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Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass spectrometry.

Biochemical and biophysical research communications (1995-12-05)
D M Bürgisser, G Siegenthaler, T Kuster, U Hellman, P Hunziker, N Birchler, C W Heizmann
RESUMEN

The Ca(2+)-binding proteins regulate a number of cellular and extracellular activities and deregulations of S100 gene expression are associated with several human diseases. For example, S100A7 is upregulated in psoriatic skin, implicating a link with psoriasis, a chronic inflammatory dermatosis. We purified human S100A7 and determined its protein sequence by tandem mass spectrometry and Edman microsequence analysis. Interestingly, a sequence comparison of S100A7 with all known human S100 proteins showed that S100A7 is the most divergent of all S100 proteins.