http://www.cnr.it/ontology/cnr/individuo/prodotto/ID170884
Synaptobrevin2-expressing vesicles in rat astrocytes: insights into molecular characterization, dynamics and exocytosis (Articolo in rivista)
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- Label
- Synaptobrevin2-expressing vesicles in rat astrocytes: insights into molecular characterization, dynamics and exocytosis (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1113/jphysiol.2005.094052 (literal)
- Alternative label
Crippa D; Schenk U; Francolini M; Rosa P; Verderio C; Zonta M; Pozzan T; Matteoli M; Carmignoto G (2006)
Synaptobrevin2-expressing vesicles in rat astrocytes: insights into molecular characterization, dynamics and exocytosis
in Journal of physiology (Lond., Print)
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- Crippa D; Schenk U; Francolini M; Rosa P; Verderio C; Zonta M; Pozzan T; Matteoli M; Carmignoto G (literal)
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- Pagina fine
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Crippa D; Zonta M; Pozzan T; Carmignoto G. Istitute of Neuroscience CNR, Padova
Verderio C.; Matteoli M. Istitute of Neuroscience CNR, Milano (literal)
- Titolo
- Synaptobrevin2-expressing vesicles in rat astrocytes: insights into molecular characterization, dynamics and exocytosis (literal)
- Abstract
- The SNARE-dependent exocytosis of glutamate-containing vesicles in astrocytes is increasingly
viewed as an important signal at the basis of the astrocyte-to-neurone communication system
in the brain. Here we provide further insights into the molecular features and dynamics of
vesicles in cultured astrocytes.We found that immunoisolated synaptobrevin2 vesicles are clear
vesicles quite heterogenous in size and contain the vesicular glutamate transporter v-Glut-2.
Moreover, they are immunopositive for synaptotagmin IV, forAMPA receptor subunits GluR2,3
and, to a lesser extent, for GluR1.We also provide direct evidence for the functional expression
of v-Glut-2 in astrocytes and demonstrate that synaptobrevin2-positive vesicles can specifically
take up (3H)L-glutamate via a bafilomycin-sensitive mechanism. Finally, by time lapse confocal
microscopy, we show that a subpopulation of vesicles (tagged with a synaptobrevin2-EGFP
chimera) is highly mobile and can fuse with the plasma membrane, preferentially at the level of
the astrocyte processes, in a Ca2+-dependent manner. These latter observations, together with
the evidence reported here for the expression of functional v-Glut-2 in synaptobrevin2-positive
vesicles, provide a molecular basis for regulated exocytosis in astrocyte. (literal)
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