Human synovial lubricin expresses sialyl Lewis x determinant and has L-selectin ligand activity

Chunsheng Jin*, Anna Karin Hultgård Ekwall, Johan Bylund, Lena Björkman, Ruby P. Estrella, John M. Whitelock, Thomas Eisler, Maria Bokarewa, Niclas G. Karlsson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)

Abstract

Lubricin (or proteoglycan 4 (PRG4)) is an abundant mucin-like glycoprotein in synovial fluid (SF) and a major component responsible for joint lubrication. In this study, it was shown that O-linked core 2 oligosaccharides (Galβ1-3(GlcNAcβ1-6)GalNAcβ1- Thr/Ser) on lubricin isolated from rheumatoid arthritis SF contained both sulfate and fucose residues, and SF lubricin was capable of binding to recombinant L-selectin in a glycosylationdependent manner. Using resting human polymorphonuclear granulocytes (PMN) from peripheral blood, confocal microscopy showed that lubricin coated circulating PMN and that it partly co-localized with L-selectin expressed by these cells. In agreement with this, activation-induced shedding of L-selectin also mediated decreased lubricin binding to PMN. It was also found thatPMNrecruited to inflamed synovial area and fluid in rheumatoid arthritis patients kept a coat of lubricin. These observations suggest that lubricin is able to bind to PMN via an L-selectin-dependent and -independent manner and may play a role in PMN-mediated inflammation.

Original languageEnglish
Pages (from-to)35922-35933
Number of pages12
JournalJournal of Biological Chemistry
Volume287
Issue number43
DOIs
Publication statusPublished - 19 Oct 2012

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