## 3 Discussion
Elevated IOP seems to decrease the MAP1A amount and, thereby, the number of axonal cross-bridges, leading to microtubule instability and abnormal organelle transportation in axon plasma [72]. TPPPs show extensive MT bundling and polymerization abilities critical for axon formation, extension, and guidance at nerve terminals, as demonstrated in retinae of the model organismsdrosophila, zebrafish, mouse, and human [73, 74, 75, 76, 77, 78, 79]. A study investigating AD showed TPPP down-regulation [80]. Our study showed that the MT-associated proteins, MAP1A and TPPP, were significantly up-regulated, suggesting increased MT stability. An actin-associated protein, coactosin-like protein 1 (COTL1), was also significantly less abundant in the DNM1L OS group (Figure 7). COTL1, as an actin depolymerization factor (ADF) and member of the cofilin family, plays a crucial role in binding to F-actin and thus preventing polymerization [81]. COTL1 overexpression showed disturbed neuronal morphology and exhibited AD-like neuropathology [82, 83]. In a study with POAG patients, COTL1 was up-regulated in aqueous humor [84]. Therefore, the low abundance of COTL1 suggested continued polymerization and stabilization of the actin cytoskeleton, which, together with MT cytoskeleton stabilization, may be part of a neuroprotective mechanism, as shown in previous studies [26, 85]. In this context, increased DNM1L abundance appeared to be a crucial factor, as DNM1L is required for proper mitochondrial distribution and mobilization of synaptic vesicles [86]. Increased vesicle trafficking and altered mitochondrial distribution could occur anterograde towards energy-demanding regions [87]. Decreased cytoplasmic dynein 1 heavy chain 1 (DYNC1H1, Figure 7) abundance in the DNM1L OS group indicated reduced retrograde cargo transportation towards the soma in the DNM1L OS group [37, 88, 89, 90]. Transportation of mitochondria or vesicles along microtubules in the direction of the pre-synapse occurs via kinesin heavy chain (KHC) proteins and milton [91]. DNM1L can bind kinesin light chain (KLC) proteins, which are KHC blocking proteins so that the interaction of KHC with cargo can occur [92]. The increased DNM1L expression in the antibody-treated group might promote cargo transportation towards synapses, e.g., mitochondria or synaptic vesicles. This hypothesis could be supported by the significantly altered proteins associated with vesicle trafficking, including SNAP91, NSF, NEGR1, SYT1, and SV2A. SNAP91, NSF, SYT1, and SV2A were significantly more abundant in the DNM1L OS group compared with IgG OS. These proteins are involved in the distribution and clustering of synaptic vesicle cargo [93, 94, 95]. In this context, SNAP91 maintains the distribution of proteins in the synapse and vesicle at nerve termini and regulates exocytosis [96, 97]. The manipulation of SNAP91, such as mutations or loss of function, is associated with abnormal vesicles or perturbed neurotransmitter exocytosis and is also involved in PD [98, 99, 100]. The NSF protein provides the necessary energy for vesicle dissociation as an AAA ATPase. However, it has also been shown that NSF and neuronal growth factor 1 (NEGR1) may also regulate vesicle fusion and recycling [101, 102]. Overexpression of NEGR1 resulted in reduced synapse formation and reduction in SNARE proteins, which play an important role in vesicle formation [102]. NSF was down-regulated in a study with PD patients, indicating reduced vesicle trafficking, the main feature of the disease [103, 104]. Neuroprotective mechanisms found in cell culture and experimental mouse models for PD were associated with the up-regulation of Snap91 and NSF [105]. NEGR1 down-regulation in the DNM1L OS group suggested improved synapse formation and increased abundance of SNARE proteins such as SNAP91, which might be underlined by increased NSF and AAA ATPase abundance providing the required energy. Down-regulation of ATP6V1A, which also plays a critical role in vesicular transport and oxidative phosphorylation, has been implicated in AD [106].