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Search: WFRF:(Eisler T) > (2010-2014)

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  • Jin, Chunsheng, et al. (author)
  • Human Synovial Lubricin Expresses Sialyl Lewis x Determinant and Has L-selectin Ligand Activity
  • 2012
  • In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 287:43, s. 35922-35933
  • Journal article (peer-reviewed)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 (Gal beta 1-3(GlcNAc beta 1-6)GalNAc alpha 1-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 glycosylation-dependent 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 that PMN recruited 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.
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  • Result 1-4 of 4

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