Rat brain synaptic vesicles are devoid of Mg2+-ATPase activity and contain β-amyloid precursor protein

Rat brain synaptic vesicles (SVs) isolated by gel filtration on Sephacryl S-500 had little Mg2+(H+)-ATPase activity, though it was identified by Western blots with antibodies against the H+-ATPase A-subunit and other vesicle proteins. In contrast, tyrosine hydroxylase and dopa decarboxylase activities in the SVs were substantial, suggesting that the absence of Mg2+(H+)-ATPase activity was not due to inactivation during isolation but rather to the nature of the SVs. The vesicle component reactive to H'-ATPase antibody was also identified in the synaptosomal cytosol, so the antibody for the A-subunit seemed unnecessary to detect H'-ATPase. The SVs contained P-amyloid precursor protein of similar to 100kDa. Based on these observations, SVs without Mg2+(H+)-ATPase seemed to play a role(s) in the delivery of cytoplasmic and plasma membrane proteins to nerve terminals as well as in neurotransmission.