Evidence map›Paper›PMID 18711002›Full record

ArticleBlood2008

Lectin-like domain of thrombomodulin binds to its specific ligand Lewis Y antigen and neutralizes lipopolysaccharide-induced inflammatory response.

Chung-Sheng Shi, Guey-Yueh Shi, Hsi-Min Hsiao, Shi-Ming Hsiao, Yuan-Chung Kao, Kuan-Lin Kuo, Chih-Yuan Ma, Cheng-Hsiang Kuo, Bi-Ing Chang, Chuan-Fa Chang and 3 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Blood, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

62 citing papers in PubMed, 188 citations in OpenAlex.

  1. Article
  2. Lewis Y (LeImmunologic research · 2026
    Article
  3. Observational
  4. Article
  5. Article
  6. Review
  7. Interferon lambda 4 is a gut antimicrobial protein.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Review
  9. Exploring Mechanisms ofCombinatorial chemistry & high throughput screening · 2024
    Article
  10. Article
  11. Chondrocyte Thrombomodulin Protects against Osteoarthritis.International journal of molecular sciences · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Signaling pathways and intervention therapies in sepsis.Signal transduction and targeted therapy · 2021
    Review
  19. Article
  20. The lectin-like domain of thrombomodulin is a drug candidate for both prophylaxis and treatment of liver ischemia and reperfusion injury in mice.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2021
    Article

2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
    Hsiao, Shi-Ming [corrected to Hsiao, Hsi-Min]
5 · Who and what money

Authors and funding

13 authors at 3 institutions in 2 countries.

Chung-Sheng ShiDepartment of Biochemistry and Molecular Biology, College of Medicine, National Cheng Kung University, Taiwan.
Guey-Yueh Shi
Hsi-Min Hsiao
Shi-Ming Hsiao
Yuan-Chung Kao
Kuan-Lin Kuo
Chih-Yuan Ma
Cheng-Hsiang Kuo
Bi-Ing Chang
Chuan-Fa Chang
Chun-Hung Lin
Chi-Huey Wong
Hua-Lin Wu
National Cheng Kung University · TWInstitute of Biological Chemistry, Academia Sinica · TWGenomics (United Kingdom) · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thrombomodulin (TM), a widely expressing glycoprotein originally identified in vascular endothelium, is an important cofactor in the protein C anticoagulant system. TM appears to exhibit anti-inflammatory ability through both protein C-dependent and -independent pathways. We presently have demonstrated that recombinant N-terminal lectinlike domain of TM (rTMD1) functions as a protective agent against sepsis caused by Gram-negative bacterial infections. rTMD1 caused agglutination of Escherichia coli and Klebsiella pneumoniae and enhanced the macrophage phagocytosis of these Gram-negative bacteria. Moreover, rTMD1 bound to the Klebsiella pneumoniae and lipopolysaccharide (LPS) by specifically interacting with Lewis Y antigen. rTMD1 inhibited LPS-induced inflammatory mediator production via interference with CD14 and LPS binding. Furthermore, rTMD1 modulated LPS-induced mitogen-activated protein kinase and nuclear factor-kappaB signaling pathway activations and inducible nitric oxide synthase expression in macrophages. Administration of rTMD1 protected the host by suppressing inflammatory responses induced by LPS and Gram-negative bacteria, and enhanced LPS and bacterial clearance in sepsis. Thus, rTMD1 can be used to defend against bacterial infection and inhibit LPS-induced inflammatory responses, suggesting that rTMD1 may be valuable in the treatment of severe inflammation in sepsis, especially in Gram-negative bacterial infections.

Indexed as

AnimalsBinding SitesCell LineGram-Negative Bacterial InfectionsHumansInflammationKlebsiella pneumoniaeLewis Blood Group AntigensLigandsLipopolysaccharidesMacrophagesMaleMAP Kinase Signaling SystemMiceNF-kappa BProtein Structure, TertiaryLewis Blood Group AntigensLewis Y antigenLigandsLipopolysaccharidesNF-kappa BRecombinant ProteinsThrombomodulin

Identifiers

PMID18711002
PMCPMC2572793
OpenAlexW2010344521

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.