S100A3 and its citrullination process are related to rigidity of endocuticle of aged hair.

What is it about?

There are two types of damage pattern of human hair cuticle: type L, where the cell membrane complex is split and the cuticle lifts up, and type E, where the fragile substructure of the cuticle cell (endocuticle) is broken. In our previous paper it was reported that the dominant damage pattern shifts from type L to E with the subjects' age around the 40s. Loss of the cuticle due to daily grooming stresses increases with the subjects' age, and is related to the level of type E damage. It is supposed that deterioration of endocuticle advances the loss of cuticle. S100A3 protein, located at the endocuticle, was found to be citrullinated and transformed into tetramer to improve its Ca2+ binding ability. It is postulated that this biochemical property affects maturation of cuticle and contributes to its reinforcement. This study aims to elucidate the role that S100A3 plays in age-dependent cuticle damage.

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Why is it important?

Our present results firstly showed that S100A3 content and citrullination rate are related with the resistance of hair cuticles. Proper cuticle maturation, which could be estimated using S100A3 protein indexes, is thought to be useful for the prevention of age-related hair deterioration. Individual hairs with low content of extracted S100A3 and/or a higher citrullination rate seem to have an advantage in terms of protecting the cuticle against daily grooming stress.