Evidence map›Paper›PMID 19259829›Full record

ReviewMolecular neurobiology2009

Protective actions of the vesicular monoamine transporter 2 (VMAT2) in monoaminergic neurons.

Thomas S Guillot, Gary W Miller

Abstract readReview
PubMed Publisher
In one paragraph

Review in Molecular neurobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

104 citing papers in PubMed, 200 citations in OpenAlex.

  1. Review
  2. Molecular mirror: reflecting the complexity of Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Review
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44 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Thomas S GuillotCenter for Neurodegenerative Disease, Emory University, Atlanta, GA, USA.
Gary W Miller
Emory University · USInstitute for Neurodegenerative Disorders · US

Funding

PROJECT 3: METABOLOMIC BIOMARKERS OF PARKINSON'S DISEASEP01ES016731 · NIEHS · EMORY UNIVERSITY · PI MILLER, GARY W · 2008 to 2012
$6.7M
NIEHS NIH HHS ES016731-01NIEHS NIH HHS P01 ES016731
6 · The paper itself

Abstract

Vesicular monoamine transporters (VMATs) are responsible for the packaging of neurotransmitters such as dopamine, serotonin, norepinephrine, and epinephrine into synaptic vesicles. These proteins evolved from precursors in the major facilitator superfamily of transporters and are among the members of the toxin extruding antiporter family. While the primary function of VMATs is to sequester neurotransmitters within vesicles, they can also translocate toxicants away from cytosolic sites of action. In the case of dopamine, this dual role of VMAT2 is combined-dopamine is more readily oxidized in the cytosol where it can cause oxidative stress so packaging into vesicles serves two purposes: neurotransmission and neuroprotection. Furthermore, the deleterious effects of exogenous toxicants on dopamine neurons, such as MPTP, can be attenuated by VMAT2 activity. The active metabolite of MPTP can be kept within vesicles and prevented from disrupting mitochondrial function thereby sparing the dopamine neuron. The highly addictive drug methamphetamine is also neurotoxic to dopamine neurons by using dopamine itself to destroy the axon terminals. Methamphetamine interferes with vesicular sequestration and increases the production of dopamine, escalating the amount in the cytosol and leading to oxidative damage of terminal components. Vesicular transport seems to resist this process by sequestering much of the excess dopamine, which is illustrated by the enhanced methamphetamine neurotoxicity in VMAT2-deficient mice. It is increasingly evident that VMAT2 provides neuroprotection from both endogenous and exogenous toxicants and that while VMAT2 has been adapted by eukaryotes for synaptic transmission, it is derived from phylogenetically ancient proteins that originally evolved for the purpose of cellular protection.

Indexed as

1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridineAnimalsBiogenic MonoaminesHumansMPTP PoisoningNeuronsNeuroprotective AgentsSynaptic TransmissionVesicular Monoamine Transport Proteins1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridineBiogenic MonoaminesNeuroprotective AgentsVesicular Monoamine Transport Proteins

Identifiers

PMID19259829
OpenAlexW2091280342

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.