Evidence map›Paper›PMID 22750521›Full record

ArticleNeurobiology of disease2012

Motor terminal degeneration unaffected by activity changes in SOD1(G93A) mice; a possible role for glycolysis.

Dario I Carrasco, Edyta K Bichler, Mark M Rich, Xueyong Wang, Kevin L Seburn, Martin J Pinter

Open access · greenAbstract read
In one paragraph

Article in Neurobiology of disease, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

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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

6 authors at 4 institutions in 1 country.

Dario I CarrascoDepartment of Physiology, Emory University, Atlanta, GA 30322, USA.
Edyta K Bichler
Mark M Rich
Xueyong Wang
Kevin L Seburn
Martin J Pinter
Emory University · USWright State University · USJackson Laboratory · USMorehouse School of Medicine · US

Funding

MOTOR NEURON DISEASE-NEUROPHYSIOLOGY AND PATHOLOGYR01NS031621 · NINDS · EMORY UNIVERSITY · PI PINTER, MARTIN J · 1993 to 2006
$1.8M
Increasing DNA marker informativeness in hereditary canine motor neuron diseaseR03NS057693 · NINDS · EMORY UNIVERSITY · PI PINTER, MARTIN J · 2008 to 2009
$153k
Intramural NIH HHSNINDS NIH HHS NS31621NINDS NIH HHS R01 NS031621NINDS NIH HHS R03 NS057693
6 · The paper itself

Abstract

This study examined whether activity is a contributing factor to motor terminal degeneration in mice that overexpress the G93A mutation of the SOD1 enzyme found in humans with inherited motor neuron disease. Previously, we showed that overload of muscles accomplished by synergist denervation accelerated motor terminal degeneration in dogs with hereditary canine spinal muscular atrophy (HCSMA). In the present study, we found that SOD1 plantaris muscles overloaded for 2months showed no differences of neuromuscular junction innervation status when compared with normally loaded, contralateral plantaris muscles. Complete elimination of motor terminal activity using blockade of sciatic nerve conduction with tetrodotoxin cuffs for 1month also produced no change of plantaris innervation status. To assess possible effects of activity on motor terminal function, we examined the synaptic properties of SOD1 soleus neuromuscular junctions at a time when significant denervation of close synergists had occurred as a result of natural disease progression. When examined in glucose media, SOD1 soleus synaptic properties were similar to wildtype. When glycolysis was inhibited and ATP production limited to mitochondria, however, blocking of evoked synaptic transmission occurred and a large increase in the frequency of spontaneous mEPCs was observed. Similar effects were observed at neuromuscular junctions in muscle from dogs with inherited motor neuron disease (HCSMA), although significant defects of synaptic transmission exist at these neuromuscular junctions when examined in glucose media, as reported previously. These results suggest that glycolysis compensates for mitochondrial dysfunction at motor terminals of SOD1 mice and HCSMA dogs. This compensatory mechanism may help to support resting and activity-related metabolism in the presence of dysfunctional mitochondria and prolong the survival of SOD1 motor terminals.

Indexed as

AnimalsDogsGlycolysisMiceMice, TransgenicMotor Neuron DiseaseMotor NeuronsMuscle, SkeletalNeuromuscular JunctionSuperoxide DismutaseSuperoxide Dismutase-1SOD1 protein, humanSod1 protein, mouseSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID22750521
PMCPMC3430970
OpenAlexW2069228759

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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.