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The Journal of Immunology, 2003, 171: 5651.
Copyright © 2003 by The American Association of Immunologists

LETTERS TO THE EDITOR

LETTERS TO THE EDITOR

Johannes Roth, Thomas Vogl, Cord Sunderkötter and Clemens Sorg

Institute for Experimental Dermatology, University of Muenster, Muenster, Germany

Chemotactic activity of S100A8 and S100A9

In two recent papers published in The Journal of Immunology, Tessier and colleagues (1, 2) present remarkable data which indicate a direct chemotactic activity of both murine and human S100A8 and S100A9. Previous studies have already reported a chemotactic effect of murine S100A8, but human S100A8 and S100A9 have been shown to be chemotactically inert (3, 4). In mice the biological relevance of the chemotactic activity has been questioned by the fact that mice overexpressing S100A8 and S100A9 in keratinocytes show no cutaneous infiltration by leukocytes (5). In addition, the S100A8/S100A9 concentrations used by the group of Tessier to induce chemotaxis in the human system are in the range from 10-12 to 10-9 M (corresponding to ~10 pg/ml to 10 ng/ml) (1, 2). This is noteworthy as systemic serum concentrations of healthy donors are already ~360 ± 60 ng/ml and thus 30 times higher than those concentrations shown to be active in the published in vitro experiments. During inflammation, concentrations increase even more, regularly reaching up to 10- or 100-fold in serum and may raise up to 80,000 ng/ml at local sites of inflammation (6). We thus wonder whether the reported in vitro effects would be of biological relevance in vivo in man. Therefore interpretation of chemotactic activities of S100A8 and S100A9, although supported by in vitro results, should be done carefully. They ought to be discussed in the context of the published data on concentrations and expression patterns of these two S100-proteins in vivo.

References

  1. Vandal, K., P. Rouleau, A. Boivin, C. Ryckman, M. Talbot, P. A. Tessier. 2003. Blockade of S100A8 and S100A9 suppresses neutrophil migration in response to lipopolysaccharide. J. Immunol. 171:2602.[Abstract/Free Full Text]
  2. Ryckman, C., K. Vandal, P. Rouleau, M. Talbot, P. A. Tessier. 2003. Proinflammatory activities of S100: proteins S100A8, S100A9, and S100A8/A9 induce neutrophil chemotaxis and adhesion. J. Immunol. 170:3233.[Abstract/Free Full Text]
  3. Lackmann, M., P. Rajasekariah, S. E. Iismaa, G. Jones, C. J. Cornish, S. Hu, R. J. Simpson, R. L. Moritz, C. L. Geczy. 1993. Identification of a chemotactic domain of the pro-inflammatory S100 protein CP-10. J. Immunol. 150:2981.[Abstract]
  4. Newton, R. A., N. Hogg. 1998. The human S100 protein MRP-14 is a novel activator of the {beta}2 integrin Mac-1 on neutrophils. J. Immunol. 160:1427.[Abstract/Free Full Text]
  5. Thorey, I. S., J. Roth, J. Regenbogen, J. P. Halle, M. Bittner, T. Vogl, S. Kaesler, P. Bugnon, B. Reitmaier, S. Durka, et al 2001. The Ca2+-binding proteins S100A8 and S100A9 are encoded by novel injury-regulated genes. J. Biol. Chem. 276:35818.[Abstract/Free Full Text]
  6. Frosch, M., A. Strey, T. Vogl, N. Wulffraat, W. Kuis, C. Sorg, E. Harms, J. Roth. 2000. MRP8 and MRP14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity of juvenile rheumatoid arthritis. Arthritis Rheum. 43:628.[Medline]



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