Journal of Biochemistry Advance Access published online on December 5, 2006
Journal of Biochemistry, doi:10.1093/jb/mvm006
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© 2006 The Japanese Biochemical Society
Rat Brain Synaptic Vesicles are Devoid of Mg2+-ATPase Activity and Contain ß-Amyloid Precursor Protein
Department of Biochemistry I, School of Medicine, Nagoya City University, Kawasumi 1, Mizuho-ku, Nagoya 467-8601, Japan
Dr. Tsudzuki, Toshihiro, Kawasumi 1, Mizuho-cho, Mizuho-ku, Nagoya, Aichi, 467-8601, Tel: +81-52-853-8140, Fax: +81-52-841-3480, E-MAIL: tsudzuki{at}sunprom.med.nagoya-cu.ac.jp
| Abstract |
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Rat brain synaptic vesicles 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 synaptic vesicles 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 synaptic vesicles. 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 synaptic vesicles contained ß-amyloid precursor protein of
100 kDa. Based on these observations, synaptic vesicles 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.
Key Words: H+-ATPase, ß-amyloid precursor protein, synaptic vesicles, dopa decarboxylase, tyrosine hydroxylase