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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Detalles Bibliográficos
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
Descripción
Sumario: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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