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


ABSTRACT: There is insufficient knowledge about the chondrocyte membranome and its molecular composition.To develop a Triton X-114 based separation technique using nanoLC-MS/MS combined with shotgun proteomics to identify chondrocyte membrane proteins.Articular chondrocytes from equine metacarpophalangeal joints were separated into hydrophobic and hydrophilic fractions; trypsin-digested proteins were analysed by nanoLC-MS/MS.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.Defining the chondrocyte membranome is likely to reveal new biomarker targets for conventional and biological drug discovery.

SUBMITTER: Matta C 

PROVIDER: S-EPMC4819840 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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

Matta Csaba C   Zhang Xiaofei X   Liddell Susan S   Smith Julia R JR   Mobasheri Ali A  

Biomarkers : biochemical indicators of exposure, response, and susceptibility to chemicals 20150101 8


<h4>Context</h4>There is insufficient knowledge about the chondrocyte membranome and its molecular composition.<h4>Objective</h4>To develop a Triton X-114 based separation technique using nanoLC-MS/MS combined with shotgun proteomics to identify chondrocyte membrane proteins.<h4>Materials and methods</h4>Articular chondrocytes from equine metacarpophalangeal joints were separated into hydrophobic and hydrophilic fractions; trypsin-digested proteins were analysed by nanoLC-MS/MS.<h4>Results</h4>A  ...[more]

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