HAIR AND HYDROLYZED WHEAT PROTEINS 203 REFERENCES (1) M. Gamez-Garcia, Effects of some oils, emulsions, and other aqueous systems on the mechanical properties of hair at small deformations, J. Soc. Cosmet. Chem., 44, 69-87 (1993). (2) S. P. Chahal, N. I. Challoner, and R. T. Jones, Moisture regulation of hair by cosmetic proteins as demonstrated by dynamic vapour sorption: A novel efficacy testing technique, Proc. 14th Latin- American and Iberian Cong. Cosmet. Chem., Santiago Chile, 45-56 (1999). (3) R. T. Jones and S. P. Chahal, The use of radiolabelling techniques to measure substantivity to, and penetration into hair of protein hydrolysates, Internat. J. Cosmet. Sci., 19, 215-226 (1997). (4) T. Wilson, Ed., Con•bcal Microscopy (Academic Press, San Diego, 1990). (5) J. A. Swift, "The Detection of Pores and Holes in Hair by Electron Microscopy," in Hair Research fir the Next Millennium, D. J.J. Van Neste and V. A. Randall, Eds. (Elsevier Science BV, Amsterdam, 1996), pp. 109-112. (6) J. A. Swift and B. Bews, The chemistry of human hair cuticle. Part 3. The isolation and amino acid analysis of various subfractions of the cuticle obtained by pronase and trypsin digestion,J. Soc. Cosmet. Chem., 27, 289-300 (1976). (7) J. A. Swift, "The Histology of Keratin Fibers," in The Chemistry of Natural Protein Fibres, R. S. Asquith, Ed. (Plenum Press, New York, 1977), pp. 81-146. (8) P. Kassenbeck, Das haar und seine struktur, Wella AG, Darmstadt, Germany (1984). (9) J. A. Swift and A. K. Allen, "Swelling of Human Hair by Water," in Abstracts of Sth Internat. Hair Sci. Symp., Kiel, Germany (Deutsches Wollforshungsinstitut, Aachen, Germany, 1992). (10) M.A. Pykett and J. A. Swift, Schutz von Haarbruch nachweisen: Ein neues Testverfahren fiir eine bessere Datenbasis, Parr. u. Kosmetik, 79, 38-40 (1998).
j. Cosmet, sci., 51,205-207 (May/June 2000) Abstracts Journal of the Society of Cosmetic Chemists Japan (as published in Vol. 33, No. 2, 1999) The Mechanism of Desquamation in the Stra- tum Comeurn and Its Relevance to Skin Care Junichi Koyama**, Jotaro Nakanishi**, Junko Sato**, Junko Nomura***, Yumiko Suzuki**, Yoshiko Masuda**, Yasuhisa Nakayama** Life Science Research Center**, Basic Research Cen- ter***, Shiseido Co., Ltd. For healthy people, the most common skin problem is the occurrence of visible scales on the skin surface. This phenomenon is commonly seen on dry skin. Many morphological and biochemical studies on the stratum comeurn have revealed the aspects of skin. However, we still do not know why and how scales appear on the skin surface, except that a defect of the desquamation process in the stratum corneum must be involved. In this study, we examined the mecha- nism of desquamation, to establish what factors in- fluence the mechanism and what treatments might be effective for skin care. We found two types of proteases, trypsin type (30 kDa) and chymotrypsin type (25 kDa), in stratum corneum (SC). cDNA cloning followed by nucleotide sequence analysis re- vealed that the chymotrypsin-like protease corre- sponded to the reported chymotrypsin-like enzyme in stratum corneum (SCCE). Trypsin-like protease corresponded to trypsinogen IV and we found new type of trypsinogen. Desmosomes in SC sheets were digested and SC sheets were dissociated into indi- vidual intact cells in buffer solution, whereas heat- treatment or addition of inhibitors of these proteases to the buffer solution prevented the degradation of desmosomes and the cell dissociation. Leupeptin or chymostatin retarded the cell dissociation only about half as effectively as aprotinin, but a mixture of the two inhibited stratum corneum sheet degra- dation as potently as aprotinin. These results sup- port the hypothesis that desmosomes play a key role in the adhesion of SC cells, and the digestion of desmosomes by these two types of serine proteases leads to SC desquamation. An age-related decrease in the activity of the trypsin-type protease was ob- served in normal subjects. Digestion of desmosomes in SC by the proteases was influenced by the water content in SC. Lower humidity (lower water content in stratum corneum) resulted in a decrease of des- mosomal degradation. Our studies demonstrated that desquamation was influenced by two factors. One is water content in the stratum corneum. Under the low water condition enzymes cannot work well, even if the contents of the enzymes are normal. In this case, humectant treatment was effective by sup- plying water to the stratum corneum. The other factor is a decline in the activity of the proteases themselves. This can be seen in diseased or aged skin. Humectant treatment is not sufficient in this case compounds that accelerate desmosomal diges- tion independently of the water content in the stra- tum corneum are required. Derivatives of dicarbox- ylic acid are thought to be the candidate for such ingredients. Key words: stratum corneum, desquamation, prote- ase, dry skin, desmosome, o•-hydroxy acid Evaluation of Pigmentation by Multispectral Image Analysis (Second Report): Reconstruc- tion of Pigmented Images Based Only on the Melanin Component in the Skin Yukiko Kawaguchi, Osamu Kaneko, Institute of Beauty Sciences, Shiseido Co., Ltd. Conventional digitized images of pigmented skin include both coloring caused by melanin and color- ing contributed by other skin factors. To accurately quantify the darkness of pigmented skin, only mela- nin should be considered. Coefficients for weighting M 1 and M 2 for the reflected light constituent factors 205
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202 JOURNAL OF COSMETIC SCIENCE Figure 7. A split end treated for 30 minutes with fluorescein-labeled peptides. Block top method. The hair has split into many separated fragments. Intense staining of the cortical nuclear remnants is still visible but not as sharp as in less damaged hairs. The continuous low level of fluorescence indicates that the peptides have permeated throughout the entire specimen. pervaded all parts, but it was noticeable that the nuclear remnants were not as sharply defined as had been seen in untreated hairs and of much lower intensity. The most likely reason for this is that effete basic nuclear proteins, normally found in untreated hairs, had been extracted during the multifarious processes of weathering. IMPLICATIONS FOR TOILETRY TREATMENTS OF HAIR Since water normally plasticizes and softens hair, the results of Gamez-Garcia (1) and Chahal et al. (2) provide expectations for significant changes in the textural behavior of human hair following treatment with hydrolyzed wheat proteins. The relatively un- crosslinked proteins of the hair's intermacrofibrillar matrix are major sites for binding water (9) and can be regarded as the main plasticizing elements separating the stiffer macrofibrils in undamaged root-end hair. Exposure of hair to excessive sunlight dra- matically increases its susceptibility to splitting (10), likely through the formation of new crosslinks in the intermacrofibrillar matrix but also through a loss of water-binding capacity. The absorption of hydrolyzed wheat proteins will increase the plasticity of hair in general by dint of their ability to retain moisture for long periods. We predict that their specific incorporation into the very components that are damaged by sunlight exposure will render the hair less susceptible to the formation of split ends. ACKNOWLEDGMENTS Particular thanks are due to Dr. Vyvyan Howard of the Department of Infant and Fetal Toxico-Pathology of Liverpool University for providing access to his confocal microscope and to Mr. Liam Barlow of the same department for technical assistance with the work.
HAIR AND HYDROLYZED WHEAT PROTEINS 203 REFERENCES (1) M. Gamez-Garcia, Effects of some oils, emulsions, and other aqueous systems on the mechanical properties of hair at small deformations, J. Soc. Cosmet. Chem., 44, 69-87 (1993). (2) S. P. Chahal, N. I. Challoner, and R. T. Jones, Moisture regulation of hair by cosmetic proteins as demonstrated by dynamic vapour sorption: A novel efficacy testing technique, Proc. 14th Latin- American and Iberian Cong. Cosmet. Chem., Santiago Chile, 45-56 (1999). (3) R. T. Jones and S. P. Chahal, The use of radiolabelling techniques to measure substantivity to, and penetration into hair of protein hydrolysates, Internat. J. Cosmet. Sci., 19, 215-226 (1997). (4) T. Wilson, Ed., Con•bcal Microscopy (Academic Press, San Diego, 1990). (5) J. A. Swift, "The Detection of Pores and Holes in Hair by Electron Microscopy," in Hair Research fir the Next Millennium, D. J.J. Van Neste and V. A. Randall, Eds. (Elsevier Science BV, Amsterdam, 1996), pp. 109-112. (6) J. A. Swift and B. Bews, The chemistry of human hair cuticle. Part 3. The isolation and amino acid analysis of various subfractions of the cuticle obtained by pronase and trypsin digestion,J. Soc. Cosmet. Chem., 27, 289-300 (1976). (7) J. A. Swift, "The Histology of Keratin Fibers," in The Chemistry of Natural Protein Fibres, R. S. Asquith, Ed. (Plenum Press, New York, 1977), pp. 81-146. (8) P. Kassenbeck, Das haar und seine struktur, Wella AG, Darmstadt, Germany (1984). (9) J. A. Swift and A. K. Allen, "Swelling of Human Hair by Water," in Abstracts of Sth Internat. Hair Sci. Symp., Kiel, Germany (Deutsches Wollforshungsinstitut, Aachen, Germany, 1992). (10) M.A. Pykett and J. A. Swift, Schutz von Haarbruch nachweisen: Ein neues Testverfahren fiir eine bessere Datenbasis, Parr. u. Kosmetik, 79, 38-40 (1998).

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