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Preliminary quantitative proteomic characterization of glaucomatous rat retinal ganglion cells.


ABSTRACT: Quantitative proteomic analysis was pursued of retinal ganglion cells (RGCs) from rats with unilateral experimental glaucoma. RGCs were isolated from 22 animals by immunopanning after 8 weeks of sustained elevated intraocular pressure. Proteins were quantified by LC MS/MS iTRAQ technology. Of the 268 proteins quantified, approximately 8% appeared elevated and approximately 13% decreased in glaucomatous RGCs. Voltage-dependent anion channel protein 2, aldose reductase, and ubiquitin were among the significantly elevated proteins while prothymosin was among the significantly decreased. The results demonstrate the feasibility of identifying global proteomic differences in protein expression between purified glaucomatous and control in vivo RGCs.

SUBMITTER: Crabb JW 

PROVIDER: S-EPMC2881315 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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Preliminary quantitative proteomic characterization of glaucomatous rat retinal ganglion cells.

Crabb John W JW   Yuan Xianglin X   Dvoriantchikova Galina G   Ivanov Dmitry D   Crabb John S JS   Shestopalov Valery I VI  

Experimental eye research 20100420 1


Quantitative proteomic analysis was pursued of retinal ganglion cells (RGCs) from rats with unilateral experimental glaucoma. RGCs were isolated from 22 animals by immunopanning after 8 weeks of sustained elevated intraocular pressure. Proteins were quantified by LC MS/MS iTRAQ technology. Of the 268 proteins quantified, approximately 8% appeared elevated and approximately 13% decreased in glaucomatous RGCs. Voltage-dependent anion channel protein 2, aldose reductase, and ubiquitin were among th  ...[more]

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