Glaucoma related proteomic changes have been documented in cell and animal models. However, proteomic studies investigating on human retina samples are still rare. In the present work, retina samples of glaucoma and non-glaucoma control donors have been examined by a state-of-the-art mass spectrometry (MS) workflow to uncover glaucoma related proteomic changes. More than 600 proteins could be identified with high confidence (FDR < 1%) in human retina samples. Distinct proteomic changes have been observed in 10% of proteins encircling mitochondrial and nucleus species. Numerous proteins showed a significant glaucoma related level change (p < 0.05) or distinct tendency of alteration (p < 0.1). Candidates were documented to be involved in cellular development, stress and cell death. . In 2010, worldwide 60.5 million people suffered from glaucoma and over 70 million people are expected to develop glaucoma by 2020 making glaucoma to one of the leading causes of blindness affecting people of all ages, however with increasing prevalence with age 3 . Inflammatory 4 and autoimmune processes 5,6 implementing oxidative stress 7 and mitochondrial dysfunction 8,9 have been documented for glaucoma so far and underlying molecular mechanisms are shifting in focus of research. Accordingly, numerous studies have demonstrated proteomic changes referring to experimental in-vivo and in-vitro models, regarding rodents 10-12 and primates 13 . Glaucoma related proteomic alterations have also been reported for human sample material, e.g. aqueous humor [14][15][16][17][18][19] , trabecular meshwork 20,21 and tears 22 proposing key proteins and biomarker candidates. Focusing on human glaucomatous retina samples, Tezel et al. documented hemoglobin upregulation using immunohistochemistry 23 , whereas the research groups of Yang and Luo revealed proteomic changes linked to TNF-α /TNFR1 24 and Toll-like receptors (TLRs) 25 using mass spectrometry. However, proteomic investigations on human retinal sample species are rare due to limitation of donors and human sample material. Therefore, the purpose of the present study was to analyze human retinal samples of glaucoma (N = 5) and non-glaucoma subjects (N = 5) by use of a state-of-the-art "bottom-up" high performance liquid chromatography electro spray ionization mass spectrometry (BU LC ESI MS) workflow. Retinal sample exploration should provide an in-depth view to the human retina proteome, reveal glaucomatous proteomic alterations and should contribute to a better understanding of the molecular pathomechanism of glaucoma. Moreover, new molecular candidates linked to glaucomatous neurodegeneration should be proposed giving direction for future glaucoma research projects.