Evidence map›Paper›PMID 30774410›Full record

ArticleJournal of inflammation research2019

Myelin basic protein charge isomers change macrophage polarization.

Elene Tsitsilashvili, Maia Sepashvili, Marika Chikviladze, Lali Shanshiashvili, David Mikeladze

Open access · goldAbstract read
In one paragraph

Article in Journal of inflammation research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 45% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
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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

5 authors at 1 institution in 1 country.

Elene TsitsilashviliInstitute of Chemical Biology, Ilia State University, Tbilisi, Georgia, lali_shanshiashvili@iliauni.edu.ge.
Maia SepashviliInstitute of Chemical Biology, Ilia State University, Tbilisi, Georgia, lali_shanshiashvili@iliauni.edu.ge.
Marika ChikviladzeInstitute of Chemical Biology, Ilia State University, Tbilisi, Georgia, lali_shanshiashvili@iliauni.edu.ge.
Lali ShanshiashviliInstitute of Chemical Biology, Ilia State University, Tbilisi, Georgia, lali_shanshiashvili@iliauni.edu.ge.
David MikeladzeInstitute of Chemical Biology, Ilia State University, Tbilisi, Georgia, lali_shanshiashvili@iliauni.edu.ge.
Ilia State University · GE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

purposeDuring a neuronal injury, a variety of immune cells infiltrate into the local microenvironment at the demyelination site. After the destruction of the intact myelin sheath, its major constituent myelin basic protein (MBP) dissociates from the plasma membrane and acts as a free ligand on the infiltrated immune cells. MBP exhibits charge microheterogeneity as a result of post-translational modifications, but the effect of various isomers of MBP on the activity of macrophages is not known. MATERIALS AND

methodsMBP was isolated and purified from bovine brain white matter. RAW 264.7 macrophages were cultured in DMEM supplemented with heat-inactivated fetal bovine serum. For evaluation of macrophage polarization following treatment of RAW 264.7 cells with MBP charge isomers, inducible nitric oxide synthase (iNOS) expression (M1 phenotype marker) and arginase-1 expression (M2 phenotype marker) were determined in cell lysates by ELISA. To assess Rac activity, G-LISA Rac Activation Assay system was used. The expression of receptor for advanced glycation end-products (RAGE) and high mobility group box 1 (HMGB1) protein were assayed by Western blot analysis.

resultsOur results have shown that minimally modified C1 component of MBP increases the expression of arginase-1 in cells, decreases the expression of iNOS, does not change the secretion of HMGB1 protein, but significantly elevates surface expression of RAGE, and in parallel, increases the activity of small GTPase Rac. On the other hand, highly modified deiminated isomer C8-MBP increases the secretion of HMGB1 protein but does not change the expression of arginase-1 or the content of RAGE.

conclusionThese data indicate that deiminated C8 isomer of MBP tends to polarize RAW macrophages into M1 phenotypes, whereas C1 enhances the activity of M2 phenotype markers.

Indexed as

Arginase-1HMGB1iNOSRAGE

Identifiers

PMID30774410
PMCPMC6350649
OpenAlexW2914770613

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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.