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Journal of Biochemistry Advance Access originally published online on December 5, 2006
Journal of Biochemistry 2007 141(1):93-99; 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

Toshihiro Tsudzuki*

Department of Biochemistry I, School of Medicine, Nagoya City University, Kawasumi 1, Mizuho-ku, Nagoya 467-8601, Japan

*To whom correspondence should be addressed. Tel: +81-52-853-8140, Fax: +81-52-841-3480, E-mail: tsudzuki{at}sunprom.med.nagoya-cu.ac.jp

Received September 20, 2006; Accepted November 12, 2006


  Abstract

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 ß-amyloid precursor protein of ~100 kDa. 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.

Key Words: ß-amyloid precursor protein, dopa decarboxylase, H+-ATPase, synaptic vesicles, tyrosine hydroxylase


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