Characterization of the Cysteine-Rich Calcium-Binding S100A3 Protein from Human Hair Cuticles

    Kenji Kizawa, Heinz Troxler, P. Kleinert, Takafumi Inoue, Masahiko Toyoda, Masaaki Morohashi, Claus W. Heizmann
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    TLDR Scientists found out how a specific protein in human hair cuticles behaves and is structured.
    The study focused on S100A3, a protein from the S100 family, which is specifically found in the inner endocuticle of human hair fibers and is released upon hair damage, potentially affecting hair structure. Researchers successfully extracted and purified native S100A3 from human hair cuticles using anion-exchange chromatography. Analysis through 2D gel electrophoresis indicated that the isoelectric point of cuticle-derived S100A3 was slightly lower than that of its recombinant counterpart. Additionally, tandem mass spectrometry revealed that the N-terminal methionine of the cuticle S100A3 was replaced by an acetyl group. This research provided the first biochemical characterization of S100A3 in human hair cuticle.
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