Parsons, P. (Philippa), Gilbert, S. J., Vaughan-Thomas, A., Sorrell, D. A., Notman, Rebecca, Bishop, M. (Mark), Hayes, A. J. (Anthony J.), Mason, D. J. (Deborah J.) and Duance, V. C.. (2011) Type IX collagen interacts with fibronectin providing an important molecular bridge in articular cartilage. Journal of Biological Chemistry, Vol.286 (No.40). pp. 34986-34997. ISSN 0021-9258

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Abstract

Type IX collagen is covalently bound to the surface of type II collagen fibrils within the cartilage extracellular matrix. The N-terminal, globular noncollagenous domain (NC4) of the alpha 1(IX) chain protrudes away from the surface of the fibrils into the surrounding matrix and is available for molecular interactions. To define these interactions, we used the NC4 domain in a yeast two-hybrid screen of a human chondrocyte cDNA library. 73% of the interacting clones encoded fibronectin. The interaction was confirmed using in vitro immunoprecipitation and was further characterized by surface plasmon resonance. Using whole and pepsin-derived preparations of type IX collagen, the interaction was shown to be specific for the NC4 domain with no interaction with the triple helical collagenous domains. The interaction was shown to be of high affinity with nanomolar K(d) values. Analysis of the fibronectin-interacting clones indicates that the constant domain is the likely site of interaction. Type IX collagen and fibronectin were shown to co-localize in cartilage. This novel interaction between the NC4 domain of type IX collagen and fibronectin may represent an in vivo interaction in cartilage that could contribute to the matrix integrity of the tissue.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Fibronectins, Collagen, Articular cartilage, Extracellular matrix, Protein-protein interactions
Journal or Publication Title:	Journal of Biological Chemistry
Publisher:	American Society for Biochemistry and Molecular Biology
ISSN:	0021-9258
Date:	7 October 2011
Volume:	Vol.286
Number:	No.40
Page Range:	pp. 34986-34997
Identification Number:	10.1074/jbc.M111.238188
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Arthritis Research UK , Cardiff University , National Institutes of Health (U.S.) (NIH), National Institute of Child Health and Human Development (U.S.) (NICHD)
Grant number:	D0596 (ARUK)
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URI:	http://wrap.warwick.ac.uk/id/eprint/40609

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