Development of high-performance two-dimensional gel electrophoresis for human hair shaft proteome
The primary components of human hair shaft-keratin and keratin-associated proteins (KAPs), together with their cross-linked networks-are the underlying reason for its rigid structure. It is therefore requisite to overcome the obstacle of hair insolubility and establish a reliable protocol for the pr...
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| Veröffentlicht in: | PloS one 2019-03, Vol.14 (3), p.e0213947-e0213947 |
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| creator | Wong, Sing Ying Hashim, Onn Haji Hayashi, Nobuhiro |
| description | The primary components of human hair shaft-keratin and keratin-associated proteins (KAPs), together with their cross-linked networks-are the underlying reason for its rigid structure. It is therefore requisite to overcome the obstacle of hair insolubility and establish a reliable protocol for the proteome analysis of this accessible specimen. The present study employed an alkaline-based method for the efficient isolation of hair proteins and subsequently examined them using gel-based proteomics. The introduction of two proteomic protocols, namely the conventional and modified protocol, have resulted in the detection of more than 400 protein spots on the two-dimensional gel electrophoresis (2DE). When compared, the modified protocol is deemed to improve overall reproducibility, whilst offering a quick overview of the total protein distribution of hair. The development of this high-performance protocol is hoped to provide a new approach for hair analysis, which could possibly lead to the discovery of biomarkers for hair in health and diseases in the future. |
| doi_str_mv | 10.1371/journal.pone.0213947 |
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Y.</contributor><creatorcontrib>Wong, Sing Ying ; Hashim, Onn Haji ; Hayashi, Nobuhiro ; Lau, Andy T. Y.</creatorcontrib><description>The primary components of human hair shaft-keratin and keratin-associated proteins (KAPs), together with their cross-linked networks-are the underlying reason for its rigid structure. It is therefore requisite to overcome the obstacle of hair insolubility and establish a reliable protocol for the proteome analysis of this accessible specimen. The present study employed an alkaline-based method for the efficient isolation of hair proteins and subsequently examined them using gel-based proteomics. The introduction of two proteomic protocols, namely the conventional and modified protocol, have resulted in the detection of more than 400 protein spots on the two-dimensional gel electrophoresis (2DE). When compared, the modified protocol is deemed to improve overall reproducibility, whilst offering a quick overview of the total protein distribution of hair. The development of this high-performance protocol is hoped to provide a new approach for hair analysis, which could possibly lead to the discovery of biomarkers for hair in health and diseases in the future.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0213947</identifier><identifier>PMID: 30889197</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Biological markers ; Biology and Life Sciences ; Biomarkers ; Crosslinking ; EDTA ; Electrophoresis ; Electrophoresis, Gel, Two-Dimensional - methods ; Gel electrophoresis ; Hair ; Hair - chemistry ; Humans ; Keratin ; Keratins - analysis ; Keratins - isolation & purification ; Life sciences ; Medicine and Health Sciences ; Methods ; Protein expression ; Proteins ; Proteome - analysis ; Proteome - isolation & purification ; Proteomics ; Proteomics - methods ; Proteomics - statistics & numerical data ; Reproducibility ; Reproducibility of Results ; Research and Analysis Methods ; Rigid structures</subject><ispartof>PloS one, 2019-03, Vol.14 (3), p.e0213947-e0213947</ispartof><rights>COPYRIGHT 2019 Public Library of Science</rights><rights>2019 Wong et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 Wong et al 2019 Wong et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c802t-8fbd219d052bfa575ac3db49381298343191659e9147cca53cd0ff18d7abb8403</citedby><cites>FETCH-LOGICAL-c802t-8fbd219d052bfa575ac3db49381298343191659e9147cca53cd0ff18d7abb8403</cites><orcidid>0000-0002-9950-094X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6424392/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6424392/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,2103,2929,23871,27929,27930,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30889197$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Lau, Andy T. 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Y.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of high-performance two-dimensional gel electrophoresis for human hair shaft proteome</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2019-03-19</date><risdate>2019</risdate><volume>14</volume><issue>3</issue><spage>e0213947</spage><epage>e0213947</epage><pages>e0213947-e0213947</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The primary components of human hair shaft-keratin and keratin-associated proteins (KAPs), together with their cross-linked networks-are the underlying reason for its rigid structure. It is therefore requisite to overcome the obstacle of hair insolubility and establish a reliable protocol for the proteome analysis of this accessible specimen. The present study employed an alkaline-based method for the efficient isolation of hair proteins and subsequently examined them using gel-based proteomics. The introduction of two proteomic protocols, namely the conventional and modified protocol, have resulted in the detection of more than 400 protein spots on the two-dimensional gel electrophoresis (2DE). When compared, the modified protocol is deemed to improve overall reproducibility, whilst offering a quick overview of the total protein distribution of hair. The development of this high-performance protocol is hoped to provide a new approach for hair analysis, which could possibly lead to the discovery of biomarkers for hair in health and diseases in the future.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>30889197</pmid><doi>10.1371/journal.pone.0213947</doi><tpages>e0213947</tpages><orcidid>https://orcid.org/0000-0002-9950-094X</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Biological markers Biology and Life Sciences Biomarkers Crosslinking EDTA Electrophoresis Electrophoresis, Gel, Two-Dimensional - methods Gel electrophoresis Hair Hair - chemistry Humans Keratin Keratins - analysis Keratins - isolation & purification Life sciences Medicine and Health Sciences Methods Protein expression Proteins Proteome - analysis Proteome - isolation & purification Proteomics Proteomics - methods Proteomics - statistics & numerical data Reproducibility Reproducibility of Results Research and Analysis Methods Rigid structures |
| title | Development of high-performance two-dimensional gel electrophoresis for human hair shaft proteome |
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