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J. Biol. Chem., Vol. 276, Issue 39, 36764-36769, September 28, 2001
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From the Departments of Pediatrics and Physiology, Steele Memorial
Children's Research Center, University of Arizona Health Sciences
Center, Tucson, Arizona 85724
Glutamate is the major excitatory
neurotransmitter in the mammalian central nervous system. Packaging and
storage of glutamate into glutamatergic neuronal vesicles requires
ATP-dependent vesicular glutamate uptake systems, which
utilize the electrochemical proton gradient as a driving force. VGLUT1,
the first identified vesicular glutamate transporter, is only expressed
in a subset of glutamatergic neurons. We report here the molecular
cloning and functional characterization of a novel glutamate
transporter, VGLUT2, from mouse brain. VGLUT2 has all major functional
characteristics of a synaptic vesicle glutamate transporter, including
ATP dependence, chloride stimulation, substrate specificity, and
substrate affinity. It has 75 and 79% amino acid identity with human
and rat VGLUT1, respectively. However, expression patterns of VGLUT2 in
brain are different from that of VGLUT1. In addition, VGLUT2 activity
is dependent on both membrane potential and pH gradient of the
electrochemical proton gradient, whereas VGLUT1 is primarily dependent
on only membrane potential. The presence of VGLUT2 in brain
regions lacking VGLUT1 suggests that the two isoforms together play an
important role in vesicular glutamate transport in glutamatergic neurons.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF 324864.
Molecular and Functional Analysis of a Novel Neuronal Vesicular
Glutamate Transporter*
,
*
This work was supported by NIDDK, National Institutes of
Health Grant 2R01-R37DK-33209 and the W. M. Keck Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Tucson Hospital Medical Education Program, 5301 E. Grant Rd., Tucson, AZ 85733. E-mail: lqbai@yahoo.com.
§
To whom correspondence should be addressed: Dept. of Pediatrics,
Director, Steele Memorial Children's Research Center, University of Arizona Health Sciences Center, 1501 N. Campbell Ave., Tucson, AZ
85724. Tel.: 520-626-5170; Fax: 520-626-4141; E-mail:
fghishan@peds.arizona.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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