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The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes

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Veröffentlicht/Copyright: 8. Januar 2013
Biological Chemistry
Aus der Zeitschrift Biological Chemistry Band 394 Heft 2

Abstract

Osteoarthritis and rheumatoid arthritis are destructive joint diseases that involve the loss of articular cartilage. Degradation of cartilage extracellular matrix is believed to occur due to imbalance between the catabolic and anabolic processes of resident chondrocytes. Previous work has suggested that various lysosomal cysteine cathepsins participate in cartilage degeneration; however, their exact roles in disease development and progression have not been elucidated. In order to study degradation processes under conditions resembling the in vivo milieu of the cartilage, we cultivated chondrocytes on a type II collagen-containing matrix. Stimulation of the cultivated chondrocytes with interleukin-1α and/or tumor necrosis factor α resulted in a time-dependent increase in cathepsin S expression and induced its secretion into the conditioned media. Using a novel bioluminescent activity-based probe, we were able to demonstrate a significant increase in proteolytic activity of cathepsin S in the conditioned media of proinflammatory cytokine-stimulated chondrocytes. For the first time, cathepsin S was demonstrated to be secreted from chondrocytes upon stimulation with the proinflammatory cytokines, and displayed proteolytic activity in culture supernatants. Its stability at neutral pH and potent proteolytic activity on extracellular matrix components mean that cathepsin S may contribute significantly to cartilage degradation and may thus be considered a potential drug target in joint diseases.

Keywords: activity-based probe; cathepsin; chondrocyte; proinflammatory cytokine; osteoarthritis
Corresponding authors: Dejan Caglič and Boris Turk, Department of Biochemistry, Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, SI-1000 Ljubljana, Slovenia
Received: 2012-9-11
Accepted: 2012-10-30
Published Online: 2013-01-08
Published in Print: 2013-02-01

©2013 by Walter de Gruyter Berlin Boston

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https://doi.org/10.1515/hsz-2012-0283
Schlagwörter für diesen Artikel
activity-based probe; cathepsin; chondrocyte; proinflammatory cytokine; osteoarthritis

Artikel in diesem Heft

  1. Masthead
  2. Masthead
  3. Guest Editorial
  4. Highlight: The physiology and dynamics of cellular microcompartments
  5. Highlight: The Physiology and Dynamics of Cellular Microcompartments
  6. Cellular microcompartments constitute general suborganellar functional units in cells
  7. Dynamics of bioenergetic microcompartments
  8. Microcompartments within the yeast plasma membrane
  9. Plant cell microcompartments: a redox-signaling perspective
  10. Microcompartments in the Drosophila heart and the mammalian brain: general features and common principles
  11. Minireviews
  12. Beyond anemia: hepcidin, monocytes and inflammation
  13. Melanoma resistance to photodynamic therapy: new insights
  14. The biosynthesis of caprazamycins and related liponucleoside antibiotics: new insights
  15. cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1
  16. Research Articles/Short Communications
  17. Protein Structure and Function
  18. Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants
  19. Cell Biology and Signaling
  20. Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
  21. Proteolysis
  22. ADAMTS: Novel proteases expressed by activated mast cells
  23. The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes
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