Link Protein Has Greater Affinity for Versican than Aggrecan

Shuiliang Shi, Suzanne Grothe, Yiping Zhang, Maureen D. O'Connor-McCourt, A. Robin Poole, Peter J. Roughley, John S. Mort

Research output: Contribution to journalArticle

40 Scopus citations


The function of link protein in stabilizing the interaction between aggrecan and hyaluronan to form aggrecan aggregates, via the binding of link protein to the aggrecan G1 domain and hyaluronan, is well established. However, it is not known whether link protein can function with similar avidity with versican, another member of the large hyaluronan-binding proteoglycan family that also binds to hyaluronan via its G1 domain. To address this issue, we have compared the interaction of the versican and aggrecan G1 domains with link protein and hyaluronan using recombinant proteins expressed in insect cells and BIAcore analysis. The results showed that link protein could significantly improve the binding of both G1 domains to hyaluronan and that its interaction with VG1 is of a higher affinity than that with AG1. These observations suggest that link protein may function as a stabilizer of the interaction, not only between aggrecan and hyaluronan in cartilage, but also between versican and hyaluronan in many tissues.

Original languageEnglish (US)
Pages (from-to)12060-12066
Number of pages7
JournalJournal of Biological Chemistry
Issue number13
StatePublished - Mar 26 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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  • Cite this

    Shi, S., Grothe, S., Zhang, Y., O'Connor-McCourt, M. D., Poole, A. R., Roughley, P. J., & Mort, J. S. (2004). Link Protein Has Greater Affinity for Versican than Aggrecan. Journal of Biological Chemistry, 279(13), 12060-12066.