Link protein has greater affinity for versican than aggrecan

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DOIResolve DOI: http://doi.org/10.1074/jbc.M310091200
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TypeArticle
Journal titleJ Biol Chem
Volume279
Issue13
Pages1206012066; # of pages: 7
Subjectanalysis; ecombinant Proteins; pha; proteins
AbstractThe 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
Publication date
LanguageEnglish
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
NoteEnglish14724283
Peer reviewedNo
NRC number46171
NPARC number3538965
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Record identifierbcc2cb24-e1f7-4ba0-9b6a-bf7c51d1d7e8
Record created2009-03-01
Record modified2016-05-09
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