FEBS Letters
Volume 582, Issue 9 , Pages 1307-1312, 16 April 2008

Extracellular catalase activity protects cysteine cathepsins from inactivation by hydrogen peroxide

Edited by David Lambeth

  • Virginie Hervé-Grépinet

      Affiliations

    • These two authors have equally contributed to the work.
    • Current address: INRA, UR 83 Recherches Avicoles, Nouzillly, France.
  • ,
  • Florian Veillard

      Affiliations

    • These two authors have equally contributed to the work.
  • ,
  • Emmanuel Godat

      Affiliations

    • Current address: Laboratoire de PhysioGénomique, SBGM/DBJC, CEA/Saclay, Gif-sur-Yvette, France.
  • ,
  • Nathalie Heuzé-Vourc’h
  • ,
  • Fabien Lecaille
  • ,
  • Gilles Lalmanach

      Affiliations

    • Corresponding Author InformationCorresponding author. Present address: INSERM U 618, Protéases et Vectorisation Pulmonaires, Université François Rabelais, Faculté de Médecine, 10 Bd Tonnellé, F-37032 Tours Cedex, France. Fax: +33 2 47 36 60 46.

INSERM U 618, Protéases et Vectorisation Pulmonaires, Equipe Protéases et Pathologies Pulmonaires, Tours F-37000, France

Université François Rabelais, Tours F-37000, France

IFR 135, Tours F-37000, France

Received 12 December 2007; received in revised form 8 February 2008; accepted 5 March 2008. published online 14 March 2008.

Abstract 

The resistance of secreted cysteine cathepsins to peroxide inactivation was evaluated using as model THP-1 cells. Differentiated cells released mostly cathepsin B, but also cathepsins H, K, and L, with a maximum of endopeptidase activity at day 6. Addition of non-cytotoxic concentrations of H2O2 did not affect mRNA expression levels and activity of cathepsins, while the catalase activity remained also unchanged, consistently with RT-PCR analysis. Conversely inhibition of extracellular catalase led to a striking inactivation of secreted cysteine cathepsins by H2O2. This report suggests that catalase may participate in the protection of extracellular cysteine proteases against peroxidation.

Abbreviations: AMC, 7-amino-4-methyl coumarin, 3-AT, 3-amino-l, 2, 4-triazole, BALF, bronchoalveolar lavage fluid, BCA, bicinchoninic acid, CA-074, N-(l-3-trans-propylcarbamoyl oxirane-2-carbonyl)-l-isoleucyl-l-proline, CP, cysteine protease, DTT, dl-dithiothreitol, E-64, l-3-carboxy-trans-2.3-epoxypropionyl-leucylamido-(4-guanidino) butane, ECM, extra cellular matrix, FBS, fetal bovine serum, GM-CSF, granulocyte–macrophage colony-stimulating factor, MDM, monocyte-derived macrophage, MMTS, methylmethanethiosulfonate, PMA, phorbol myristate acetate, PMSF, phenylmethylsulfonyl fluoride, ROS, reactive oxygen species, Z, benzyloxycarbonyl

Keywords: Cathepsin, Cysteine protease, Inflammation, Oxidation, Proteolysis, THP-1 cell

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PII: S0014-5793(08)00210-X

doi:10.1016/j.febslet.2008.03.007

FEBS Letters
Volume 582, Issue 9 , Pages 1307-1312, 16 April 2008