Abstract
Sheep (Ovis aries) and goats (Capra hircus) have, for more than a millennia, been a source of fibres for human use, be it for use in clothing and furnishings, for insulation, for decorative and ceremonial purposes, or for combinations thereof. While use of these natural fibres has in some respects been superseded by the use of synthetic and plant-based fibres, increased accounting for the carbon and water footprint of these fibres is creating a re-emergence of interest in fibres derived from sheep and goats. The keratin-associated proteins (KAPs) are structural components of wool and hair fibres, where they form a matrix that cross-links with the keratin intermediate filaments (KIFs), the other main structural component of the fibres. Since the first report of a complete KAP protein sequence in the late 1960s, considerable effort has been made to identify the KAP proteins and their genes in mammals, and to ascertain how these genes and proteins control fibre growth and characteristics. This effort is ongoing, with more and more being understood about the structure and function of the genes. This review consolidates that knowledge and suggests future directions for research to further our understanding.
Highlights
The keratin-associated proteins (KAPs) are structural components of the fibres that form the pelage of mammals
The hair and wool fibres are produced by follicles that are located in the skin, but the value of these fibres varies considerably depending on their qualities, including their fineness, their uniformity, their length, and their colour
30 KRTAPs from 18 different families have been identified in sheep and 18 KRTAPs from 12 families have been reported in goats
Summary
The keratin-associated proteins (KAPs) are structural components of the fibres that form the pelage of mammals. In the wool follicles of sheep, the KAPs are produced soon after the synthesis of keratins during the development of fibres in the follicle, and they are thought to cross-link with the KIFs by forming disulphide bonds with cysteine residues in the head and tail domains of the keratins [1]. The nature of this cross-linking is not well understood, and while co-immunoprecipitation studies have demonstrated an interaction between the head domain of human keratin K86 and KAP2-1 [2], and Western blot studies have demonstrated an interaction between the head domain of K85 and KAP81 [2], a complete understanding of which K and KAP cysteine thiol groups form disulphide bridges (be they inter- or intra-chain) is not well known, the bulk of the most readily accessible cysteines in the KAPs are reported to be found close to either the N- or C-terminal domains in these proteins [3]. This has enabled more ovine and caprine KAP genes to be identified and characterized
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