Despite in primary open angle glaucoma, uveitic glaucoma

Despite the advances made in the understanding of glaucoma, molecular markers & mechanisms that can be used to target treatment are still unclear. The large scale analysis offered by proteomic studies could enable researchers to discover simultaneously cellular proteins involved in glaucomatous neurodegeneration. Analysis of protein expression, protein network interactions & posttranslational modifications will pave the way for improved targeted therapy. ( , , ) Gel-based and gel-free techniques of protein analysis using mass spectrometry and isotope labeling-based or label-free techniques for relative quantification for protein expression between glaucomatous and control samples have been increasingly used to study molecular mechanisms and identify potential biomarker candidates of glaucoma. Protein content has been previously described in primary open angle glaucoma, uveitic glaucoma and myopia ( , , , , )  Global proteomic approaches have been used to study AH protein content ( ,  , )Bouhenni et al ( ) attempted to identify proteins that may be altered in PCG. Tryptic digests of the complex mixtures of proteins in AH were analyzed using Liquid Chromatography/Mass Spectrometry (LC-MS/MS). The proteomes of AH in 7 PCG and 4 controls undergoing cataract surgery were compared. Apolipoprotein A-IV, Albumin and Antithrombin 3 were detected at significantly higher levels in PCG AH compared to control, whereas Transthyretin, Prostaglandin-H2 D-isomerase, Opticin and Interphotoreceptor Retinoid Binding Protein were detected at significantly lower levels. They explained that these proteins played a role in retinoic acid binding/transport and have been implicated in the pathogenesis of other neurodegenerative diseases such as Alzheimer’s. They concluded that PCG development could be influenced by the availability of retinoic acid in the anterior chamber.The aqueous humor of primary open-angle glaucoma patients was studied using SELDI-TOF-MS (Surface-enhanced laser desorption ionization. The study revealed characteristic differences in protein/peptide profiles from control patients. 250 protein peaks were consistently clustered in both groups. Eight biomarkers discriminated glaucoma from non-glaucoma controls with a sensitivity of 90% and a specificity of 87%. (23). Application of mass spectrometry for analyses of anterior eye proteome was reviewed recently. MALDI TOF MS was employed in the analysis of the human lens. MALDI TOF MS concentrated on the major protein differences for identification in order to determine the variances between proteins in age-related cataracts and normal lens nuclei. This was used to grade cataracts and total solubilized proteins . Corneal proteins were also studied using MALDI TOF MS techniques. ( , )  MALDI imaging on the anterior capsule which showed presence of LOXL-1 protein was more abundant in the iris region and apolipoprotein E in the pseudoexfoliation deposits in anterior capsule in the pupillary area. ( ) Our literature search did not reveal any research on hAH proteomic research using MALDI mass spectrometry.References: