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

December 2002 in “ Biochemical and biophysical research communications ”

Kenji Kizawa, Heinz Troxler, P. Kleinert, Takafumi Inoue, Masahiko Toyoda, Masaaki Morohashi, Claus W. Heizmann

S100A3 S100 family inner endocuticle hair fibers hair damage anion-exchange chromatography 2D gel electrophoresis isoelectric point tandem mass spectrometry N-terminal methionine acetyl group

Studysummary This study reports on the biochemical characteristics of S100A3 protein in human hair cuticle, notably finding its N-terminal methionine is acetylated and has a slightly lower isoelectric point compared to the recombinant version. Our plain-language summary of this paper — not a Tressless recommendation.

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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research Ultrastructural Localization of S100A3, a Cysteine-Rich, Calcium Binding Protein, in Human Scalp Hair Shafts Revealed by Rapid-Freezing Immunocytochemistry

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In this study, the researchers identified the specific subcellular localization of the protein S100A3 in the endocuticle and cortex of human hair shafts.

research Gene Expression of Mouse S100A3, a Cysteine-Rich Calcium-Binding Protein, in Developing Hair Follicle

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This study found that the S100A3 gene is exclusively expressed in hair follicle cells differentiating into hair shaft components in mice, suggesting its important role in hair formation.