Evidence map›Paper›PMID 24188129›Full record

ArticleJournal of neuroinflammation2013

The absence of myelin basic protein promotes neuroinflammation and reduces amyloid β-protein accumulation in Tg-5xFAD mice.

Ming-Hsuan Ou-Yang, William E Van Nostrand

Open access · goldAbstract read
In one paragraph

Article in Journal of neuroinflammation, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.

  1. Pooled it
  2. Emerging Role of Oligodendrocytes Malfunction in the Progression of Alzheimer's Disease.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2025
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  15. Proteomic Analysis of Mouse Brain Subjected to Spaceflight.International journal of molecular sciences · 2018
    Article
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  18. Article
  19. Activation of the factor XII-driven contact system in Alzheimer's disease patient and mouse model plasma.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  20. Article
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 1 institution in 1 country.

Ming-Hsuan Ou-Yang
William E Van NostrandDepartments of Neurosurgery & Medicine, Stony Brook University, Stony Brook, NY 11794-8122, USA. William.VanNostrand@stonybrook.edu.
Stony Brook University · US

Funding

Influence of myelin basic protein on neuronal A Beta assembly and toxicityR21NS079951 · NINDS · STATE UNIVERSITY NEW YORK STONY BROOK · PI VAN NOSTRAND, WILLIAM E. · 2012 to 2013
$424k
Mouse Model of Myelin Basic Protein-Amyloid Beta Interactions in BrainR21AG039215 · NIA · STATE UNIVERSITY NEW YORK STONY BROOK · PI VAN NOSTRAND, WILLIAM E. · 2011 to 2012
$310k
NIA NIH HHS R21-AG039215NINDS NIH HHS R21-NS079951
6 · The paper itself

Abstract

backgroundAbnormal accumulation of amyloid β-protein (Aβ) in the brain plays an important role in the pathogenesis \of Alzheimer's disease (AD). Aβ monomers assemble into oligomers and fibrils that promote neuronal dysfunction. This assembly pathway is influenced by naturally occurring brain molecules, the Aβ chaperone proteins, which bind to Aβ and modulate its aggregation. Myelin basic protein (MBP) was previously identified as a novel Aβ chaperone protein and a potent inhibitor for Aβ fibril assembly in vitro.

methodsIn this study, we determined whether the absence of MBP would influence Aβ pathology in vivo by breeding MBP knockout mice (MBP-/-) with Tg-5xFAD mice, a model of AD-like parenchymal Aβ pathology.

resultsThrough biochemical and immunohistochemical experiments, we found that bigenic Tg-5xFAD/MBP-/- mice had a significant decrease of insoluble Aβ and parenchymal plaque deposition at an early age. The expression of transgene encoded human AβPP, the levels of C-terminal fragments generated during Aβ production and the intracellular Aβ were unaffected in the absence of MBP. Likewise, we did not find a significant difference in plasma Aβ or cerebrospinal fluid Aβ, suggesting these clearance routes were unaltered in bigenic Tg-5xFAD/MBP-/- mice. However, MBP-/- mice and bigenic Tg-5xFAD/MBP-/- mice exhibited elevated reactive astrocytes and activated microglia compared with Tg-5xFAD mice. The Aβ degrading enzyme matrix metalloproteinase 9 (MMP-9), which is expressed by activated glial cells, was significantly increased in the Tg-5xFAD/MBP-/- mice.

conclusionsThese findings indicate that the absence of MBP decreases Aβ deposition in transgenic mice and that this consequence may result from increased glial activation and expression of MMP-9, an Aβ degrading enzyme.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsBrainDisease Models, AnimalEnzyme-Linked Immunosorbent AssayHumansImmunoblottingImmunohistochemistryInflammationMiceMice, KnockoutMice, TransgenicMyelin Basic ProteinAmyloid beta-PeptidesMbp protein, mouseMyelin Basic Protein

Identifiers

PMID24188129
PMCPMC4228351
OpenAlexW2137664031

What OpenQuestion holds

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LicenceCC BY
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.