A new function for glycine GlyT2 transporters: Stimulation of ?-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca2+-dependent anion channels (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• A new function for glycine GlyT2 transporters: Stimulation of ?-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca2+-dependent anion channels (Articolo in rivista) (literal)

Anno

• 2014-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1002/jnr.23321 (literal)

Alternative label

• Milanese M.; Romei C.; Usai C.; Oliveri M.; Raiteri L. (2014)
  A new function for glycine GlyT2 transporters: Stimulation of ?-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca2+-dependent anion channels
  in Journal of neuroscience research
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Milanese M.; Romei C.; Usai C.; Oliveri M.; Raiteri L. (literal)

Pagina inizio

• 398 (literal)

Pagina fine

• 408 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.scopus.com/inward/record.url?eid=2-s2.0-84892476427&partnerID=q2rCbXpz (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 92 (literal)

Rivista

• Journal of neuroscience research (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 3 (literal)

Note

• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Pharmacy, Pharmacology and Toxicology Section, University of Genoa, Genoa, Italy; Center of Excellence for Biomedical Research, University of Genoa, Genoa, Italy; Institute of Biophysics, National Research Council, Genoa, Italy; National Institute of Neuroscience, Genoa, Italy (literal)

Titolo

• A new function for glycine GlyT2 transporters: Stimulation of ?-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca2+-dependent anion channels (literal)

Abstract

• Glycine GlyT2 transporters are localized on glycine-storing nerve endings. Their main function is to accumulate glycine to replenish synaptic vesicles. Glycine was reported to be costored with -aminobutyric acid (GABA) in cerebellar interneurons that may coexpress glycine and GABA transporters, and this is confirmed here by confocal microscopy analysis showing coexpression of GAT1 and GlyT2 transporters on microtubule-associated protein-2-positive synaptosomes. It was found that GABA uptake elicited glycine release from cerebellar nerve endings by various mechanisms. We investigated whether and by what mechanisms activation of glycine transporters could mediate release of GABA. Nerve endings purified from cerebellum were prelabeled with [H-3]GABA and exposed to glycine. Glycine stimulated [H-3]GABA release in a concentration-dependent manner. The glycine effect was insensitive to strychnine or to 5,7-dichlorokynurenate but it was abolished when GlyT2 transporters were blocked. About 20% of the evoked release was dependent on external Ca2+ entered by reversal of plasmalemmal Na+/Ca(2+)exchangers. A significant portion of the GlyT2-mediated release of [H-3]GABA (about 50% of the external Ca2+-independent release) occurred by reversal of GABA GAT1 transporters. Na+ ions, reaching the cytosol during glycine uptake through GlyT2, activated mitochondrial Na+/Ca2+ exchangers, causing an increase in cytosolic Ca2+, which in turn triggered a Ca2+-induced Ca2+ release process at inositoltrisphosphate receptors. Finally, the increased availability of Ca2+ in the cytosol allowed the opening of anion channels permeable to GABA. In conclusion, GlyT2 transporters not only take up glycine to replenish synaptic vesicles but can also mediate release of GABA by reversal of GAT1 and permeation through anion channels. (c) 2013 Wiley Periodicals, Inc. (literal)

Prodotto di

• Processi di membrana nella comunicazione intra- ed inter-cellulare (MD.P01.001.001) (Modulo)
• Istituto di biofisica (IBF) (Istituto)

Autore CNR

• CESARE USAI (Persona)

Insieme di parole chiave

• Keywords of "A new function for glycine GlyT2 transporters: Stimulation of ?-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca2+-dependent anion channels" (Insieme di parole chiave)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Processi di membrana nella comunicazione intra- ed inter-cellulare (MD.P01.001.001) (Modulo)

Autore CNR di

• CESARE USAI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Journal of neuroscience research (Rivista)

Insieme di parole chiave di

• Keywords of "A new function for glycine GlyT2 transporters: Stimulation of ?-aminobutyric acid release from cerebellar nerve terminals through GAT1 transporter reversal and Ca2+-dependent anion channels" (Insieme di parole chiave)