Studies on the proteome of human hair - identification of histones and deamidated keratins
Human hair is laminar-fibrous tissue and an evolutionarily old keratinization product of follicle trichocytes. Studies on the hair proteome can give new insights into hair function and lead to the development of novel biomarkers for hair in health and disease. Human hair proteins were extracted by d...
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sg-ntu-dr.10356-875512020-11-01T05:21:17Z Studies on the proteome of human hair - identification of histones and deamidated keratins Kerk, Swat Kim Lee, Amelia Yilin Lai, Hui Ying Ng, Kee Woei Sze, Siu Kwan Schmidtchen, Artur Adav, Sunil Shankar Subbaiaih, Roopa Shree Interdisciplinary Graduate School (IGS) Lee Kong Chian School of Medicine (LKCMedicine) School of Materials Science & Engineering School of Biological Sciences Nanyang Environment and Water Research Institute Hair Proteome Keratin-associated Proteins (KAPs) Human hair is laminar-fibrous tissue and an evolutionarily old keratinization product of follicle trichocytes. Studies on the hair proteome can give new insights into hair function and lead to the development of novel biomarkers for hair in health and disease. Human hair proteins were extracted by detergent and detergent-free techniques. We adopted a shotgun proteomics approach, which demonstrated a large extractability and variety of hair proteins after detergent extraction. We found an enrichment of keratin, keratin-associated proteins (KAPs), and intermediate filament proteins, which were part of protein networks associated with response to stress, innate immunity, epidermis development, and the hair cycle. Our analysis also revealed a significant deamidation of keratin type I and II, and KAPs. The hair shafts were found to contain several types of histones, which are well known to exert antimicrobial activity. Analysis of the hair proteome, particularly its composition, protein abundances, deamidated hair proteins, and modification sites, may offer a novel approach to explore potential biomarkers of hair health quality, hair diseases, and aging. MOE (Min. of Education, S’pore) Published version 2018-07-31T06:26:42Z 2019-12-06T16:44:22Z 2018-07-31T06:26:42Z 2019-12-06T16:44:22Z 2018 Journal Article Adav, S. S., Subbaiaih, R. S., Kerk, S. K., Lee, A. Y., Lai, H. Y., Ng, K. W., et al. (2018). Studies on the proteome of human hair - identification of histones and deamidated keratins. Scientific Reports, 8(1), 1599-. 2045-2322 https://hdl.handle.net/10356/87551 http://hdl.handle.net/10220/45415 10.1038/s41598-018-20041-9 en Scientific Reports © 2018 The Author(s) (Nature Publishing Group). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. 11 p. application/pdf |
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Hair Proteome Keratin-associated Proteins (KAPs) |
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Hair Proteome Keratin-associated Proteins (KAPs) Kerk, Swat Kim Lee, Amelia Yilin Lai, Hui Ying Ng, Kee Woei Sze, Siu Kwan Schmidtchen, Artur Adav, Sunil Shankar Subbaiaih, Roopa Shree Studies on the proteome of human hair - identification of histones and deamidated keratins |
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Human hair is laminar-fibrous tissue and an evolutionarily old keratinization product of follicle trichocytes. Studies on the hair proteome can give new insights into hair function and lead to the development of novel biomarkers for hair in health and disease. Human hair proteins were extracted by detergent and detergent-free techniques. We adopted a shotgun proteomics approach, which demonstrated a large extractability and variety of hair proteins after detergent extraction. We found an enrichment of keratin, keratin-associated proteins (KAPs), and intermediate filament proteins, which were part of protein networks associated with response to stress, innate immunity, epidermis development, and the hair cycle. Our analysis also revealed a significant deamidation of keratin type I and II, and KAPs. The hair shafts were found to contain several types of histones, which are well known to exert antimicrobial activity. Analysis of the hair proteome, particularly its composition, protein abundances, deamidated hair proteins, and modification sites, may offer a novel approach to explore potential biomarkers of hair health quality, hair diseases, and aging. |
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Interdisciplinary Graduate School (IGS) |
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Interdisciplinary Graduate School (IGS) Kerk, Swat Kim Lee, Amelia Yilin Lai, Hui Ying Ng, Kee Woei Sze, Siu Kwan Schmidtchen, Artur Adav, Sunil Shankar Subbaiaih, Roopa Shree |
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Article |
author |
Kerk, Swat Kim Lee, Amelia Yilin Lai, Hui Ying Ng, Kee Woei Sze, Siu Kwan Schmidtchen, Artur Adav, Sunil Shankar Subbaiaih, Roopa Shree |
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Kerk, Swat Kim |
title |
Studies on the proteome of human hair - identification of histones and deamidated keratins |
title_short |
Studies on the proteome of human hair - identification of histones and deamidated keratins |
title_full |
Studies on the proteome of human hair - identification of histones and deamidated keratins |
title_fullStr |
Studies on the proteome of human hair - identification of histones and deamidated keratins |
title_full_unstemmed |
Studies on the proteome of human hair - identification of histones and deamidated keratins |
title_sort |
studies on the proteome of human hair - identification of histones and deamidated keratins |
publishDate |
2018 |
url |
https://hdl.handle.net/10356/87551 http://hdl.handle.net/10220/45415 |
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1683493798964887552 |