campaign, UK, the Medical Research Council, UK, and the Dunhill Medical Trust, UK. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Musculoskeletal Research Group, 4th Floor, Catherine Cookson Bldg., The Medical School, Framlington Place, University of Newcastle-upon-Tyne NE2 4HH, UK. Tel.: 44-191-222-5462; Fax: 44-191-222-5455; E-mail: Heather.Bigg{at}ncl.ac.uk.

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