Crosslinking Between Trichocyte Keratins and Keratin Associated Proteins

  • Santanu Deb-ChoudhuryEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 1054)


Trichocyte keratins differ considerably from their epithelial cousins in having a higher number of cysteine residues, of which the greater proportion are located in the head and tail regions of these proteins. Coupled with this is the presence of a large number of keratin associated proteins in these fibres that are high in their cysteine content, the high sulfur proteins and ultra-high sulfur proteins. Thus it is the crosslinking that occurs between the cysteines in the keratins and KAPs that is an important determinant in the functionality of wool and hair fibres. Studies have shown the majority of the cysteine residues are involved in internal crosslinking in the KAPs leaving only a few specific cysteines to interact with the keratins, with most evidence pointing to interactions between these KAP cysteines and the keratin head groups.


Trichocyte keratins Keratin associated proteins Protein crosslinks Disulfide bridges Cysteine accessibility 


  1. 1.
    Fraser, R. D. B., MacRae, T.P., & Rogers, G. E. (1972). Keratins: Their composition, structure and biosynthesis (The Bannerstone division of American lectures in living chemistry, p. 320). Springfield: Charles C Thomas Publisher, Ltd.Google Scholar
  2. 2.
    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.CrossRefPubMedGoogle Scholar
  3. 3.
    Lee, Y. J., Rice, R. H., & Lee, Y. M. (2006). Proteome analysis of human hair shaft – From protein identification to posttranslational modification. Molecular & Cellular Proteomics, 5(5), 789–800.CrossRefGoogle Scholar
  4. 4.
    Orwin, D. F. G. (1979). The cytology and cytochemistry of the wool follicle. International Review of Cytology, 60, 331–374.CrossRefPubMedGoogle Scholar
  5. 5.
    Hill, P., Brantley, H., & Van Dyke, M. (2010). Some properties of keratin biomaterials: Kerateines. Biomaterials, 31(4), 585–593.CrossRefPubMedGoogle Scholar
  6. 6.
    Alexander, P., & Earland, C. (1950). Structure of wool fibres: Isolation of an α- and β-protein in wool. Nature, 166(4218), 396–397.CrossRefPubMedGoogle Scholar
  7. 7.
    Deb-Choudhury, S., et al. (2015). Mapping the accessibility of the disulfide crosslink network in the wool fiber cortex. Proteins: Structure, Function, and Bioinformatics, 83(2), 224–234.CrossRefGoogle Scholar
  8. 8.
    Arai, K., et al. (1996). Crosslinking structure of keratin. VI. Number, type, and location of disulfide crosslinkages in low-sulfur protein of wool fiber and their relation to permanent set. Journal of Applied Polymer Science, 60(2), 169–179.CrossRefGoogle Scholar
  9. 9.
    Stappenbeck, T. S., et al. (1993). Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks. The Journal of Cell Biology, 123(3), 691–705.CrossRefPubMedGoogle Scholar
  10. 10.
    Getsios, S., et al. (2004). Coordinated expression of desmoglein 1 and desmocollin 1 regulates intercellular adhesion. Differentiation, 72(8), 419–433.CrossRefPubMedGoogle Scholar
  11. 11.
    Syed, S. E., et al. (2002). Molecular interactions between desmosomal cadherins. Biochemical Journal, 362(Pt 2), 317–327.CrossRefPubMedPubMedCentralGoogle Scholar
  12. 12.
    Orwin, D. F. G., & Thomson, R. W. (1973). Plasma membrane differentiations of keratinizing cells of the wool follicle (4. Further membrane differentiations). Journal of Ultrastructure Research, 45(1), 41–49.CrossRefPubMedGoogle Scholar
  13. 13.
    Plowman, J. E., & Deb-choudhury, S. (2016). Wool proteomics. In S. G. H. (Ed.), Animal proteomics (pp. 201–213). Springer.CrossRefGoogle Scholar
  14. 14.
    Steinert, P. M., & Marekov, L. N. (1995). The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. Journal of Biological Chemistry, 270(30), 17702–17711.CrossRefPubMedGoogle Scholar
  15. 15.
    Harding, H. W., & Rogers, G. E. (1971). (γ-glutamyl)lysine cross-linkage in citrulline-containing protein fractions from hair. Biochemistry, 10, 624–630.CrossRefPubMedGoogle Scholar
  16. 16.
    Rogers, G. E. (2004). Hair follicle differentiation and regulation. International Journal of Developmental Biology, 48(2-3), 163–170.CrossRefPubMedGoogle Scholar
  17. 17.
    Rogers, G. E. (2006). Biology of the wool follicle: An excursion into a unique tissue interaction system waiting to be re-discovered. Experimental Dermatology, 15(12), 931–949.CrossRefPubMedGoogle Scholar
  18. 18.
    Zahn, H. (1980). Wool is not keratin only. In Proceedings of the 6th International Wool Textile Research. Pretoria: Deutsches Wollforschungsinstitut.Google Scholar
  19. 19.
    Nienhaus, M. & Föhles, J. (1980). Zur chemie von humanhaar. In 6th quinquennial international wool textile Research conference (pp. 487–495). Pretoria: South African Wool and Textile Reseach Institute.Google Scholar
  20. 20.
    Harding, H. W. J., & Rogers, G. E. (1972). The occurrence of the (γ-glutamyl)lysine cross-link in the medulla of hair and quill. Biochimica et Biophysica Acta, 257(1), 37–39.CrossRefPubMedGoogle Scholar
  21. 21.
    Rogers, G. E. (1989). Special biochemical features of the hair follicle. In G. E. Rogers, P. J. Reis, K. A. Ward, & R. C. Marshall (Eds.), The biology of wool and hair (pp. 69–85). London/New York: Chapman and Hall.CrossRefGoogle Scholar
  22. 22.
    Parry, D. A. D., & Steinert, P. M. (1995). Intermediate filament structure. Heidelberg: Springer.Google Scholar
  23. 23.
    Steinert, P. M. (1993). Structure, function and dynamics of keratin intermediate filaments. Journal of Investigative Dermatology, 100(6), 729–734.CrossRefPubMedGoogle Scholar
  24. 24.
    Gillespie, J. M. (1972). Proteins rich in glycine and tyrosine from keratins. Comparative Biochemistry and Physiology B.Biochemistry and Molecular Biology, 41B, 723–734.CrossRefGoogle Scholar
  25. 25.
    Rafik, M. E., Doucet, J., & Briki, F. (2004). The intermediate filament architecture as determined by X-ray diffraction modeling of hard α-keratin. Biophysical Journal, 86, 3893–3904.CrossRefGoogle Scholar
  26. 26.
    Fraser, R. D. B., MacRae, T. P., & Suzuki, E. (1976). Structure of the α-keratin microfibril. Journal of Molecular Biology, 108, 435–452.CrossRefPubMedGoogle Scholar
  27. 27.
    Parry, D. A., et al. (2007). Towards a molecular description of intermediate filament structure and assembly. Experimental Cell Research, 313(10), 2204–2216.CrossRefPubMedGoogle Scholar
  28. 28.
    Matsunaga, R., et al. (2013). Bidirectional binding property of high glycine-tyrosine keratin-associated protein contributes to the mechanical strength and shape of hair. Journal of Structural Biology, 183(3), 484–494.CrossRefPubMedGoogle Scholar
  29. 29.
    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.CrossRefPubMedGoogle Scholar
  30. 30.
    Parry, D. A. D. (1995). Hard α-keratin IF: A structural model lacking a head-to-tail molecular overlap but having hybrid features characteristic of both epidermal keratin and vimentin IF. Proteins: Structure, Function, and Bioinformatics, 22(3), 267–272.CrossRefGoogle Scholar
  31. 31.
    Parry, D. A. D. (1996). Hard α-keratin intermediate filaments: An alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks. International Journal of Biological Macromolecules, 19(1), 45–50.CrossRefPubMedGoogle Scholar
  32. 32.
    Wang, H., et al. (2000). In vitro assembly and structure of trichocyte keratin intermediate filaments: A novel role for stabilization by disulfide bonding. Journal of Cell Biology, 151(7), 1459–1468.CrossRefPubMedGoogle Scholar
  33. 33.
    Whiteley, K. J., Balasubramaniam, E., & Armstrong, L. D. (1970). The swelling and supercontraction of sulphur-enriched wool fibers. Textile Research Journal, 40, 1047–1048.Google Scholar
  34. 34.
    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.CrossRefPubMedGoogle Scholar
  35. 35.
    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.CrossRefGoogle Scholar
  36. 36.
    Fujimoto, S., et al. (2013). Krtap11-1, a hair keratin-associated protein, as a possible crucial element for the physical properties of hair shafts. Journal of Dermatological Science, 74(1), 39–47.CrossRefPubMedGoogle Scholar
  37. 37.
    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.CrossRefPubMedGoogle Scholar
  38. 38.
    Plowman, J. E., et al. (2003). The effect of oxidation or alkylation on the separation of wool keratin proteins by two-dimensional gel electrophoresis. Proteomics, 3(6), 942–950.CrossRefPubMedGoogle Scholar
  39. 39.
    Benham, C. J., & Saleet Jafri, M. (1993). Disulfide bonding patterns and protein topologies. Protein Science, 2(1), 41–54.CrossRefPubMedPubMedCentralGoogle Scholar
  40. 40.
    Steinert, P. M., et al. (1991). Glycine loops in proteins: Their occurrence in certain intermediate filament proteins, loricrins and single-stranded RNA binding proteins. International Journal of Biological Macromolecules, 13(3), 130–139.CrossRefPubMedGoogle Scholar
  41. 41.
    Fraser, R. D. B., et al. (1988). Disulphide bonding in α-keratin. International Journal of Biological Macromolecules, 10, 106–112.CrossRefGoogle Scholar
  42. 42.
    Parry, D. A. D., et al. (2002). A role for the 1A and L1 rod domain segments in head domain organisation and function of intermediate filaments: Structural analysis of trichocyte keratin. Journal of Structural Biology, 137, 97–108.CrossRefPubMedGoogle Scholar

Copyright information

© Springer Nature Singapore Pte Ltd. 2018

Authors and Affiliations

  1. 1.AgResearch Ltd.LincolnNew Zealand

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