Figure 8
Mass spectrometric analysis revealed neurodegenerative and neuroprotective pathways. Proteins were isolated from retinae and digested to peptides, which were ionized for mass spectrometric analysis. Mass chromatograms provide information for protein identification. Regulations of more than two-fold were regarded as distinct (dotted line) Results from mass spectrometry revealed the proteome of the retina isolated from IOP elevated eyes. GO annotation was performed for (a) cellular component, (b) molecular function and (c) biological processes. (d) Retinal protein alterations of retina of IOP elevated eyes were compared with fellow eyes (black bars). The retinal proteome of α-synuclein Ab injected IOP elevated eyes was compared with the retinal proteome of IOP elevated eyes to reveal the neuroprotective mechanisms (white bars). Cofilin 1 (CFL1) is downregulated in the retinal proteome of IOP elevated eyes (−2.5x), but upregulated in the retinal proteome of eyes after α-synuclein Ab injection (3.5x). Superoxide dismutase 1 (SOD1) is upregulated in the retinal proteome of IOP elevated eyes (3.5x) and distinctly downregulated in the retinal proteome of eyes after α-synuclein Ab injection (−27.7x). (e) An overview of possible reactions after formation of α-synuclein Ab/protein complex based on STRING protein interaction analysis. Cofilin 1 (green), a major protein involved in the actin cytoskeleton organization, is upregulated while superoxide dismutase 1 (red), a major antioxidant enzyme, is downregulated in the retinal proteome of α -synuclein Ab injected IOP elevated eyes. It is possible that the formation of α -synuclein Ab/protein complex (white) influences downstream signaling pathways, having an effect on the expression level of cofilin 1 and superoxide dismutase 1. It was shown previously that phosphorylation of cofilin 1 via PAK2 and Rac1 is influenced by the presence of α-synuclein protein.
