Evidence map›Paper›PMID 18258845›Full record

ArticleThe American journal of pathology2008

Impaired luminal processing of human defensin-5 in Crohn's disease: persistence in a complex with chymotrypsinogen and trypsin.

David Elphick, Susan Liddell, Yashwant R Mahida

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.0field-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

29 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Functional characterization of novel anti-DEFA5 monoclonal antibody clones 1A8 and 4F5 in inflammatory bowel disease colitis tissues.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025
    Article
  3. Article
  4. Human Defensin 5 InhibitsTropical medicine and infectious disease · 2024
    Article
  5. The epithelium takes the stage in asthma and inflammatory bowel diseases.Frontiers in cell and developmental biology · 2024
    Review
  6. Review
  7. Article
  8. Bacterial Translocation as Inflammatory Driver in Crohn's Disease.Frontiers in cell and developmental biology · 2021
    Review
  9. Article
  10. Article
  11. Review
  12. Frontiers in immunology · 2019
    Article
  13. Review
  14. Review
  15. Pro-inflammatory and pro-apoptotic properties of Human Defensin 5.Biochemical and biophysical research communications · 2013
    Article
  16. Inflammatory bowel disease: an impaired barrier disease.Langenbeck's archives of surgery · 2013
    Review
  17. Antimicrobial peptides and colitis.Current pharmaceutical design · 2013
    Review
  18. Article
  19. Enteric alpha defensins in norm and pathology.Annals of clinical microbiology and antimicrobials · 2012
    Review
  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

3 authors at 2 institutions in 2 countries.

David ElphickInstitute of Infection, Immunity, and Inflammation, University of Nottingham, Nottingham, UK.
Susan Liddell
Yashwant R Mahida
University of Nottingham · GBBD Biosciences (United States) · US

Funding

Medical Research Council G0100577Medical Research Council G0500067
6 · The paper itself

Abstract

Human defensin (HD)-5 is an antimicrobial peptide expressed in small intestinal Paneth cells, and alterations in HD-5 expression may be important in Crohn's disease (CD) pathogenesis. Levels of HD-5 in Paneth cells and ileostomy fluid from control and CD patients were studied by quantitative immunodot analysis, immunohistochemistry, acid urea-polyacrylamide gel electrophoresis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis Western blotting, reverse phase-high performance liquid chromatography, N-terminal amino acid sequencing, and ES-QToF mass spectrometry. In both control and CD patients, HD-5 in Paneth cell extracts was present almost exclusively in the precursor form. HD-5 levels in ileostomy fluid were lower in CD patients (n = 51) than in controls (n = 20): median (range), 7.9 (5.5 to 35.0) microg/ml versus 10.5 (6.0 to 30.4) microg/ml; P = 0.05; this difference was most marked in CD patients with homozygous/compound heterozygous mutations in NOD2 (P = 0.03). In control ileostomy fluid, HD-5 was present in the mature form only. In contrast, CD patient ileostomy fluid contained both precursor and mature forms of HD-5, with the majority present in a complex with trypsin, chymotrypsinogen/chymotrypsin, and alpha1-anti-trypsin. Pro-HD-5 was not associated with trypsin or chymotrypsinogen in Paneth cell extracts. In conclusion, pro-HD-5 in the intestinal lumen is processed by trypsin in a complex in which chymotrypsinogen is also cleaved for activation. The persistence of this complex in CD may be attributable to increased luminal levels of proteinase inhibitors such as alpha1-anti-trypsin.

Indexed as

Protein Processing, Post-TranslationalAdultalpha 1-Antitrypsinalpha-DefensinsAmino Acid SequenceBody FluidsCase-Control StudiesChromatography, High Pressure LiquidChymotrypsinogenCrohn DiseaseDefensinsFemaleHumansIleostomyIntestinal MucosaIntestine, Smallalpha 1-Antitrypsinalpha-DefensinsChymotrypsinogenDEFA5 protein, humanDefensinsMultiprotein ComplexesProtein PrecursorsTissue ExtractsTrypsin

Identifiers

PMID18258845
PMCPMC2258249
OpenAlexW1568874426

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.