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J. Cosmet. Sd., 51, 15-25 (January/February 2000) Elution of S'100Aa from hair fiber: New model for hair damage emphasizing the loss of S'100Aa from cuticle TAKAFUMI INOUE, ICHIRO SASAKI, MASAHITO YAMAGUCHI, and KENJI KIZAWA, Basic Research Laboratory (T.I., LS., K.K.) and Cosmetic Laboratory (M.Y.), Kanebo Ltd., Odawara 5-3-28, Kotobuki-cho, 250-0002, Japan. Accepted for publication December 15, 1999. Presented in part at the 20th Congress International Federation of the Societies of Cosmetic Chemists, Cannes, France, September 14-18, 1998. Synopsis In hair fiber, a cysteine-rich calcium-binding S100A3 protein is segregated in the inner part of the cuticle and postulated to play an important role in the attachment to the adjacent cuticular scale. In this study, elution of S100A3 from hair fiber was examined under various conditions by means of immunoblot analyses. The exposure of hair fiber to permanent waving lotions resulted in recoveries of substantial amounts of S100A3 by elution. Ultraviolet-light radiation and perming also increased the elution of S100A3 even without reductant. The distal part of hair fiber eluted less S100A3, as compared to the proximal section, under reducing conditions. These results suggest that S100A3 is eluted preferentially by daily washing and rinsing, especially from damaged hair. Given the presence of soluble S100A3 in the inner part of cuticle, we propose a new mechanism of hair damage in which the elution of S100A3 plays a major role. INTRODUCTION The structure and chemistry of hair was to be considered in seeking to understand the damaging effects of topically applied preparations (i.e., perming, bleaching, dyeing, and shampooing), environmental influences (i.e., sunlight and oxidants), and mechanical factors (i.e., combing, brushing, and drying). The cuticle has been recognized as a tough and impervious layer providing protection for the hair shaft emerging from the follicle (1). It was shown that the cuticle was damaged before any degradation occurs to the cortex (2). S100A3 protein was identified as a component of cuticle in our previous work (3). Members belonging to a calcium-binding S100 protein family are small, acidic, and soluble, even in 100% saturated ammonium sulfate solutions (4). Among all members, S100A3 possesses the highest cysteine content (10 of 101 amino acids) (5). In particular, we have shown that S100A3 was accumulated primarily in the cuticular cells and, to a lesser extent, in cortical cells, during the maturation of hair in mouse hair follicle (6). Recently, we reported ultrastructural localization of S100A3 in human hair fiber (7). 15