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Human Synovial Lubricin Expresses Sialyl Lewis x Determinant and Has L-selectin Ligand Activity

Journal article
Authors Chunsheng Jin
Anna-Karin H Ekwall
Johan Bylund
Lena Björkman
R. P. Estrella
J. M. Whitelock
T. Eisler
Maria Bokarewa
Niclas G. Karlsson
Published in Journal of Biological Chemistry
Volume 287
Issue 43
Pages 35922-35933
ISSN 0021-9258
Publication year 2012
Published at Institute of Medicine, Department of Rheumatology and Inflammation Research
Institute of Biomedicine, Department of Medical Biochemistry and Cell Biology
Pages 35922-35933
Language en
Links dx.doi.org/10.1074/jbc.M112.363119
Keywords superficial zone protein, rheumatoid-arthritis, articular-cartilage, gene-expression, lubricating properties, recombinant lubricin, mass-spectrometry, o-glycans, cells, fluid
Subject categories Medical Biotechnology

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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