Evidence map›Paper›PMID 26223783›Full record

ArticleMolecular neurodegeneration2015

Studies of lipopolysaccharide effects on the induction of α-synuclein pathology by exogenous fibrils in transgenic mice.

Nicola J Rutherford, Amanda N Sacino, Mieu Brooks, Carolina Ceballos-Diaz, Thomas B Ladd, Jasie K Howard, Todd E Golde, Benoit I Giasson

Open access · goldAbstract read
In one paragraph

Article in Molecular neurodegeneration, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.

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  10. NK cells clear α-synuclein and the depletion of NK cells exacerbates synuclein pathology in a mouse model of α-synucleinopathy.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

8 authors at 1 institution in 1 country.

Nicola J RutherfordCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. njrutherford@ufl.edu.
Amanda N SacinoCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. asacino@ufl.edu.
Mieu BrooksCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. mbrooks87@ufl.edu.
Carolina Ceballos-DiazCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. caro.ceb81@ufl.edu.
Thomas B LaddCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. tomladd@ufl.edu.
Jasie K HowardCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. jasiehoward@ufl.edu.
Todd E GoldeCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. tgolde@ufl.edu.
Benoit I GiassonCenter for Translational Research in Neurodegenerative Disease, Department of Neuroscience, University of Florida, 1275 Center Drive, Room BMS J-483, PO Box 100159, Gainesville, FL, 32610, USA. bgiasson@ufl.edu.
University of Florida · US

Funding

Mechanisms of Aggregated Alpha-Synuclein Induction and ProgressionR01NS089622 · NINDS · UNIVERSITY OF FLORIDA · PI GIASSON, BENOIT I · 2014 to 2018
$1.6M
NINDS NIH HHS NS089622NINDS NIH HHS R01 NS089622
6 · The paper itself

Abstract

backgroundParkinson's disease (PD) is a progressive neurodegenerative disorder that is pathologically characterized by loss of dopaminergic neurons from the substantia nigra, the presence of aggregated α-synuclein (αS) and evidence of neuroinflammation. Experimental studies have shown that the cerebral injection of recombinant fibrillar αS, especially in αS transgenic mouse models, can induce the formation and spread of αS inclusion pathology. However, studies reporting this phenomenon did not consider the presence of lipopolysaccharide (LPS) in the injected αS, produced in E. coli, as a potential confound. The objectives of this study are to develop a method to remove the LPS contamination and investigate the differences in pathologies induced by αS containing LPS or αS highly purified of LPS. RESULTS AND

conclusionsWe were able to remove >99.5% of the LPS contamination from the αS preparations through the addition of a cation exchange step during purification. The αS pathology induced by injection of fibrils produced from αS containing LPS or purified of LPS, showed a similar distribution pattern; however, there was less spread into the cortex of the mice injected with αS containing higher levels of LPS. As previously reported, injection of αS fibrils could induce astrogliosis, and αS inclusions were present within astrocytes in mice injected with fibrils comprised of αS with or without cation exchange purification. Furthermore, we identified the presence of αS pathology in ependymal cells in both groups of mice, which suggests the involvement of a novel mechanism for spread in this model of αS pathology.

Indexed as

alpha-SynucleinAnimalsAstrocytesCell CountCells, CulturedChromatography, Ion ExchangeDisease ProgressionDrug ContaminationEndotoxinsEntorhinal CortexEscherichia coliHippocampusHumansHydrophobic and Hydrophilic InteractionsInclusion BodiesInflammationalpha-Synucleinendotoxin, Escherichia coliEndotoxinsRecombinant Proteins

Identifiers

PMID26223783
PMCPMC4520273
OpenAlexW2152827274

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.