Evidence map›Paper›PMID 29618516›Full record

ArticleThe Journal of biological chemistry2018

The proinflammatory protein HMGB1 is a substrate of transglutaminase-2 and forms high-molecular weight complexes with autoantigens.

William L Willis, Linan Wang, Takuma Tsuzuki Wada, Mark Gardner, Omar Abdouni, Jeffrey Hampton, Giancarlo Valiente, Nicholas Young, Stacy Ardoin, Sudha Agarwal and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. 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
1.3field-weighted citation impact, top 23% 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, 21 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Assessment of HMGB1 Release During Experimentally Induced Pyroptosis.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Bio-protocol · 2020
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. 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

13 authors at 2 institutions in 1 country.

William L WillisFrom the Departments of Internal Medicine, william.willis@osumc.edu.
Linan WangThe Ohio State University Wexner Medical Center, Columbus, Ohio 43210.
Takuma Tsuzuki WadaFrom the Departments of Internal Medicine.
Mark GardnerFrom the Departments of Internal Medicine.
Omar AbdouniFrom the Departments of Internal Medicine.
Jeffrey HamptonFrom the Departments of Internal Medicine.
Giancarlo ValienteFrom the Departments of Internal Medicine.
Nicholas YoungFrom the Departments of Internal Medicine.
Stacy ArdoinFrom the Departments of Internal Medicine.
Sudha AgarwalDivision of Biosciences, The Ohio State University College of Dentistry, Columbus, Ohio 43210.
Michael A FreitasThe Ohio State University Wexner Medical Center, Columbus, Ohio 43210.
Lai-Chu WuFrom the Departments of Internal Medicine.
Wael N JarjourFrom the Departments of Internal Medicine, wael.jarjour@osumc.edu.
The Ohio State University · USThe Ohio State University Wexner Medical Center · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
The Ohio State University Center for clinical and Translational ScienceUL1TR001070 · NCATS · OHIO STATE UNIVERSITY · PI JACKSON, REBECCA D · 2013 to 2017
$22.6M
Tumor ImmunologyT32CA090223 · NCI · OHIO STATE UNIVERSITY · PI CARSON, WILLIAM E. · 2002 to 2023
$4.1M
Understanding the role of EZH2 misregulation in chromatin crosstalR01GM122436 · NIGMS · OHIO STATE UNIVERSITY · PI FREITAS, MICHAEL A., PARTHUN, MARK R · 2018 to 2019
$611k
NCATS NIH HHS UL1 TR001070NCI NIH HHS P30 CA016058NCI NIH HHS T32 CA090223NIGMS NIH HHS R01 GM122436
6 · The paper itself

Abstract

High-mobility group box 1 (HMGB1) is a chromatin-associated protein that, in response to stress or injury, translocates from the nucleus to the extracellular milieu, where it functions as an alarmin. HMGB1's function is in part determined by the complexes (HMGB1c) it forms with other molecules. However, structural modifications in the HMGB1 polypeptide that may regulate HMGB1c formation have not been previously described. In this report, we observed high-molecular weight, denaturing-resistant HMGB1c in the plasma and peripheral blood mononuclear cells of individuals with systemic lupus erythematosus (SLE) and, to a much lesser extent, in healthy subjects. Differential HMGB1c levels were also detected in mouse tissues and cultured cells, in which these complexes were induced by endotoxin or the immunological adjuvant alum. Of note, we found that HMGB1c formation is catalyzed by the protein-cross-linking enzyme transglutaminase-2 (TG2). Cross-link site mapping and MS analysis revealed that HMGB1 can be cross-linked to TG2 as well as a number of additional proteins, including human autoantigens. These findings have significant functional implications for studies of cellular stress responses and innate immunity in SLE and other autoimmune disease.

Indexed as

AutoantigensCells, CulturedGTP-Binding ProteinsHMGB1 ProteinHumansLeukocytes, MononuclearLupus Erythematosus, SystemicMolecular WeightProtein Glutamine gamma Glutamyltransferase 2Substrate SpecificityTransglutaminasesAutoantigensGTP-Binding ProteinsHMGB1 ProteinHMGB1 protein, humanProtein Glutamine gamma Glutamyltransferase 2Transglutaminasesautoimmune diseaseautoimmunitycalciumhigh-mobility group box 1lipopolysaccharide (LPS)protein cross-linkingsystemic lupus erythematosustransglutaminase

Identifiers

PMID29618516
PMCPMC5986221
OpenAlexW2795793231

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.