Anti-SNPH (center domain) polyclonal antibody

Chronic mitochondrial stress is a central problem associated with neurodegenerative diseases. Early removal of defective mitochondria from axons constitutes a critical step of mitochondrial quality control. Here we investigate axonal mitochondrial response to mild stress in wild-type neurons and chronic mitochondrial defects in Amytrophic Lateral Sclerosis (ALS)- and Alzheimer's disease (AD)-linked neurons. We show that stressed mitochondria are removed from axons triggered by the bulk release of mitochondrial anchoring protein syntaphilin via a new class of mitochondria-derived cargos independent of Parkin, Drp1, and autophagy. Immuno-electron microscopy and super-resolution imaging show the budding of syntaphilin cargos, which then share a ride on late endosomes for transport toward the soma. Releasing syntaphilin is also activated in the early pathological stages of ALS- and AD-linked mutant neurons. Our study provides new mechanistic insights into the maintenance of axonal mitochondrial quality through SNPH-mediated coordination of mitochondrial stress and motility before activation of Parkin-mediated mitophagy.

The synthesis of ReH7(AsPh(3))(2) is reported. Surprisingly, this complex appears to be a classical heptahydride and is remarkably resistant to substitution by nitrogen and phosphorus donor ligands. The reactivity of this polyhydride towards silanes and stannanes was also studied. The new complexes, ReH6(SiPh(3))(AsPh(3))(2) and ReH6(SnPh(3))(AsPh(3))(2), are formed with Ph(3)EH (E = Si,Sn) but ReH7(AsPh(3))(2) does not react with chelating silanes. These products appear to be more stable than their phosphine-supported analogues.