title: Activity-dependent changes of the presynaptic synaptophysin-synaptobrevin complex in adult rat brain.
abstract: The vesicular protein synaptobrevin contributes to two mutually exclusive complexes in mature synapses. Synaptobrevin tightly interacts with the plasma membrane proteins syntaxin and SNAP 25 forming the SNARE complex as a prerequisite for exocytotic membrane fusion. Alternatively, synaptobrevin binds to the vesicular protein synaptophysin. It is unclear whether SNARE complex formation is diminished or facilitated when synaptobrevin is bound to synaptophysin. Here we show that the synaptophysin-synaptobrevin complex is increased in adult rat brain after repeated synaptic hyperactivity in the kindling model of epilepsy. Two days after the last kindling-induced stage V seizure the relative amount of synaptophysin-synaptobrevin complex obtained by co-immunoprecipitation from cortical and hippocampal membranes was increased twofold compared to controls. By contrast the relative amounts of various synaptic proteins as well as that of the SNARE complex did not change in membrane preparations from kindled rats compared to controls. The increased amount of synaptophysin-synaptobrevin complex in kindled rats supports the idea that this complex represents a reserve pool for synaptobrevin enabling synaptic vesicles to adjust to an increased demand for synaptic efficiency. We conclude that the synaptophysin-synaptobrevin interaction is involved in activity-dependent plastic changes in adult rat brain.
authors.affiliation: Institut für Anatomie, NWFZ, Humboldt-Universität Berlin, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Hinz
authors.forename: A
authors.initials: A
authors.lastname: Becher
authors.forename: D
authors.initials: D
authors.lastname: Mitter
authors.forename: K
authors.initials: K
authors.lastname: Schulze
authors.forename: U
authors.initials: U
authors.lastname: Heinemann
authors.forename: A
authors.initials: A
authors.lastname: Draguhn
authors.forename: G
authors.initials: G
authors.lastname: Ahnert-Hilger
mesh_terms: D000367:Age Factors; D000679:Amygdala / Q000378:metabolism* / Q000503:physiopathology; D000818:Animals; D004827:Epilepsy / Q000378:metabolism* / Q000503:physiopathology; D007696:Kindling, Neurologic / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000378:metabolism; D009473:Neuronal Plasticity / Q000502:physiology; D017729:Presynaptic Terminals / Q000378:metabolism*; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D051381:Rats; D050600:SNARE Proteins; D016708:Synaptophysin / Q000378:metabolism*; D050825:Synaptosomal-Associated Protein 25; D033921:Vesicular Transport Proteins
chemical_list: D008565:Membrane Proteins; D009419:Nerve Tissue Proteins; D050765:Qa-SNARE Proteins; D050683:R-SNARE Proteins; D050600:SNARE Proteins; C494210:Snap25 protein, rat; D016708:Synaptophysin; D050825:Synaptosomal-Associated Protein 25; D033921:Vesicular Transport Proteins