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Publication : Synaptic vesicle mobility in mouse motor nerve terminals with and without synapsin.

First Author  Gaffield MA Year  2007
Journal  J Neurosci Volume  27
Issue  50 Pages  13691-700
PubMed ID  18077680 Mgi Jnum  J:130565
Mgi Id  MGI:3771915 Doi  10.1523/JNEUROSCI.3910-07.2007
Citation  Gaffield MA, et al. (2007) Synaptic vesicle mobility in mouse motor nerve terminals with and without synapsin. J Neurosci 27(50):13691-700
abstractText  We measured synaptic vesicle mobility using fluorescence recovery after photobleaching of FM 1-43 [N-(3-triethylammoniumpropyl)-4-(4-(dibutylamino)styryl) pyridinium dibromide] stained mouse motor nerve terminals obtained from wild-type (WT) and synapsin triple knock-out (TKO) mice at room temperature and physiological temperature. Vesicles were mobile in resting terminals at physiological temperature but virtually immobile at room temperature. Mobility was increased at both temperatures by blocking phosphatases with okadaic acid, decreased at physiological temperature by blocking kinases with staurosporine, and unaffected by disrupting actin filaments with latrunculin A or reducing intracellular calcium concentration with BAPTA-AM. Synapsin TKO mice showed reduced numbers of synaptic vesicles and reduced FM 1-43 staining intensity. Synaptic transmission, however, was indistinguishable from WT, as was synaptic vesicle mobility under all conditions tested. Thus, in TKO mice, and perhaps WT mice, a phospho-protein different from synapsin but otherwise of unknown identity is the primary regulator of synaptic vesicle mobility.
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