Known and Unknown Features of Hair Cuticle Structure: A Brief Review

Cosmetics - Tập 6 Số 2 - Trang 32
George E. Rogers1
1Molecular and Biomedical Sciences, University of Adelaide, Adelaide, SA 5005, Australia

Tóm tắt

The cuticle is the outermost layer of overlapping flattened cells of hair and has been subjected to many years of study to understand its structure and how it develops in the follicle. The essential function of the cuticle with its tough inelastic protein content is to protect the inner cortex that provides the elastic properties of hair. Progress in our knowledge of hair came from studies with the electron microscope, initially transmission electron microscopy (TEM) for internal structure and later the scanning electron microscope (SEM) for cuticle surface shape and for investigating changes caused by various environmental influences such as cosmetic treatments and industrial processing of wool. Other physical techniques have been successfully applied in conjunction with proteomics. The outstanding internal features of the cuticle cells are the internal layers consisting of keratin filament proteins and the keratin-associated proteins. The stability and physical toughness of the cuticle cell is partly accounted for by the high content of disulphide crosslinking. The material between the cells that holds them tightly together, the cell membrane complex, consists of a layer of lipid on both sides of a central protein layer. The lipid contains 18-methyleicosanoic acid that is part of the hydrophobic lipid surface of hair. For the past decade there have been aspects that remained unanswered because they are difficult to study. Some of these are discussed in this brief review with suggestions for experimental approaches to shed more light.

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Tài liệu tham khảo

Auber, 1951, The anatomy of follicles producing wool fibres with special reference to keratinization, Trans. R. Soc. Edinb., 62, 191, 10.1017/S0080456800009285

Rogers, 1959, Electron microscope studies of hair and wool, Ann. N. Y. Acad. Sci., 83, 378, 10.1111/j.1749-6632.1960.tb40914.x

Rogers, 1959, Electron. microscopy of wool, J. Ultrastruct. Res., 2, 309, 10.1016/S0022-5320(59)80004-6

Parry, D.A.D., and Creamer, L.K. (1980). Studies on the surface layers of the wool fibre cuticle. Fibrous Proteins: Scientific, Medical and Industrial Aspects, Academic Press.

Orwin, 1979, The cytology and cytochemistry of the wool follicle, Int. Rev. Cytol., 60, 331, 10.1016/S0074-7696(08)61266-8

Forslind, B., and Lindberg, M. (2003). The hair fibre surface. Skin, Hair and Nails, CRC.

Evans, D.J., Leeder, J.D., Rippon, J.A., and Rivett, D.E. (September, January 28). Separation and analysis of surface lipids of the wool fibre. Proceedings of the 7th International Wool Textile Research Conference, Tokyo, Japan.

Negri, 1991, The nature of covalently bound fatty acids in wool fibres, Aust. J. Agric. Res., 42, 1285, 10.1071/AR9911285

Negri, 1993, A model for the surface of keratin fibres, Text. Res. J., 63, 109, 10.1177/004051759306300207

Ward, 1993, Surface analysis of wool by X-ray photoelectron spectroscopy and static secondary ion mass spectrometry, Text. Res. J., 63, 362, 10.1177/004051759306300609

Jones, 1997, The role of 18-methyleicosanoic acid in the structure and formation of mammalian hair fibres, Micron, 28, 469, 10.1016/S0968-4328(97)00039-5

Zahn, 1994, Covalently-linked fatty acids at the surface of wool: Part of the “cuticle cell envelope, Text. Res. J., 64, 554, 10.1177/004051759406400910

Kizawa, 1996, Highly expressed S100A3, a calcium binding protein in human hair cuticle, Biochim. Biophys. Acta, 13, 94, 10.1016/0167-4889(96)00023-7

Lindberg, 1948, Occurrence of thin membranes in the structure of wool, Nature, 162, 458, 10.1038/162458b0

vonAllworden, 1916, The properties of wool and a new chemical method for detecting damaged wool, Angew. Chem., 29, 77

Bradbury, 1970, Keratin fibres. IV. Structure of the cuticle, Aust. J. Biol. Sci., 23, 843, 10.1071/BI9700843

King, 1968, The chemical composition of wool. V: The epicuticle, Aust. J. Biol. Sci., 21, 375, 10.1071/BI9680375

Rogers, 1977, The origin of citrulline-containing proteins in the hair follicle and the chemical nature of trichohyalin, an intracellular precursor, Biochim. Biophys. Acta, 495, 159, 10.1016/0005-2795(77)90250-1

Rogers, 1958, Some observations on the proteins of the inner root sheath cells of hair follicles, Biochim. Biophys. Acta, 29, 33, 10.1016/0006-3002(58)90143-4

Rogers, 1959, Newer findings on the enzymes and proteins of hair follicles, Ann. N. Y. Acad. Sci., 83, 408, 10.1111/j.1749-6632.1960.tb40916.x

Leeder, J.D. (1984). Wool-Nature’s Wonder Fibre, Australasian Textile Publishers.

Jones, 1994, Formation of surface membranes in developing mammalian hair fibres, Micron, 25, 589, 10.1016/0968-4328(94)90021-3

Swift, 1974, The chemistry of human hair cuticle- II: The isolation and amino acid analysis of the cell membranes and A-layer, J. Soc. Cosmet. Chem., 25, 355

Jones, 1996, Hairs from patients with maple syrup urine disease show a structural defect in the fiber cuticle, J. Investig. Dermatol., 106, 461, 10.1111/1523-1747.ep12343618

Fujikawa, 2013, Characterization of the human hair shaft cuticle-specific keratin-associated protein 10 family, J. Investig. Dermatol., 133, 2780, 10.1038/jid.2013.233

Bringans, 2007, Characterization of the exocuticle a-layer proteins of wool, Exp. Dermatol., 16, 951, 10.1111/j.1600-0625.2007.00610.x

Drisdel, 2004, Labeling and quantifying sites of protein palmitoylation, Biotechniques, 36, 276, 10.2144/04362RR02