Evidence map›Paper›PMID 26334391›Full record

ArticleNeurochemical research2015

Functional Expression of Electron Transport Chain and FoF1-ATP Synthase in Optic Nerve Myelin Sheath.

Martina Bartolucci, Silvia Ravera, Greta Garbarino, Paola Ramoino, Sara Ferrando, Daniela Calzia, Simona Candiani, Alessandro Morelli, Isabella Panfoli

Abstract read
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In one paragraph

Article in Neurochemical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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    Article
  10. Article
  11. Review
  12. Review
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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

9 authors at 1 institution in 1 country.

Martina BartolucciBiochemistry Laboratory, Department of Pharmacy (DIFAR), University of Genova, Viale Benedetto XV, 3, 16132, Genoa, Italy.
Silvia RaveraBiochemistry Laboratory, Department of Pharmacy (DIFAR), University of Genova, Viale Benedetto XV, 3, 16132, Genoa, Italy. silvia.ravera@gmail.com.
Greta GarbarinoDepartment of Earth, Environmental and Life Sciences, (DISTAV), University of Genova, C.so Europa 26, 16132, Genoa, Italy.
Paola RamoinoDepartment of Earth, Environmental and Life Sciences, (DISTAV), University of Genova, C.so Europa 26, 16132, Genoa, Italy.
Sara FerrandoDepartment of Earth, Environmental and Life Sciences, (DISTAV), University of Genova, C.so Europa 26, 16132, Genoa, Italy.
Daniela CalziaBiochemistry Laboratory, Department of Pharmacy (DIFAR), University of Genova, Viale Benedetto XV, 3, 16132, Genoa, Italy.
Simona CandianiDepartment of Earth, Environmental and Life Sciences, (DISTAV), University of Genova, C.so Europa 26, 16132, Genoa, Italy.
Alessandro MorelliBiochemistry Laboratory, Department of Pharmacy (DIFAR), University of Genova, Viale Benedetto XV, 3, 16132, Genoa, Italy.
Isabella PanfoliBiochemistry Laboratory, Department of Pharmacy (DIFAR), University of Genova, Viale Benedetto XV, 3, 16132, Genoa, Italy.
University of Genoa · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Our previous studies reported evidence for aerobic ATP synthesis by myelin from both bovine brainstem and rat sciatic nerve. Considering that the optic nerve displays a high oxygen demand, here we evaluated the expression and activity of the five Respiratory Complexes in myelin purified from either bovine or murine optic nerves. Western blot analyses on isolated myelin confirmed the expression of ND4L (subunit of Complex I), COX IV (subunit of Complex IV) and β subunit of F1Fo-ATP synthase. Moreover, spectrophotometric and in-gel activity assays on isolated myelin, as well as histochemical activity assays on both bovine and murine transversal optic nerve sections showed that the respiratory Complexes are functional in myelin and are organized in a supercomplex. Expression of oxidative phosphorylation proteins was also evaluated on bovine optic nerve sections by confocal and transmission electron microscopy. Having excluded a mitochondrial contamination of isolated myelin and considering the results form in situ analyses, it is proposed that the oxidative phosphorylation machinery is truly resident in optic myelin sheath. Data may shed a new light on the unknown trophic role of myelin sheath. It may be energy supplier for the axon, explaining why in demyelinating diseases and neuropathies, myelin sheath loss is associated with axonal degeneration.

Indexed as

Adenosine TriphosphateAnimalsAxonsCattleElectron Transport Chain Complex ProteinsMaleMiceMitochondriaMyelin SheathNADH DehydrogenaseNeurogliaOptic NerveOxidative PhosphorylationProton-Translocating ATPasesAdenosine TriphosphateElectron Transport Chain Complex ProteinsNADH DehydrogenaseNADH dehydrogenase subunit 4Proton-Translocating ATPasesATP synthesisGlia metabolismMyelin sheathOptic nerveOxidative phosphorylation

Identifiers

PMID26334391
OpenAlexW1480277763

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.