PBT434 inhibits alpha- synuclein in the brain., page-23

Kpax, note in the study above as A-Syn aggregation was reduced, levels of ferroportin, an iron exporter that is strong enough to degrade ferritin and release iron into the plasma, increased. Although PBT434 is not strong enough to remove iron from ferritin stores, ferroportin which is increased during PBT434 treatment is capable of removing stored iron. Looks like a natural increase of Fpn going on once the ambient environment is cleaned up of labile iron, but I have no idea what is going on there.
[There is substantial genetic and physiological data that show that Fpn is the iron exporter responsible for the entry of iron into plasma (Ganz and Nemeth, 2006). Expression of Fpn results in the loss of cellular iron including iron stored in ferritin (Nemeth et al, 2004). We show here that Fpn-mediated ferritin degradation occurs in the cytosol and requires the activity of the proteasome. Release of iron from ferritin occurs before ferritin degradation and does not require ubiquitination. ]
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1636618/