The hetero-oligomeric complex of the S100A8/S100A9 protein is extremely protease resistant |
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Authors: | Nacken Wolfgang Kerkhoff Claus |
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Affiliation: | Institute for Experimental Dermatology, University of Muenster, Roentgenstrasse 21, 48149 Muenster, Germany. nacken@uni-muenster.de |
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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. |
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Keywords: | S100A8/A9 S100A12 Protease resistance Proteinase K Inflammation |
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