title: The hetero-oligomeric complex of the S100A8/S100A9 protein is extremely protease resistant.
abstract: S100A8, S100A9 and S100A12 proteins are associated with inflammation and tissue remodelling, both processes known to be associated with high protease activity. Here, we report that homo-oligomeric forms of S100A8 and S100A9 are readily degraded by proteases, but that the preferred hetero-oligomeric S100A8/A9 complex displays a high resistance even against proteinase K degradation. S100A12 is not as protease resistant as the S100A8/A9 complex. Since specific functions have been assigned to the homo- and heterooligomeric forms of the S100A8 and A9 proteins, this finding may point to a post-translational level of regulation of the various functions of these proteins in inflammation and tissue remodelling.
authors.affiliation: Institute for Experimental Dermatology, University of Muenster, Roentgenstrasse 21, 48149 Muenster, Germany. nacken@uni-muenster.de
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Nacken
authors.forename: Claus
authors.initials: C
authors.lastname: Kerkhoff
mesh_terms: D000818:Animals; D040501:Calgranulin A / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D040502:Calgranulin B / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019286:Endopeptidase K / Q000737:chemistry / Q000378:metabolism*
chemical_list: D040501:Calgranulin A; D040502:Calgranulin B; D019286:Endopeptidase K