Abstract
Wool and hair fibres are primarily composed of proteins of which the keratins and keratin associated proteins (KAPs) are the major component. Considerable diversity is known to exist within these two groups of proteins. In the case of the keratins two major families are known, of which there are 11 members in the acidic Type I family and 7 members in the neutral-basic Type II family. The KAPs are even more diverse than the keratins, with 35 families being known to exist when the KAPs found in monotremes, marsupials and other mammalian species are taken into consideration. Human hair and wool are known to have 88 and 73 KAPs respectively, though this number rises for wool when polymorphism within KAP families is included.
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References
Shorland, F. B., & Gray, J. M. (1970). The preparation of nutritious protein from wool. British Journal of Nutrition, 24, 717.
Gillespie, J. M., & Goldsmith, L. A. (1983). The structural proteins of hair: Isolation, characterization, and regulation of biosynthesis. In L. A. Goldsmith (Ed.), Biochemistry and physiology of the skin (pp. 475–510). Oxford: Oxford University Press.
Goddard, D. R., & Michaelis, L. (1934). A study on keratin. Journal of Biological Chemistry, 106, 605–614.
Crewther, W. G., & Lennox, F. G. (1975). Wool research in the division of protein chemistry, CSIRO. Proceedings of the Royal Society of New South Wales, 108(3 &4), 95–110.
Crewther, W. G., et al. (1980). The microfibrillar proteins of α-keratin. In D. A. D. Parry & L. K. Creamer (Eds.), Fibrous proteins: Scientific, industrial and medical aspects (pp. 151–159). London: Academic Press.
Powell, B. C. (1996). The keratin proteins and genes of wool and hair. Wool Technology and Sheep Breeding, 44(2), 100–118.
Powell, B. C., & Rogers, G. E. (1997). The role of keratin proteins and their genes in the growth, structure and properties of hair. In P. Jolles, H. Zahn, & H. Hoecker (Eds.), Formation and structure of human hair (pp. 59–148). Basel: Birkhäuser Verlag.
Moll, R., Franke, W. W., & Schiller, D. L. (1982). The catalog of human cytokeratins: Patterns of expression in normal epithelia, tumors and cultured cells. Cell, 31, 11–24.
Heid, H. W., Werner, E., & Franke, W. W. (1986). The complement of native α-keratin polypeptides of hair-forming cells: A subset of eight polypeptides that differ from epithelial cytokeratins. Differentiation, 32, 101–119.
Rogers, M. A., et al. (1998). Characterization of a 190-kilobase pair domain of human type I hair keratin genes. Journal of Biological Chemistry, 273(41), 26683–26691.
Rogers, M. A., et al. (2000). Characterization of a 300 kbp region of human DNA containing the type II hair keratin gene domain. Journal of Investigative Dermatology, 114(3), 464–472.
Langbein, L., et al. (1999). The catalog of human hair keratins. I. Expression of the nine type I members in the hair follicle. Journal of Biological Chemistry, 274(28), 19874–19884.
Plowman, J. E., et al. (2006). Wool keratins – The challenge ahead. Proceedings of the New Zealand Society of Animal Production, 66, 133–139.
Schweizer, J., et al. (2006). New consensus nomenclature for mammalian keratins. Journal of Cell Biology, 174(2), 169–174.
Gillespie, J. M., & Broad, A. (1972). Ultra-high sulphur proteins in the hairs of the Artiodactyla. Australian Journal of Biological Science, 25, 139–145.
Stein, W. H., & Moore, S. (1948). Chromatography of amino acids on starch columns; separation of phenylalanine, leucine, isoleucine, methionine, tyrosine and valine. Journal of Biological Chemistry, 176, 337–365.
Harrap, B. S., & Gillespie, J. M. (1963). A further study on the extraction of reduced proteins from wool. Australian Journal of Biological Science, 16, 542–557.
Crewther, W. G. (1975). Primary structure and chemical properties of wool. In Proceedings of the 5th International Wool Textile Research conference. Aachen, Germany.
Lindley, H., & Elleman, T. C. (1972). The preparation and properties of a group of proteins from the high-sulphur fraction of wool. Biochemical Journal, 128, 859–867.
Swart, L. S., Joubert, F. J., & Strydom, A. J. C. (1969). The apparent microheterogeneous nature of the high-sulfur proteins of à -keratins. Textile Research Journal, 39, 273–279.
Haylett, T., Swart, L. S., & Parris, D. (1971). Studies on the high-sulphur proteins of reduced merino wool. Amino acid sequence of protein SCMKB-IIIB 3. Biochemical Journal, 123(2), 191–200.
Haylett, T., & Swart, L. S. (1969). Studies on the high-sulfur proteins of reduced Merino wool. Part III. The amino-acid sequence of protein SCMKB-IIIB2. Textile Research Journal, 39, 917.
Swart, L. S., & Haylett, T. (1971). Studies on the high-sulphur proteins of reduced merino wool. Amino acid sequence of protein SCMKB-IIIB 4. Biochemical Journal, 123(2), 201–210.
Gillespie, J. M., & Darskus, R. L. (1971). Relation between the tyrosine content of various wools and their content of a class of proteins rich in tyrosine and glycine. Australian Journal of Biological Science, 24, 1189–1197.
Gillespie, J. M. (1991). The structural proteins of hair: isolation, characterisation and regulation of biosynthesis. In L. A. Goldsmith (Ed.), Physiology, biochemistry and molecular biology of the skin (Vol. 1, 2nd ed., pp. 625–659). New York: Oxford University Press.
Powell, B. C., & Beltrame, J. S. (1994). Characterization of a hair (wool) keratin intermediate filament gene domain. Journal of Investigative Dermatology, 102(2), 171–177.
Fratini, A., Powell, B. C., & Rogers, G. E. (1993). Sequence, expression, and evolutionary conservation of a gene encoding a glycine/tyrosine-rich keratin-associated protein of hair. Journal of Biological Chemistry, 268(6), 4511–4518.
MacKinnon, P. J., Powell, B. C., & Rogers, G. E. (1990). Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles. Journal of Cell Biology, 111(6), 2587–2600.
Jenkins, B. J., & Powell, B. C. (1994). Differential expression of genes encoding a cysteine-rich keratin family in the hair cuticle. Journal of Investigative Dermatology, 103(3), 310–317.
Fratini, A., et al. (1994). Dietary cysteine regulates the levels of mRNAs encoding a family of cysteine-rich proteins of wool. Journal of Investigative Dermatology, 102(2), 178–185.
Powell, B. C., Arthur, J. R., & Nesci, A. (1995). Characterisation of a gene encoding a cysteine-rich keratin associated protein synthesised late in rabbit hair follicle differentiation. Differentiation, 58, 227–232.
Gong, H., et al. (2012). An updated nomenclature for keratin-associated proteins (KAPs). International Journal of Biological Sciences, 8(2), 258–264.
Rogers, M. A., & Schweizer, J. (2005). Human KAP genes, only the half of it? Extensive polymorphisms in hair keratin-associated protein genes. Journal of Investigative Dermatology, 124, vii–vix.
Rogers, M. A., et al. (2006). Human hair keratin-associated proteins (KAPs). International Review of Cytology, 251, 209–263.
Itenge-Mweza, T. O., et al. (2007). Polymorphism of the KAP1.1, KAP1.3 and KRT.1.2 genes in merino sheep. Molecular and Cellular Probes, 21(5–6), 338–342.
Gong, H., Zhou, H., & Hickford, J. G. (2010). Polymorphism of the ovine keratin-associated-protein 1-4 (KRTAP1-4) gene. Molecular Biology Reports, 37, 3377–3380.
Gong, H., et al. (2011). Identification of the ovine keratin-associated protein KAP1-2 gene (KRTAP1-2). Experimental Dermatology, 20, 815–819.
Gong, H., Zhou, H., & Hickford, J. G. (2011). Diversity of the glycine/tyrosine-rich keratin-associated protein 6 gene (KAP6) family in sheep. Molecular Biology Reports, 38(1), 31–35.
Gong, H., et al. (2011). Identification of the ovine KAP11-1 gene (KRTAP11-1) and genetic variation in its coding sequence. Molecular Biology Reports, 38(8), 5429–5433.
Gong, H., et al. (2011). Search for variation in the ovine KAP7-1 and KAP8-1 genes using PCR-SSCP. DNA and Cell Biology, 31(3), 367–370.
Shimomura, Y., et al. (2002). Polymorphisms in the human high sulfur hair keratin-associated protein 1, KAP1, gene family. Journal of Biological Chemistry, 277(47), 45493–45501.
Wu, D.-D., Irwin, D. M., & Zhang, Y.-P. (2008). Molecular evolution of the keratin associated protein gene family in mammals, role in the evolution of mammalian hair. BMC Evolutionary Biology, 25(8), 241–255.
Langbein, L., et al. (2007). Novel type I hair keratins K39 and K40 are the last to be expressed in differentiation of the hair: Completion of the human hair keratin catalogue. Journal of Investigative Dermatology, 127, 1532–1535.
Yu, Z., et al. (2011). Annotations of sheep keratin intermediate filament genes and their patterns of expression. Experimental Dermatology, 20(7), 582–588.
Langbein, L., et al. (2010). The keratins of the human beard hair medulla: The riddle in the middle. Journal of Investigative Dermatology, 130(1), 55–73.
Deb-Choudhury, S., et al. (2010). Electrophoretic mapping of highly homologous keratins: A novel marker peptide approach. Electrophoresis, 31(17), 2894–2902.
Langbein, L., et al. (2001). The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins. Journal of Biological Chemistry, 276(37), 35123–35132.
Elleman, T. C. (1972). The amino acid sequence of protein SCMK-B2A from the high-sulphur fraction of wool keratin. Biochemical Journal, 130(3), 833–845.
Elleman, T. C. (1972). The amino acid sequence of protein SCMK-B2C from the high-sulphur fraction of wool keratin. Biochemcal Journal, 128, 1229–1239.
Elleman, T. C., & Dopheide, T. A. (1972). The sequence of SCMK-B2B, a high-sulfur protein from wool keratin. Journal of Biological Chemistry, 247(12), 3900–3909.
Powell, B. C., et al. (1983). Mammalian keratin gene families: Organisation of genes coding for the B2 high-sulphur proteins of sheep wool. Nucleic Acids Research, 11(16), 5327–5346.
Rogers, G. R., Hickford, J. G., & Bickerstaffe, R. (1994). Polymorphism in two genes for B2 high sulfur proteins of wool. Animal Genetics, 25(6), 407–415.
Rogers, M. A., et al. (2001). Characterization of a cluster of human high/ultrahigh sulfur keratin-associated protein genes embedded in the type I keratin gene domain on chromosome 17q12-21. Journal of Biological Chemistry, 276(22), 19440–19451.
Flanagan, L. M., Plowman, J. E., & Bryson, W. G. (2002). The high sulphur proteins of wool: Towards an understanding of sheep breed diversity. Proteomics, 2(9), 1240–1246.
Swart, L. S., & Haylett, T. (1973). Studies on the high-sulphur proteins of reduced merino wool. Amino acid sequence of protein SCMKB-IIIA3. Biochemical Journal, 133(4), 641–654.
Fujikawa, H., et al. (2012). Characterization of the human hair keratin-associated protein 2 (KRTAP2) gene family. Journal of Investigative Dermatology, 132(7), 1806–1813.
Frenkel, M. J., et al. (1989). The keratin BIIIB gene family: Isolation of cDNA clones and structure of a gene and a related pseudogene. Genomics, 4, 182–191.
Yu, Z., et al. (2009). Expression patterns of keratin intermediate filament and keratin associated protein genes in wool follicles. Differentiation, 77(3), 307–316.
Rogers, M. A., et al. (2002). Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1. Journal of Biological Chemistry, 277(50), 48993–49002.
Parry, D. A. D., et al. (2006). Human hair keratin-associated proteins: Sequence regularities and structural implications. Journal of Structural Biology, 155(2), 361–369.
Shimomura, Y., et al. (2010). Mutations in the keratin 85 (KRT85/hHb5) gene underlie pure hair and nail ectodermal dysplasia. Journal of Investigative Dermatology, 130, 892–895.
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Plowman, J.E. (2018). Diversity of Trichocyte Keratins and Keratin Associated Proteins. In: Plowman, J., Harland, D., Deb-Choudhury, S. (eds) The Hair Fibre: Proteins, Structure and Development. Advances in Experimental Medicine and Biology, vol 1054. Springer, Singapore. https://doi.org/10.1007/978-981-10-8195-8_3
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DOI: https://doi.org/10.1007/978-981-10-8195-8_3
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