Evidence map›Paper›PMID 27157803›Full record

ArticleScientific reports2016

Galectin-3 Binds to Lubricin and Reinforces the Lubricating Boundary Layer of Articular Cartilage.

Heidi L Reesink, Edward D Bonnevie, Sherry Liu, Carolyn R Shurer, Michael J Hollander, Lawrence J Bonassar, Alan J Nixon

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Recombinant manufacturing of multispecies biolubricants.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
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  10. Decrease of core 2The Journal of biological chemistry · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Heidi L ReesinkDepartment of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, United States of America.
Edward D BonnevieSibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY, United States of America.
Sherry LiuDepartment of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, United States of America.
Carolyn R ShurerSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, United States of America.
Michael J HollanderSchool of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, United States of America.
Lawrence J BonassarSibley School of Mechanical and Aerospace Engineering, Cornell University, Ithaca, NY, United States of America.
Alan J NixonDepartment of Clinical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, NY, United States of America.
Cornell University · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Graduate Training Program in Comparative MedicineT32OD011000 · OD · CORNELL UNIVERSITY · PI Amanda Marjorie DE MESTRE · 2012 to 2026
$5.7M
Broad wavelength range Zeiss 780 NLO/confocal system for the Cornell Imaging CoreS10OD018516 · OD · CORNELL UNIVERSITY · PI ZIPFEL, WARREN R · 2014 to 2014
$834k
NIGMS NIH HHS P41 GM103490NIH HHS S10 OD018516NIH HHS T32 OD011000
6 · The paper itself

Abstract

Lubricin is a mucinous, synovial fluid glycoprotein that enables near frictionless joint motion via adsorption to the surface of articular cartilage and its lubricating properties in solution. Extensive O-linked glycosylation within lubricin's mucin-rich domain is critical for its boundary lubricating function; however, it is unknown exactly how glycosylation facilitates cartilage lubrication. Here, we find that the lubricin glycome is enriched with terminal β-galactosides, known binding partners for a family of multivalent lectins called galectins. Of the galectin family members present in synovial fluid, we find that galectin-3 is a specific, high-affinity binding partner for lubricin. Considering the known ability of galectin-3 to crosslink glycoproteins, we hypothesized that galectins could augment lubrication via biomechanical stabilization of the lubricin boundary layer. We find that competitive inhibition of galectin binding results in lubricin loss from the cartilage surface, and addition of multimeric galectin-3 enhances cartilage lubrication. We also find that galectin-3 has low affinity for the surface layer of osteoarthritic cartilage and has reduced affinity for sialylated O-glycans, a glycophenotype associated with inflammatory conditions. Together, our results suggest that galectin-3 reinforces the lubricin boundary layer; which, in turn, enhances cartilage lubrication and may delay the onset and progression of arthritis.

Indexed as

LubricationAnimalsCartilage, ArticularCattleGalectin 3GlycomicsGlycoproteinsHorsesHumansKineticsPhenotypeProtein BindingProteoglycan 4Galectin 3GlycoproteinsProteoglycan 4

Identifiers

PMID27157803
PMCPMC4860590
OpenAlexW2346750548

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.