The susceptibility of disulfide bonds to modification in keratin fibers undergoing tensile stress

Harland, Duane P.; Popescu, C.; Richena, Marina; Deb‐Choudhury, Santanu; Wichlatz, Claudia; Lee, Erin; Plowman, Jeffrey E.

doi:10.1016/j.bpj.2022.04.029

Cited by 13 publications

(11 citation statements)

References 32 publications

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“…In this context, the central rod region in keratin fibres may be associated with keratin-keratin interactions between anti-parallel heterodimers (Harland et al, 2022). The sensitivity of disulfide bonds in keratin fibres to modification may explain the varying degrees of contribution to fibre mechanics.…”

Section: Discussionmentioning

confidence: 99%

“…It has been stated that when hydrogen bonds between proteins are broken under wet conditions, disulfide labeling can occur in the head areas of type II keratins and in the tail areas of type I keratins that affect keratin‐keratin interactions. In this context, the central rod region in keratin fibres may be associated with keratin–keratin interactions between anti‐parallel heterodimers (Harland et al, 2022). The sensitivity of disulfide bonds in keratin fibres to modification may explain the varying degrees of contribution to fibre mechanics.…”

Section: Discussionmentioning

confidence: 99%

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Intermediate filament proteins are reliable immunohistological biomarkers to help diagnose multiple tissue‐specific diseases

Doğanyiğit

Eroğlu

Okan

2023

Anat Histol Embryol

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Cytoskeletal networks are proteins that effectively maintain cell integrity and provide mechanical support to cells by actively transmitting mechanical signals. Intermediate filaments, which are from the cytoskeleton family and are 10 nanometres in diameter, are unlike actin and microtubules, which are highly dynamic cytoskeletal elements. Intermediate filaments are flexible at low strain, harden at high strain and resist breaking. For this reason, these filaments fulfil structural functions by providing mechanical support to the cells through their different strain‐hardening properties. Intermediate filaments are suitable in that cells both cope with mechanical forces and modulate signal transmission. These filaments are composed of fibrous proteins that exhibit a central α‐helical rod domain with a conserved substructure. Intermediate filament proteins are divided into six groups. Type I and type II include acidic and basic keratins, type III, vimentin, desmin, peripheralin and glial fibrillary acidic protein (GFAP), respectively. Type IV intermediate filament group includes neurofilament proteins and a fourth neurofilament subunit, α‐internexin proteins. Type V consists of lamins located in the nucleus, and the type VI group consists of lens‐specific intermediate filaments, CP49/phakinin and filen. Intermediate filament proteins show specific immunoreactivity in differentiating cells and mature cells of various types. Various carcinomas such as colorectal, urothelial and ovarian, diseases such as chronic pancreatitis, cirrhosis, hepatitis and cataract have been associated with intermediate filaments. Accordingly, this section reviews available immunohistochemical antibodies to intermediate filament proteins. Identification of intermediate filament proteins by methodological methods may contribute to the understanding of complex diseases.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Intermediate filament proteins are reliable immunohistological biomarkers to help diagnose multiple tissue‐specific diseases

Doğanyiğit

Eroğlu

Okan

2023

Anat Histol Embryol

View full text Add to dashboard Cite

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“…In this respect, if expressed, this amino change would be in the head region of K84, a region that is important in the formation of the keratin dimers and tetramers that arrange into protofilaments. In the report of Harland et al [20], fibers from Romney sheep were subjected to stretching or to their breaking point under wet or dry conditions to detect disulfide bonds breakage. Many of the identified cysteine residues were located close to the terminal ends of the keratins (head or tail domains), where they likely affect keratin-associated protein interactions and keratin interactions.…”

Section: Variation In Krt84mentioning

confidence: 99%

Spatiotemporal Expression and Haplotypes Identification of KRT84 Gene and Their Association with Wool Traits in Gansu Alpine Fine-Wool Sheep

Yu,

Li,

Zhou

et al. 2024

Genes

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Keratin (K) is a major protein component of hair and is involved in hair growth and development. In this study, we analysed the expression, localization, and polymorphism of the K84 gene (KRT84) in Gansu Alpine Fine-wool sheep using immunofluorescence, RT-qPCR, and PARMS (Penta-primer amplification refractory mutation system). Haplotypes of KRT84 were also constructed and their relationship with wool traits analysed. It was revealed that KRT84 was highly expressed in hair follicles, including the inner root sheath, outer root sheath, and hair medulla and at all six lamb ages investigated from 1 to 270 days of age. Three SNPs were detected in KRT84 exon 1, and they formed three haplotypes (named H1, H2, and H3) and six genotypes. Analyses revealed an association between haplotype combinations (diplotypes) and the mean fibre curvature, mean staple length, mean staple strength, mean fibre diameter, the coefficient of variation of fibre diameter, and comfort factor for these sheep. These results suggest that KRT84 is of importance in determining several key traits in Gansu Alpine Fine-wool sheep and that the gene could possibly be used as a genetic marker for wool trait selection in these sheep.

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“…These clusters critically underpin the mitochondrial respiratory chain in hair follicle cells, subsequently promoting ATP synthesis (Lill 2009 ), which furnishes the requisite energy for hair follicle growth. Within hair structures, the disulphide bonds, a salient component formed by cysteine, are instrumental in sustaining hair stability (Harland et al 2022 ). As their count surges, the rigidity of hair fibres intensifies concurrently (Gniadecka et al 1998 ).…”

Section: The Role Of Cysteine Metabolism In Aa: a Potential Connectionmentioning

confidence: 99%

Dissecting hair breakage in alopecia areata: the central role of dysregulated cysteine homeostasis

Xu,

Xie,

Wei

et al. 2024

Amino Acids

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In the initial stages of Alopecia Areata (AA), the predominance of hair breakage or exclamation mark hairs serves as vital indicators of disease activity. These signs are non-invasive and are commonly employed in dermatoscopic examinations. Despite their clinical salience, the underlying etiology precipitating this hair breakage remains largely uncharted territory. Our exhaustive review of the existing literature points to a pivotal role for cysteine—a key amino acid central to hair growth—in these mechanisms. This review will probe and deliberate upon the implications of aberrant cysteine metabolism in the pathogenesis of AA. It will examine the potential intersections of cysteine metabolism with autophagy, ferroptosis, immunity, and psychiatric manifestations associated with AA. Such exploration could illuminate new facets of the disease's pathophysiology, potentially paving the way for innovative therapeutic strategies.

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The susceptibility of disulfide bonds to modification in keratin fibers undergoing tensile stress

Cited by 13 publications

References 32 publications

Intermediate filament proteins are reliable immunohistological biomarkers to help diagnose multiple tissue‐specific diseases

Intermediate filament proteins are reliable immunohistological biomarkers to help diagnose multiple tissue‐specific diseases

Spatiotemporal Expression and Haplotypes Identification of KRT84 Gene and Their Association with Wool Traits in Gansu Alpine Fine-Wool Sheep

Dissecting hair breakage in alopecia areata: the central role of dysregulated cysteine homeostasis

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