TLDR Modern techniques have improved the understanding of keratin proteins, revealing their roles in various cells and potential in disease diagnosis.
Keratin proteins, known for their structural role in hair, wool, and skin, were challenging to study due to extraction difficulties, high sequence homology, and post-translational modifications. However, modern proteomic techniques, such as mass spectrometry, improved the analysis of these proteins. Keratins were found in various cell types, including epithelial, neuronal, and glial cells, and were involved in forming intermediate filaments. The study of keratins extended beyond hair and wool to other tissues, recognizing their role in diseases and potential for diagnostic tool development. Despite the challenges, advancements in proteomics provided valuable insights into the complex nature of keratin proteins.
122 citations
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January 2006 in “Molecular & Cellular Proteomics” Human hair contains many proteins, with some being highly abundant and modified.
226 citations
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January 2002 in “Biological and Pharmaceutical Bulletin” A new method quickly extracts and identifies proteins from hair and other keratin sources.
272 citations
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September 2001 in “Journal of Biological Chemistry” Human hair keratins were cataloged, showing their roles in hair differentiation stages.
235 citations
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July 1999 in “Journal of biological chemistry/The Journal of biological chemistry” Human hair is made up of different keratins, some strong and some weak, with specific types appearing at various stages of hair growth.
175 citations
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January 1995 in “Birkhäuser Basel eBooks” Human hair growth and structure are influenced by keratin proteins, genes, melanin, and lipids.
10 citations
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January 1989 in “Archives of Dermatological Research” The method effectively analyzes human hair proteins, especially nonfilamentous ones.
248 citations
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April 1988 in “Differentiation” Human and bovine hair follicles have distinct cytokeratins specific to hair-forming cells.
