Structure/function studies of S100a8/a9

Craig A. Harrison, Mark J. Raftery, Paul Alewood, Carolyn L. Geczy

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2 Citations (Scopus)


The functional importance of members of the S100 Ca2+-binding protein family is recently emerging. A variety of activities, several of which are apparently opposing, are attributed to S100A8, a protein implicated in embryogenesis, growth, differentiation, and immune and inflammatory processes. Murine (m) S100A8 was initially described as a chemoattractant (CP-10) for myeloid cells. It is coordinately expressed with mS100A9 (MRP14) in neutrophils and the non-covalent heterodimer is presumed to be the functional intracellular species. The extracellular chemotactic activity of mS100A8, however, is not dependent on mS100A9 and occurs at concentrations (10-1310-11 M) at which the non-covalent heterodimer would probably dissociate. This review focuses on the structure and post-translational modifications of mS100A8/A9 and their effects on function, particularly chemotaxis.

Original languageEnglish
Pages (from-to)359-369
Number of pages11
JournalLetters in Peptide Science
Issue number5-6
Publication statusPublished - 1999
Externally publishedYes


  • Chemotaxis
  • Inflammation
  • Oxidation
  • Post-translational
  • S100

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