Evidence map›Paper›PMID 23264627›Full record

ArticleThe Journal of biological chemistry2013

Identification of the low density lipoprotein (LDL) receptor-related protein-1 interactome in central nervous system myelin suggests a role in the clearance of necrotic cell debris.

Anthony Fernandez-Castaneda, Sanja Arandjelovic, Travis L Stiles, Ryan K Schlobach, Kerri A Mowen, Steven L Gonias, Alban Gaultier

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
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

41 citing papers in PubMed.

  1. Article
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  16. A Soluble PrPJournal of immunology (Baltimore, Md. : 1950) · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Entanglement of CCR5 and Alzheimer's Disease.Frontiers in aging neuroscience · 2019
    Review
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

7 authors.

Anthony Fernandez-CastanedaDepartment of Neuroscience and Center for Brain Immunology and Glia, University of Virginia, Charlottesville, Virginia 22908, USA.
Sanja Arandjelovic
Travis L Stiles
Ryan K Schlobach
Kerri A Mowen
Steven L Gonias
Alban Gaultier

Funding

REGULATION OF UROKINASE RECEPTOR ACTIVITY BY LRPR01HL060551 · NHLBI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI GONIAS, STEVEN L. · 1999 to 2014
$4.0M
Cytokine Gene Regulation by Modification of Arginine ResiduesR01AI067460 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI MOWEN, KERRI A · 2006 to 2010
$2.3M
The Role of Arginine Methyltransferases in Interferon SignalingR01GM085117 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI MOWEN, KERRI A · 2008 to 2011
$1.5M
Function of LRP-1 in Multiple Sclerosis.R21NS071347 · NINDS · UNIVERSITY OF VIRGINIA · PI GAULTIER, ALBAN P · 2011 to 2012
$435k
NHLBI NIH HHS R01 HL-060551NHLBI NIH HHS R01 HL060551NIAID NIH HHS R01 AI067460NIGMS NIH HHS R01 GM085117NINDS NIH HHS R21 NS071347NINDS NIH HHS R21NS071347
6 · The paper itself

Abstract

In the central nervous system (CNS), fast neuronal signals are facilitated by the oligodendrocyte-produced myelin sheath. Oligodendrocyte turnover or injury generates myelin debris that is usually promptly cleared by phagocytic cells. Failure to remove dying oligodendrocytes leads to accumulation of degraded myelin, which, if recognized by the immune system, may contribute to the development of autoimmunity in diseases such as multiple sclerosis. We recently identified low density lipoprotein receptor-related protein-1 (LRP1) as a novel phagocytic receptor for myelin debris. Here, we report characterization of the LRP1 interactome in CNS myelin. Fusion proteins were designed corresponding to the extracellular ligand-binding domains of LRP1. LRP1 partners were isolated by affinity purification and characterized by mass spectrometry. We report that LRP1 binds intracellular proteins via its extracellular domain and functions as a receptor for necrotic cells. Peptidyl arginine deiminase-2 and cyclic nucleotide phosphodiesterase are novel LRP1 ligands identified in our screen, which interact with full-length LRP1. Furthermore, the extracellular domain of LRP1 is a target of peptidyl arginine deiminase-2-mediated deimination in vitro. We propose that LRP1 functions as a receptor for endocytosis of intracellular components released during cellular damage and necrosis.

Indexed as

AnimalsApoptosisCentral Nervous SystemCitrullineCloning, MolecularEndocytosisGlutathione TransferaseGreen Fluorescent ProteinsHomeostasisHumansJurkat CellsLigandsLow Density Lipoprotein Receptor-Related Protein-1Mass SpectrometryMiceMultiple SclerosisCitrullineGlutathione TransferaseGreen Fluorescent ProteinsLigandsLow Density Lipoprotein Receptor-Related Protein-1

Identifiers

PMID23264627
PMCPMC3576060

What OpenQuestion holds

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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.