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Actomyosin-like ATPase extracted from plain synaptic vesicle fractions
1Departments of Physiology and Biochemistry, Nagoya City University Medical School, Mizuho-ku, Nagoya 467, Japan.
Neurochemistry International
|May 22, 2010
Summary
Brain synaptic vesicles contain a Ca(2+)-sensitive Mg(2+)-dependent ATPase, likely composed of actin and myosin-like proteins (neurostenin). This neurostenin complex appears localized specifically within plain synaptic vesicles.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- The Ca(2+)-sensitive Mg(2+)-dependent ATPase (EC 3.6.1.3) plays a crucial role in cellular functions.
- Identifying the specific protein components and localization of this ATPase is essential for understanding synaptic vesicle dynamics.
Purpose of the Study:
- To characterize the Ca(2+)-sensitive Mg(2+)-dependent ATPase from brain synaptic vesicles.
- To determine the protein composition and subcellular localization of this ATPase.
Main Methods:
- Extraction of ATPase from purified plain synaptic vesicle fractions.
- Analysis of protein composition using SDS polyacrylamide gel electrophoresis.
- Comparison with ATPase extracted from microsomes and coated vesicles.
Main Results:
- The ATPase from plain synaptic vesicles exhibited a protein pattern similar to actomyosin.
- This suggests the ATPase is composed of actin- and myosin-like proteins (stenin and neurin).
- Distinct ATPases were found in microsomes, and a different pattern in coated vesicles, supporting specific localization.
Conclusions:
- The primary components of the Ca(2+)-sensitive Mg(2+)-dependent ATPase in brain synaptic vesicles are likely actin- and myosin-like proteins, collectively termed neurostenin.
- The neurostenin complex appears to be specifically localized within plain synaptic vesicles.
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