The Proteins of Hair and Other Hard α-Keratins

Gillespie, J. M.

doi:10.1007/978-1-4757-9604-9_4

Cited by 69 publications

(27 citation statements)

References 61 publications

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“…The biochemical function of copper is unknown but the oxidation of SH groups to SS bonds might be by copper alone or as a component of an enzyme that has SH oxidation activity (85,87). A possible candidate for the process of oxidation is protein disulphide isomerase, an ubiquitous enzyme in eukaryotes that catalyses oxidative protein folding (88).…”

Section: Wool Follicle Cyclingmentioning

confidence: 99%

Biology of the wool follicle: an excursion into a unique tissue interaction system waiting to be re‐discovered

Rogers

2006

Experimental Dermatology

127

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: Wool fibres are hairs and the term ‘wool’ is usually restricted to describe the fine curly hairs that constitute the fleece produced by sheep. In a broader sense, it can be used to describe the fleeces produced by related species such as goat or yak. Research into the biology of wool growth and the structure of the wool fibre has been driven by the demands of the wool industry to improve both the efficiency of growing wool and the quality of the product. Well beyond this very applied perspective however, the wool follicle is a unique basic research model for the life sciences in general. These unique features include, to name just a few selected examples, accessibility for studying the molecular controls involved in branching of secondary epithelial‐mesenchymal structures, the photoperiod‐dependence of regenerating tissue interaction systems, the origin of fibre curliness and follicle wave pattern formation, and the effect of alterations in nutrient supply on epithelial growth and fibre structure. In this review, investigation of growth processes in the formation of the wool fibre is broadly surveyed. The relevance and potential for practical outcomes through characterization of wool follicle genes are discussed and particular features of the wool follicle contributing to our knowledge of the biology of hair growth are highlighted. The practical potential of gene discovery in wool research is the provision of molecular markers for selective breeding and for altering wool growth and wool structure by other biological pathways such as sheep transgenesis that could lead to novel wool properties. In this background, the current review attempts to revive general interest in the fascinating biology of the wool follicle which is not only of profound economic and practical importance but offers an exquisite, highly instructive research model for addressing key questions of modern biology.

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Section: Wool Follicle Cyclingmentioning

confidence: 99%

Biology of the wool follicle: an excursion into a unique tissue interaction system waiting to be re‐discovered

Rogers

2006

Experimental Dermatology

127

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“…The content of HGT-KAPs in hair/wool fiber varies considerably within and between species, ranging from < 3% in human hair and Lincoln sheep wool, through to 4%-12% in Merino wool, 18% in mouse hair, and 30%-40% in echidna quill (Gillespie, 1990). The HGT-KAP content appears to be influenced by dietary, physiological, and genetic factors (Gillespie, 1990).…”

Section: Introductionmentioning

confidence: 97%

Search for Variation in the Ovine KAP7-1 and KAP8-1 Genes Using Polymerase Chain Reaction–Single-Stranded Conformational Polymorphism Screening

Gong

Zhou

Plowman

et al. 2012

DNA and Cell Biology

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Keratins and keratin-associated proteins (KAPs) are large heterogeneous groups of proteins that constitute about 90% of the wool fiber. The genes encoding the high glycine-tyrosine (HGT) KAPs are the first sub-group of KAP genes expressed in the wool follicle and just after expression of the keratin genes. Little is known about variation in these genes, which led us to investigate two HGT-KAP genes, KRTAP7-1 and KRTAP8-1. Polymerase chain reaction-single-stranded conformational polymorphism analysis was used to investigate these genes in 250 Romney-cross sheep. For KRTAP7-1, two unique banding patterns were detected for amplicons that spanned the entire coding region. Sequencing confirmed the presence of two sequences with only one nucleotide difference (c.173G/A) putatively resulting in p.Ser58Asn. One was identical to the published ovine KRTAP7-1 sequence. For KRTAP8-1, five unique banding patterns were detected in an amplicon that spanned the entire coding region. Sequencing revealed five different DNA sequences, all of which were highly homologous to the previously reported ovine KRTAP8-1 sequence. Among these five sequences, four single-nucleotide substitutions were identified and three of them were located in the coding region. One of these was nonsynonymous and would putatively result in p.Tyr34Asn. The variation detected in KRTAP7-1 and KRTAP8-1 may influence their expression or protein structure.

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“…In particular, mammalian hard keratins contain three disparate groups of proteins, each with many members (Gillespie 1990), whereas feathers contain only one type of protein with very few members (O'Donnell 1973). The first indication of differences in molecular structure was revealed in X-ray diffraction studies on feather keratin which indicated that the dominant secondary structure was based on the β-conformation (Marwick 1931;Astbury and Marwick 1932).…”

Section: Avian and Reptilian Keratinsmentioning

confidence: 99%

The role of β-sheets in the structure and assembly of keratins

Fraser

2009

Biophys Rev

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X-ray diffraction, infrared and electron microscope studies of avian and reptilian keratins, and of stretched wool and hair, have played a central role in the development of models for the β-conformation in proteins. Both α-and β-keratins contain sequences that are predicted to adopt a β-conformation and these are believed to play an important part in the assembly of the filaments and in determining their mechanical properties. Interactions between the small β-sheets in keratins provide a simple mechanism through which shape and chemical complementarity can mediate the assembly of molecules into highly specific structures. Interacting β-sheets in crystalline proteins are often related to one another by diad symmetry and the data available on feather keratin suggest that the filament is assembled from dimers in which the β-sheets are related by a perpendicular diad. The most detailed model currently available is for feather and reptilian keratin but the presence of related β-structural forms in mammalian keratins is also noted.

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The Proteins of Hair and Other Hard α-Keratins

Cited by 69 publications

References 61 publications

Biology of the wool follicle: an excursion into a unique tissue interaction system waiting to be re‐discovered

Biology of the wool follicle: an excursion into a unique tissue interaction system waiting to be re‐discovered

Search for Variation in the Ovine KAP7-1 and KAP8-1 Genes Using Polymerase Chain Reaction–Single-Stranded Conformational Polymorphism Screening

The role of β-sheets in the structure and assembly of keratins

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