Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers

Context: There is insufficient knowledge about the chondrocyte membranome and its molecular composition. Objective: To develop a Triton X-114 based separation technique using nanoLC-MS/MS combined with shotgun proteomics to identify chondrocyte membrane proteins. Materials and methods: Articular cho...

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Autores principales: Matta, Csaba, Zhang, Xiaofei, Liddell, Susan, Smith, Julia R., Mobasheri, Ali
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4819840/
https://www.ncbi.nlm.nih.gov/pubmed/26864288
http://dx.doi.org/10.3109/1354750X.2015.1130191
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author Matta, Csaba
Zhang, Xiaofei
Liddell, Susan
Smith, Julia R.
Mobasheri, Ali
author_facet Matta, Csaba
Zhang, Xiaofei
Liddell, Susan
Smith, Julia R.
Mobasheri, Ali
author_sort Matta, Csaba
collection PubMed
description Context: There is insufficient knowledge about the chondrocyte membranome and its molecular composition. Objective: To develop a Triton X-114 based separation technique using nanoLC-MS/MS combined with shotgun proteomics to identify chondrocyte membrane proteins. Materials and methods: Articular chondrocytes from equine metacarpophalangeal joints were separated into hydrophobic and hydrophilic fractions; trypsin-digested proteins were analysed by nanoLC-MS/MS. Results: A total of 315 proteins were identified. The phase extraction method yielded a high proportion of membrane proteins (56%) including CD276, S100-A6 and three VDAC isoforms. Discussion: Defining the chondrocyte membranome is likely to reveal new biomarker targets for conventional and biological drug discovery.
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spelling pubmed-48198402016-04-22 Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers Matta, Csaba Zhang, Xiaofei Liddell, Susan Smith, Julia R. Mobasheri, Ali Biomarkers Research Article Context: There is insufficient knowledge about the chondrocyte membranome and its molecular composition. Objective: To develop a Triton X-114 based separation technique using nanoLC-MS/MS combined with shotgun proteomics to identify chondrocyte membrane proteins. Materials and methods: Articular chondrocytes from equine metacarpophalangeal joints were separated into hydrophobic and hydrophilic fractions; trypsin-digested proteins were analysed by nanoLC-MS/MS. Results: A total of 315 proteins were identified. The phase extraction method yielded a high proportion of membrane proteins (56%) including CD276, S100-A6 and three VDAC isoforms. Discussion: Defining the chondrocyte membranome is likely to reveal new biomarker targets for conventional and biological drug discovery. Taylor & Francis 2015-11-17 2015-12-22 /pmc/articles/PMC4819840/ /pubmed/26864288 http://dx.doi.org/10.3109/1354750X.2015.1130191 Text en © 2016 The Author(s). Published by Taylor & Francis. http://creativecommons.org/Licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/Licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.
spellingShingle Research Article
Matta, Csaba
Zhang, Xiaofei
Liddell, Susan
Smith, Julia R.
Mobasheri, Ali
Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
title Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
title_full Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
title_fullStr Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
title_full_unstemmed Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
title_short Label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
title_sort label-free proteomic analysis of the hydrophobic membrane protein complement in articular chondrocytes: a technique for identification of membrane biomarkers
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4819840/
https://www.ncbi.nlm.nih.gov/pubmed/26864288
http://dx.doi.org/10.3109/1354750X.2015.1130191
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