Crosslinking Between Trichocyte Keratins and Keratin Associated Proteins

Adv Exp Med Biol. 2018:1054:173-183. doi: 10.1007/978-981-10-8195-8_12.

Abstract

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.

Keywords: Cysteine accessibility; Disulfide bridges; Keratin associated proteins; Protein crosslinks; Trichocyte keratins.

Publication types

  • Review

MeSH terms

  • Animals
  • Cysteine / chemistry*
  • Hair / ultrastructure*
  • Humans
  • Keratins / chemistry*
  • Wool / ultrastructure*

Substances

  • Keratins
  • Cysteine