TLDR Different keratin types have unique amino acid patterns that are evolutionarily conserved.
The study analyzed keratin sequences from various species, focusing on epidermal, simple-type epithelial, and hair keratins. It found that keratin domains have distinct amino acid compositions: hair keratins are rich in cysteines and prolines, epidermal keratins are abundant in glycine and phenylalanine but low in alanine, and simple-type epithelial keratins are enriched in acidic and basic residues. These differences are evolutionarily conserved and reflect the unique structural and functional roles of each keratin type. Additionally, cysteines and histidines, though rare, are frequently involved in de novo mutations in keratins, highlighting their significance in keratin function and mutation hotspots.
87 citations,
July 2009 in “The journal of investigative dermatology/Journal of investigative dermatology” Human beard hair medulla contains a unique and complex mix of keratins not found in other human tissues.
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July 2009 in “The Journal of clinical investigation/The journal of clinical investigation” Epidermolysis bullosa simplex causes easily blistered skin due to faulty skin cell proteins, leading to new treatment ideas.
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Human hair keratins can self-assemble and support cell growth, useful for biomedical applications.
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April 2009 in “Journal of anatomy” Hard skin features like scales, feathers, and hair evolved through specific protein changes in different animal groups.
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November 2020 in “The FASEB journal” Intermediate filaments are crucial for cell differentiation and stem cell function.