Galectin-3 surface expression on human adult chondrocytes

A potential substrate for collagenase-3

M. Guévremont, J. Martel-Pelletier, C. Boileau, Fu-Tong Liu, M. Richard, J. C. Fernandes, J. P. Pelletier, P. Reboul

Research output: Contribution to journalArticle

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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.

Original languageEnglish (US)
Pages (from-to)636-643
Number of pages8
JournalAnnals of the Rheumatic Diseases
Volume63
Issue number6
DOIs
StatePublished - Jun 2004

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Matrix Metalloproteinase 13
Galectin 3
Chondrocytes
Substrates
Cartilage
Flow cytometry
Polymerase chain reaction
Flow Cytometry
Immunohistochemistry
Proteolysis
RNA-Directed DNA Polymerase
Matrix Metalloproteinase 2
Matrix Metalloproteinase 9
Fractionation
Reverse Transcriptase Polymerase Chain Reaction
Lectins
Integrins
Cytosol
Real-Time Polymerase Chain Reaction
Assays

ASJC Scopus subject areas

  • Rheumatology
  • Immunology

Cite this

Guévremont, M., Martel-Pelletier, J., Boileau, C., Liu, F-T., Richard, M., Fernandes, J. C., ... Reboul, P. (2004). Galectin-3 surface expression on human adult chondrocytes: A potential substrate for collagenase-3. Annals of the Rheumatic Diseases, 63(6), 636-643. https://doi.org/10.1136/ard.2003.007229

Galectin-3 surface expression on human adult chondrocytes : A potential substrate for collagenase-3. / Guévremont, M.; Martel-Pelletier, J.; Boileau, C.; Liu, Fu-Tong; Richard, M.; Fernandes, J. C.; Pelletier, J. P.; Reboul, P.

In: Annals of the Rheumatic Diseases, Vol. 63, No. 6, 06.2004, p. 636-643.

Research output: Contribution to journalArticle

Guévremont, M, Martel-Pelletier, J, Boileau, C, Liu, F-T, Richard, M, Fernandes, JC, Pelletier, JP & Reboul, P 2004, 'Galectin-3 surface expression on human adult chondrocytes: A potential substrate for collagenase-3', Annals of the Rheumatic Diseases, vol. 63, no. 6, pp. 636-643. https://doi.org/10.1136/ard.2003.007229
Guévremont M, Martel-Pelletier J, Boileau C, Liu F-T, Richard M, Fernandes JC et al. Galectin-3 surface expression on human adult chondrocytes: A potential substrate for collagenase-3. Annals of the Rheumatic Diseases. 2004 Jun;63(6):636-643. https://doi.org/10.1136/ard.2003.007229
Guévremont, M. ; Martel-Pelletier, J. ; Boileau, C. ; Liu, Fu-Tong ; Richard, M. ; Fernandes, J. C. ; Pelletier, J. P. ; Reboul, P. / Galectin-3 surface expression on human adult chondrocytes : A potential substrate for collagenase-3. In: Annals of the Rheumatic Diseases. 2004 ; Vol. 63, No. 6. pp. 636-643.
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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.",
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AU - Martel-Pelletier, J.

AU - Boileau, C.

AU - Liu, Fu-Tong

AU - Richard, M.

AU - Fernandes, J. C.

AU - Pelletier, J. P.

AU - Reboul, P.

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N2 - 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.

AB - 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.

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