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Kawasaki, Japan

Kizawa K.,Kanebo Cosmetics Inc. | Takahara H.,Ibaraki University | Unno M.,Ibaraki University | Heizmann C.W.,University of Zurich
Biochimie | Year: 2011

Epithelial Ca 2+-regulation, which governs cornified envelope formation in the skin epidermis and hair follicles, closely coincides with the expression of S100A3, filaggrin and trichohyalin, and the post-translational modification of these proteins by Ca 2+-dependent peptidylarginine deiminases. This review summarizes the current nomenclature and evolutional aspects of S100 Ca 2+-binding proteins and S100 fused-type proteins (SFTPs) classified as a separate protein family with special reference to the molecular structure and function of S100A3 dominantly expressed in hair cuticular cells. Both S100 and SFTP family members are identified by two distinct types of Ca 2+-binding loops in an N-terminal pseudo EF-hand motif followed by a canonical EF-hand motif. Seventeen members of the S100 protein family including S100A3 are clustered with seven related genes encoding SFTPs on human chromosome 1q21, implicating their association with epidermal maturation and diseases. Human S100A3 is characterized by two disulphide bridges and a preformed Zn 2+-pocket, and may transfer Ca 2+ ions to peptidylarginine deiminases after its citrullination-mediated tetramerization. Phylogenetic analysis utilizing current genome databases suggests that divergence of the S100A3 gene coincided with the emergence of hair, a defining feature of mammals, and that the involvement of S100A3 in epithelial Ca 2+-cycling occurred as a result of a skin adaptation in terrestrial mammals. © 2011 Elsevier Masson SAS. All rights reserved. Source

Kizawa K.,Kanebo Cosmetics Inc.
Methods in molecular biology (Clifton, N.J.) | Year: 2013

High quantity and quality of recombinant Ca(2+)-binding proteins are required to study their molecular interactions, self-assembly, posttranslational modifications, and biological activities to elucidate Ca(2+)-dependent cellular signaling pathways. S100A3 is a unique member of the S100 protein family with the highest cysteine content (10%). This protein, derived from human hair follicles and cuticles, is characterized by an N-terminal acetyl group and irreversible posttranslational citrullination by peptidylarginine deiminase causing its homotetramer assembly. Insect cells, capable of introducing eukaryotic N-terminus and disulfide bonds, are an appropriate host in which to express this cysteine-rich protein. Four out of ten cysteines in the recombinant S100A3 form two intramolecular disulfide bridges that modulate its Ca(2+)-affinity. Three free thiol groups located at the C-terminus are predicted to form the high-affinity Zn(2+)-binding site. Citrullination of specific arginine residues in native S100A3 can be mimicked by site-directed mutagenic substitution of Arg/Ala. This chapter details our procedures used for the purification and characterization of the human S100A3 protein and its pseudo citrullinated forms expressed in insect cells. Source

Nakagawa N.,Innovative Beauty Science Laboratory | Naito S.,Kao Corporation | Yakumaru M.,Kanebo Cosmetics Inc. | Sakai S.,Innovative Beauty Science Laboratory
Experimental Dermatology | Year: 2011

Natural moisturizing factors (NMFs) play an important role in maintaining the physical properties of the stratum corneum (SC). The relationship between SC water content and NMFs has long been investigated. Recently, we demonstrated that potassium lactate as an NMF increased SC water content more than sodium lactate did. The details of the moisturizing mechanism of NMFs, however, were not revealed. We, therefore, investigated the cause of the SC moisturizing effect of potassium lactate in comparison with sodium lactate. Using differential scanning calorimetry, we found that potassium lactate increased the bound water content of plantar SC more than what sodium lactate did. We also found, however, that the bound water content of the potassium lactate solution was less than that of the sodium lactate solution, suggesting that potassium lactate increased the water molecules interacting with SC components. Moreover, potassium lactate increased the ratio of hydrogen/deuterium exchange at 1340/cm, which represents the OH bending mode, of plantar SC spectra obtained by the attenuated total reflectance infrared spectroscopy. We assign this band to the OH group of the serine residue. These results suggest that potassium lactate increases the water-holding capacity of the SC by increasing interaction between water molecules and the OH group of serine in SC keratin. © 2011 John Wiley & Sons A/S. Source

Sakai S.,Kanebo Cosmetics Inc. | Yamanari M.,University of Tsukuba | Lim Y.,University of Tsukuba | Nakagawa N.,Kanebo Cosmetics Inc. | Yasuno Y.,University of Tsukuba
Biomedical Optics Express | Year: 2011

We performed an in vivo three-dimensional analysis of anisotropic changes in the dermal birefringence of mechanically deformed human skin using polarization-sensitive optical coherence tomography (PS-OCT). The papillary-dermal birefringence of the forehead increased significantly when the skin was shrunk parallel to the body axis, and decreased significantly when the skin was shrunk perpendicular to the body axis. En-face images of the papillary-dermal birefringence revealed variations among individual subjects, and that both shrinking parallel to and stretching in perpendicular to the body axis promoted the formation of macro rope-like birefringent domains. We found that PS-OCT is useful for understanding anisotropic properties of collagen structure in the skin. © 2011 Optical Society of America. Source

Sasaki M.,Kanebo Cosmetics Inc. | Kondo M.,Kanebo Cosmetics Inc. | Sato K.,Kanebo Cosmetics Inc. | Umeda M.,Kanebo Cosmetics Inc. | And 4 more authors.
Pigment Cell and Melanoma Research | Year: 2014

Rhododendrol, an inhibitor of melanin synthesis developed for lightening/whitening cosmetics, was recently reported to induce a depigmentary disorder principally at the sites of repeated chemical contact. Rhododendrol competitively inhibited mushroom tyrosinase and served as a good substrate, while it also showed cytotoxicity against cultured human melanocytes at high concentrations sufficient for inhibiting tyrosinase. The cytotoxicity was abolished by phenylthiourea, a chelator of the copper ions at the active site, and by specific knockdown of tyrosinase with siRNA. Hence, the cytotoxicity appeared to be triggered by the enzymatic conversion of rhododendrol to active product(s). No reactive oxygen species were detected in the treated melanocytes, but up-regulation of the CCAAT-enhancer-binding protein homologous protein gene responsible for apoptosis and/or autophagy and caspase-3 activation were found to be tyrosinase dependent. These results suggest that a tyrosinase-dependent accumulation of ER stress and/or activation of the apoptotic pathway may contribute to the melanocyte cytotoxicity. © 2014 The Authors. Source

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