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Related Concept Videos

Glycosaminoglycans01:23

Glycosaminoglycans

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Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
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Proteoglycans01:05

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Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Structural Joints: Synovial Joints01:16

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Synovial joints are the most common type of joint in the body. A key structural characteristic for a synovial joint is the presence of a joint cavity. This fluid-filled space is where the articulating surfaces of the bones contact each other. Also, unlike fibrous or cartilaginous joints, the articulating bone surfaces at a synovial joint are not directly connected to each other with fibrous connective tissue or cartilage. This gives the bones of a synovial joint the ability to move smoothly...
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Development of the Limb Synovial Joints01:07

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Joints form during embryonic development in conjunction with the formation and growth of the associated bones. The embryonic tissue that gives rise to all bones, cartilage, and connective tissues of the body is called mesenchyme.
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Knee Joint01:23

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The knee joint is the most complicated joint in the body. It consists of three articulations– two tibiofemoral and one patellofemoral. As is characteristic of synovial joints, the knee joint has a thin articular capsule that partially surrounds this joint cavity. Additionally, several ligaments, muscles, and cartilaginous structures support the movement of the knee.
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Updated: Dec 9, 2025

Synovial Fluid Analysis to Identify Osteoarthritis
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Decrease of core 2 O-glycans on synovial lubricin in osteoarthritis reduces galectin-3 mediated crosslinking.

Sarah A Flowers1, Kristina A Thomsson1, Liaqat Ali1

  • 1Department of Medical Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.

The Journal of Biological Chemistry
|September 15, 2020
PubMed
Summary

Core 2 O-linked glycans on lubricin mediate its interaction with galectin-3, crucial for cartilage lubrication. This interaction is impaired in osteoarthritis (OA), suggesting a defect in joint lubrication mechanisms in OA patients.

Keywords:
biolubricationgalectinglycobiologyglycomicslubricinmucinosteoarthritissialic acid

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Area of Science:

  • Biochemistry
  • Glycobiology
  • Osteoarthritis Research

Background:

  • Lubricin (proteoglycan 4) is a key synovial fluid glycoprotein involved in joint lubrication.
  • Its lubricating properties are linked to O-linked glycosylation, including Tn-antigens and core 1/2 structures.
  • Lubricin's interaction with galectin-3 is proposed to stabilize cartilage, but specific mediating glycans were unknown.

Purpose of the Study:

  • To identify the specific O-linked glycan structures on lubricin responsible for galectin-3 binding.
  • To investigate the role of lubricin-galectin-3 interaction in osteoarthritis (OA) pathogenesis.
  • To determine changes in lubricin glycosylation and galectin-3 binding in OA patients.

Main Methods:

  • Surface plasmon resonance (SPR) to assess binding between recombinant lubricin variants and galectin-3.
  • Transfection of Chinese hamster ovary (CHO) cells with core 2 GlcNAc transferase to study galectin-3 binding.
  • Analysis of synovial fluid from OA patients to quantify galectin-3 levels and lubricin glycan structures.

Main Results:

  • Recombinant lubricin lacking core 2 O-linked glycans did not bind to galectin-3, confirming core 2 structures mediate this interaction.
  • Enhanced expression of core 2 GlcNAc transferase increased galectin-3 binding to lubricin.
  • Late-stage OA patients showed decreased galectin-3 levels and impaired lubricin-galectin-3 interaction, alongside increased T-antigens and Tn-antigens.

Conclusions:

  • Core 2 O-linked glycans are essential for lubricin-galectin-3 binding, mediating cartilage lubrication.
  • A defect in this crosslinking interaction, associated with altered glycosylation, is implicated in OA molecular pathology.
  • These findings offer new insights into the mechanisms underlying osteoarthritis development and progression.