Abstract
Wool is almost entirely composed of proteins, the major component of which are the keratins and the keratin-associated proteins (KAPs). Though they were first identified in 1934, it is only comparatively recently that they have been subject to study using modern proteomic techniques. Using a variety of approaches both gel and gel-free proteomics, many new keratins and KAPs have been identified and characterised in the mature fibre and its various subcomponents as well as through the various stages of keratinisation of wool follicle. Preliminary studies have also revealed distinctive differences both within and between breeds. Proteomic approaches have also allowed investigations to be extended into examining the effect of feed restriction on protein composition as well as modifications to the proteins caused by either environmental or process damage.
Similar content being viewed by others
Abbreviations
- %T:
-
Total percentage of acrylamide
- 2DE:
-
Two-dimensional electrophoresis
- ESI:
-
Electro-spray ionisation
- HGTP:
-
High-glycine-tyrosine protein
- HSP:
-
High-sulphur protein
- KAP:
-
Keratin-associated protein
- LC:
-
Liquid chromatography
- MALDI:
-
Matrix-assisted adsorption/desorption ionisation
- MS:
-
Mass spectrometry
- TOF:
-
Time of flight
- UHSP:
-
Ultrahigh-sulphur protein
References
Almeida AM, Plowman JE, Harland DP, Thomas A, Kilminster T, Scanlon T, Milton J, Greeff J, Oldham C, Clerens S (2014) Influence of feed restriction on the wool proteome: a combined iTRAQ and fiber structural study. J Proteomics 103:170–177. https://doi.org/10.1016/j.jprot.2014.03.036
Bringans SD, Plowman JE, Dyer JM, Clerens S, Vernon JA, Bryson WG (2007) Characterization of the exocuticle a-layer proteins of wool. Exp Dermatol 16:951–960. https://doi.org/10.1111/j.1600-0625.2007.00610.x
Clerens S, Cornellison CD, Deb-Choudhury S, Thomas A, Plowman JE, Dyer JM (2010) Developing the wool proteome. J Proteomics 73:1722. https://doi.org/10.1016/j.jprot.2010.05.005
Cottle DJ (1991) Australian sheep and wool handbook, 1st edn. Inkata Press, Melbourne
Deb-Choudhury S, Plowman JE, Rao K, Lee E, van Koten C, Clerens S, Dyer JM, Harland DP (2015) Mapping the accessibility of the disulfide crosslink network in the wool fiber cortex. Proteins 83:224–234. https://doi.org/10.1002/prot.24727
Deb-Choudhury S, Plowman JE, Thomas A, Krsinic GL, Dyer JM, Clerens S (2010) Electrophoretic mapping of highly homologous keratins: a novel marker peptide approach. Electrophoresis 31:2894–2902. https://doi.org/10.1002/elps.201000134
Dowling LM, Ley KF, Pearce AM (1990) The protein composition of cells in the wool cortex. In: Proceedings of the 8th International Wool Textile Research Conference. pp 205–214
Dyer JM, Bringans SD, Aitken GD, Joyce NI, Bryson WG (2007) Extraction and characterisation of non-scourable chromophores from discoloured fleece wool. Color Technol 123:54–58. https://doi.org/10.1111/j.1478-4408.2006.00060.x
Dyer JM, Bringans SD, Bryson WG (2006a) Characterisation of photo-oxidation products within photoyellowed wool proteins: tryptophan and tyrosine derived chromophores. Photochem Photobiol Sci 5:698–706. https://doi.org/10.1039/b603030k
Dyer JM, Bringans SD, Bryson WG (2006b) Determination of photo-oxidation products within photoyellowed bleached wool proteins. Photochem Photobiol 82:551–557. https://doi.org/10.1562/2005-08-29-RA-663
Dyer JM, Plowman J, Krsinic G, Deb-Choudhury S, Koehn H, Millington K, Clerens S (2010) Proteomic evaluation and location of UVB-induced photomodification in wool. Photochem Photobiol B Biol 98:118–127. https://doi.org/10.1016/j.jphotobiol.2009.11.008
Flanagan LM, Plowman JE, Bryson WG (2002) The high sulphur proteins of wool: towards an understanding of sheep breed diversity. Proteomics 2:1240–1246. https://doi.org/10.1002/1615-9861(200209)2:9<1240::AID-PROT1240>3.0.CO;2-#
Goddard DR, Michaelis L (1934) A study on keratin. J Biol Chem 106:605–614
Gong H, Zhou H, Dyer J, Hickford J (2011) Identification of the ovine KAP11-1 gene (KRTAP11-1) and genetic variation in its coding sequence. Mol Biol Rep 38:5429–5433. https://doi.org/10.1007/s11033-011-0697-2
Grosvenor AJ, Morton JD, Dyer JM (2012) Determination and validation of markers for heat-induced damage in wool proteins. Am J Anal Chem 3:431–436. https://doi.org/10.4236/ajac.2012.36056
Grosvenor AJ, Plowman JE, Dyer JM (2009) Targeted mitigation of non-scourable wool discolouration. Int J Sheep Wool Sci 57:Article 9
Herbert BR, Chapman AL, Rankin DA (1996) Investigation of wool protein heterogeneity using two-dimensional electrophoresis with immobilised pH gradients. Electrophoresis 17:239–243. https://doi.org/10.1002/elps.1150170141
Herbert BR, Molloy MP, Gooley AA, Walsh BJ, Bryson WG, Williams KL (1998) Improved protein solubility in two-dimensional electrophoresis using tributyl phosphine as reducing agent. Electrophoresis 19:845–851
Herbert BR, Molloy MP, Yan JX, Gooley AA, Bryson WG, Williams KL (1997) Characterisation of wool intermediate filament proteins separated by micropreparative two-dimensional electrophoresis. Electrophoresis 18:568–572. https://doi.org/10.1002/elps.1150180339
Herbert BR, Woods JL (1994) Immobilised pH gradient isoelectric focusing of wool proteins. Electrophoresis 15:972–976. https://doi.org/10.1002/elps.11501501142
Koehn H, Clerens S, Deb-Choudhury S, Morton JD, Dyer JM, Plowman JE (2010) The proteome of the wool cuticle. J Proteome Res 9:2920–2928. https://doi.org/10.1021/pr901106m
Langbein L, Rogers MA, Praetzel-Wunder S, Böckler D, Schirmacher P, Schweizer J (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. J Invest Dermatol 127:1532–1535
Langbein L, Rogers MA, Winter H, Praetzel S, Beckhaus U, Rackwitz H-R, Schweizer J (1999) The catalog of human hair keratins. I. Expression of the nine type I members in the hair follicle. J Biol Chem 274:19874–19884. https://doi.org/10.1074/jbc.274.28.19874
Langbein L, Rogers MA, Winter H, Praetzel S, Schweizer J (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. J Biol Chem 276:35123–35132. https://doi.org/10.1074/jbc.M103305200
MacKinnon PJ, Powell BC, Rogers GE (1990) Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles. J Cell Biol 111:2587–2600. https://doi.org/10.1083/jcb.111.6.2587
Marshall RC (1981) Analysis of the proteins from single wool fibers by two-dimensional polyacrylamide gel electrophoresis. Text Res J 51:106–108
Marshall RC, Ley KF (1986) Examination of proteins from wool cuticle by two-dimensional gel electrophoresis. Text Res J 56:772–774
Marshall RC, Orwin DFG, Gillespie JM (1991) Structure and biochemistry of mammalian hard keratin. Electron Microsc Rev 4:47–83
Parry DAD, Smith TA, Rogers MA, Schweizer J (2006) Human hair keratin-associated proteins: sequence regularities and structural implications. J Struct Biol 155:361–369. https://doi.org/10.1016/j.jsb.2006.03.018
Parry DAD, Steinert PM (1995) Intermediate filament structure. Springer, Heidelberg, Germany
Paton LN, Gerrard JA, Bryson WG (2008) Investigations into charge heterogeneity of wool intermediate filament proteins. J Proteomics 71:513–529. https://doi.org/10.1016/j.jprot.2008.08.001
Peter M, Heitlinger E, Häner M, Aebi U, Nigg EA (1991) Disassembly of in vitro formed lamin head-to-tail polymers by CDC2 kinase. EMBO J 10:1535–1544
Plowman JE, Bryson WG, Flanagan LM, Jordan TW (2002) Problems associated with the identification of proteins in homologous families: the wool keratin family as a case study. Anal Biochem 300:221–229. https://doi.org/10.1006/abio.2001.5459
Plowman JE, Bryson WG, Jordan TW (2000) Application of proteomics for determining protein markers for wool quality traits. Electrophoresis 21:1899–1906. https://doi.org/10.1002/(SICI)1522-2683(20000501)21:9<1899::AID-ELPS1899>3.0.CO;2-R
Plowman JE, Deb-Choudhury S, Bryson WG, Clerens S, Dyer JM (2009) Protein expression in orthocortical and paracortical cells of merino wool fibers. J Agric Food Chem 57:2174–2180. https://doi.org/10.1021/jf803290h
Plowman JE, Deb-Choudhury S, Thomas A, Clerens S, Cornellison CD, Grosvenor AJ, Dyer JM (2010) Characterisation of low abundance wool proteins through novel differential extraction techniques. Electrophoresis 31:1937–1946. https://doi.org/10.1002/elps.201000053
Plowman JE, Flanagan LM, Paton LN, Fitzgerald AC, Joyce NI, Bryson WG (2003) The effect of oxidation or alkylation on the separation of wool keratin proteins by two-dimensional gel electrophoresis. Proteomics 3:942–950. https://doi.org/10.1002/pmic.200300419
Plowman JE, Harland DP, Ganeshan S, Woods JL, van Shaijik B, Deb-Choudhury S, Thomas A, Clerens S, Scobie DR (2015) The proteomics of wool fibre morphogenesis. J Struct Biol 191:341–351. https://doi.org/10.1016/j.jsb.2015.07.005
Powell BC (1996) The keratin proteins and genes of wool and hair. Wool Tech Sheep Breed 44:100–118
Powell BC, Rogers GE (1997) The role of keratin proteins and their genes in the growth, structure and properties of hair. In: Formation and structure of human hair. Birkhäuser, Basel, pp 59–148
Rogers MA, Langbein L, Praetzel-Wunder S, Giehl K (2008) Characterization and expression analysis of the hair keratin associated protein KAP26.1. Br J Dermatol 159:725–729. https://doi.org/10.1111/j.1365-2133.2008.08743.x
Rogers MA, Langbein L, Winter H, Ehmann C, Praetzel S, Korn B, Schweizer J (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. J Biol Chem 276:19440–19451. https://doi.org/10.1074/jbc.M100657200
Rogers MA, Langbein L, Winter H, Ehmann C, Praetzel S, Schweizer J (2002) Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1. J Biol Chem 277:48993–49002. https://doi.org/10.1074/jbc.M206422200
Yu Z, Gordon SW, Nixon AJ, Bawden CS, Rogers MA, Wildermoth JE, Maqbool NJ, Pearson AJ (2009) Expression patterns of keratin intermediate filament and keratin associated protein genes in wool follicles. Differentiation 77:307–316. https://doi.org/10.1016/j.diff.2008.10.009
Yu Z, Wildermoth JE, Wallace OAM, Gordon SW, Maqbool NJ, MacLean P, Nixon AJ, Pearson AJ (2011) Annotations of sheep keratin intermediate filament genes and their patterns of expression. Exp Dermatol 20:582–588. https://doi.org/10.1111/j.1600-0625.2011.01274.x
Zeuner FE (1963) A history of domesticated animals. Hutchinson, London
Zhou H, Gong H, Yan W, Luo Y, Hickford JG (2012) Identification and sequence analysis of the keratin-associated protein 24-1 (KAP24-1) gene homologue in sheep. Gene 511:62–65
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer International Publishing AG
About this chapter
Cite this chapter
Plowman, J.E. (2018). Proteomics in Wool and Fibre Research. In: de Almeida, A., Eckersall, D., Miller, I. (eds) Proteomics in Domestic Animals: from Farm to Systems Biology. Springer, Cham. https://doi.org/10.1007/978-3-319-69682-9_14
Download citation
DOI: https://doi.org/10.1007/978-3-319-69682-9_14
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-69681-2
Online ISBN: 978-3-319-69682-9
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)