Evidence map›Paper›PMID 17544816›Full record

ReviewImmunobiology2007

C1 inhibitor: biologic activities that are independent of protease inhibition.

Alvin E Davis, Shenghe Cai, Dongxu Liu

Open access · greenAbstract readReview
In one paragraph

Review in Immunobiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 57 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Therapeutic Potential of C1-Inhibitor in Vascular Diseases and Beyond.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Growth factors and IL-17 in hereditary angioedema.Clinical and experimental medicine · 2016
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

Alvin E DavisCBR Institute for Biomedical Research, Harvard Medical School, 800 Huntington Avenue, Boston, MA 02114, USA. aldavis@cbrinstitute.org
Shenghe Cai
Dongxu Liu
Harvard University · USBoston Biomedical Research Institute · US

Funding

C1 INHIBITOR GENE AND HEREDITARY ANGIONEUROTIC EDEMAR37HD022082 · NICHD · IMMUNE DISEASE INSTITUTE, INC. · PI DAVIS, ALVIN E · 1999 to 2008
$3.9M
C1 INHIBITOR-MEDIATED PROTECTION FROM ENDOTOXIN SHOCKR01AI057366 · NIAID · IMMUNE DISEASE INSTITUTE, INC. · PI DAVIS, ALVIN E · 2005 to 2009
$2.3M
NIAID NIH HHS R01 AI057366NICHD NIH HHS R37 HD022082
6 · The paper itself

Abstract

C1 inhibitor therapy improves outcome in several animal models of inflammatory disease. These include sepsis and Gram negative endotoxin shock, vascular leak syndromes, hyperacute transplant rejection, and ischemia-reperfusion injury. Furthermore, some data suggest a beneficial effect in human inflammatory disease. In many inflammatory conditions, complement system activation plays a role in pathogenesis. The contact system also very likely is involved in mediation of damage in inflammatory disease. Therefore, the beneficial effect of C1 inhibitor has been assumed to result from inhibition of one or both of these systems. Over the past several years, several other potential anti-inflammatory effects of C1 inhibitor have been described. These effects do not appear to require protease inhibition and depend on non-covalent interactions with other proteins, cell surfaces or lipids. In the first, C1 inhibitor binds to a variety of extracellular matrix components including type IV collagen, laminin, entactin and fibrinogen. The biologic role of these reactions is unclear, but they may serve to concentrate C1 inhibitor at extravascular inflammatory sites. The second is a non-covalent interaction with C3b that results in inhibition of formation of the alternative pathway C3 convertase, a function analogous to that of factor H. The third is an interaction with E and P selectins on endothelial cells that is mediated by the Lewis(x) tetrasaccharides that are expressed on C1 inhibitor. These interactions result in suppression of leukocyte rolling and transmigration. The fourth interaction is the binding of C1 inhibitor to Gram negative bacterial endotoxin that results in suppression of endotoxin shock by interference with the interaction of endotoxin with its receptor complex on macrophages. Lastly, C1 inhibitor binds directly to Gram negative bacteria, which leads to suppression of the development of sepsis, as demonstrated in the cecal ligation and puncture model. These observations suggest that C1 inhibitor is a multi-faceted anti-inflammatory protein that exerts its effects through a variety of mechanisms including both protease inhibition and several different non-covalent interactions that are unrelated to protease inhibition.

Indexed as

AnimalsComplement ActivationComplement C1 Inhibitor ProteinEndopeptidasesEndotoxinsExtracellular MatrixHumansProtein BindingComplement C1 Inhibitor ProteinEndopeptidasesEndotoxins

Identifiers

PMID17544816
PMCPMC2680681
OpenAlexW1967358462

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.