Article Text

Download PDFPDF
Galectin-3 surface expression on human adult chondrocytes: a potential substrate for collagenase-3
  1. M Guévremont1,
  2. J Martel-Pelletier1,
  3. C Boileau1,
  4. F-T Liu2,
  5. M Richard3,
  6. J-C Fernandes1,
  7. J-P Pelletier1,
  8. P Reboul1
  1. 1Unité de Recherche en Arthrose, Centre de Recherche du Centre Hospitalier de l’Université de Montréal, Montréal, Québec, Canada
  2. 2Department of Dermatology, Sacramento, University of California-Davis, California, USA
  3. 3Département de Biochimie, Faculté de Médecine Lyon-Sud, Lyon, France
  1. Correspondence to:
    Dr P Reboul
    Osteoarthritis Research Unit, CR-CHUM, Y2604, 1560 Sherbrooke Street East, Montreal, Quebec, Canada H2L 4M1; pascal.reboulumontreal.ca

Abstract

Background: Galectin-3 is a lectin detected in mature and early hypertrophic chondrocytes; osteoarthritic (OA) chondrocytes can re-express hypertrophic markers.

Objective: To investigate the synthesis and subcellular localisation of galectin-3 in adult chondrocytes as well as the possibility of cleavage of galectin-3 by collagenase-1 and -3.

Methods: Galectin-3 was assessed by immunohistochemistry and real time polymerase chain reaction (PCR) in normal and OA cartilage. Its localisation was investigated by subcellular fractionation, immunocytology, and flow cytometry. Proteolysis of galectin-3 by collagenase-1 and -3 was determined by in vitro assay.

Results: Galectin-3 expression was increased 2.4-fold as measured by reverse transcriptase (RT)-PCR (p<0.05, n = 5) and threefold by immunohistochemistry (p<0.003 n = 6) in OA cartilage compared with normal cartilage. In adult chondrocytes, galectin-3 was found in the cytosol and membrane enriched fractions. Both immunocytology and flow cytometry confirmed the presence of galectin-3 at the surface of chondrocytes. A strong correlation was found between integrin-β1 and galectin-3 expression at the surface of chondrocytes. Moreover, collagenase-3 cleaved galectin-3 with a higher activity than collagenase-1. The proteolysed sites generated were identical to those produced by gelatinases A and B.

Conclusion: Galectin-3 may play a part in OA, having two roles, one intracellular and not yet identified, and another at the cell surface, possibly related to the interaction of chondrocytes and the cartilage matrix.

  • galectin-3
  • osteoarthritis
  • chondrocytes
  • collagenase-3
  • integrin-β1
  • 7-AAD, 7-aminoactinomycin D
  • ECM, extracellular matrix
  • MMP, matrix metalloproteinase
  • OA, osteoarthritis/osteoarthritic
  • PBS, phosphate buffered saline
  • PCR, polymerase chain reaction
  • RT-PCR, reverse transcriptase-polymerase chain reaction
  • SDS-PAGE, sodium dodecyl sulphate-polyacrylamide gel electrophoresis

Statistics from Altmetric.com

Request Permissions

If you wish to reuse any or all of this article please use the link below which will take you to the Copyright Clearance Center’s RightsLink service. You will be able to get a quick price and instant permission to reuse the content in many different ways.

Footnotes