Fig. 1
From: Insights into the pathogenesis of multiple system atrophy: focus on glial cytoplasmic inclusions
![Fig. 1](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2Fs40035-020-0185-5/MediaObjects/40035_2020_185_Fig1_HTML.png)
Hypothetical overview of GCI pathogenesis and post-mortem analysis of TPPP/p25α translocation. a: Hypothetical overview of a normal OLG (left) and a pathological OLG generating GCI (right). Left: Intracellular homeostasis is maintained by normal expression levels of myelin-associated proteins and their colocalization with TPPP/p25α as well as autophagic degradation of endogenous α-syn and balanced iron metabolism. Right: Aggregation formation is enhanced by decreased expression of myelin-associated proteins, cytosolic translocation of TPPP/p25α, impaired autophagy-lysosomal degradation, and oxidation of ferrous to ferric ions. Secretion of pathological α-syn in response to insufficient degradation leads to microglial and astrocytic activation. OLG dysfunction also causes compromised neuronal support such as reduced production of neurotrophic factors. b: Translocation of TPPP/p25α from myelin to cell bodies in the frontal cortex white matter of a control patient (left) and an MSA patient (right). The scale bar represents 50 μm. c: Localization of TPPP/p25α (red) and its interaction with MBP (green) in the frontal cortex white matter of a control patient (left) and an MSA patient (right). Blue; DAPI. The scale bar represents 10 μm