Abstract
Peptidoglycane-recognizing protein Tag7 formed a complex with S100A4 (a representative of S100 protein family), the apparent dissociation constants in the absence and presence of Ca2+ were 2×10−8 M and 10−9 M, respectively. Analysis of fluorescence spectra of hydrophobic fluorescent probe 2-toluidinyl naphthalene-6-sulfonate in the presence of S100A4 and Tag7 proteins showed that extensive area or several sites are involved into the complex formation between these proteins. The formation of Tag7-S100A4 complex had virtually no effect on the role of S100A4 in the regulation of intracellular Ca2+ metabolism. Removal of not only Tag7, but also S100A4 from neutrophil conditioned medium reduced lysis of E. coli cell, while addition of the Tag7-S100A4 complex to the medium restored antibacterial activity.
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 145, No. 2, pp. 151–153, February, 2008
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Dukhanina, E.A., Romanova, E.A., Dukhanin, A.S. et al. Interactions and possible functional characteristics of Tag7-S100A4 protein complex. Bull Exp Biol Med 145, 191–193 (2008). https://doi.org/10.1007/s10517-008-0047-0
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DOI: https://doi.org/10.1007/s10517-008-0047-0