Evidence map›Paper›PMID 12071855›Full record

ArticleThe Biochemical journal2002

Ferritin binds to light chain of human H-kininogen and inhibits kallikrein-mediated bradykinin release.

Narayanan Parthasarathy, Suzy V Torti, Frank M Torti

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

17 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Increased serum ferritin and interleukin-18 levels in children with dengue.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2019
    Article
  9. Emerging and Dynamic Biomedical Uses of Ferritin.Pharmaceuticals (Basel, Switzerland) · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Serum ferritin: Past, present and future.Biochimica et biophysica acta · 2010
    Review
  16. Ferritin for the clinician.Blood reviews · 2009
    Review
  17. Regulatory effects of ferritin on angiogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2009
    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 1 institution in 1 country.

Narayanan ParthasarathyDepartment of Cancer Biology, Wake Forest University School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157, USA.
Suzy V Torti
Frank M Torti
Wake Forest University · US

Funding

Tumor Tissue CoreP30CA012197 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI Ruben A. Mesa · 1985 to 2026
$55.4M
Ferritin, Iron Homeostasis and Cellular StressR37DK042412 · NIDDK · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI TORTI, FRANK M. · 2001 to 2011
$3.8M
TUMOR NECROSIS FACTOR AND IRON METABOLISMR01DK042412 · NIDDK · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI TORTI, FRANK M · 1989 to 2000
$204k
NCI NIH HHS CA12197NIDDK NIH HHS DK-42412
6 · The paper itself

Abstract

Ferritin is an iron-storage protein that exists in both intracellular and extracellular compartments. We have previously identified H-kininogen (high-molecular-weight kininogen) as a ferritin-binding protein [Torti and Torti (1998) J. Biol. Chem. 273, 13630-13635]. H-Kininogen is a precursor of the potent pro-inflammatory peptide bradykinin, which is released from H-kininogen following cleavage of H-kininogen by the serine protease kallikrein. In this report, we demonstrate that binding of ferritin to H-kininogen occurs via the modified light chain of H-kininogen, and that ferritin binds preferentially to activated H-kininogen. We further demonstrate that binding of ferritin to H-kininogen retards the proteolytic cleavage of H-kininogen by kallikrein and its subsequent release of bradykinin from H-kininogen. Ferritin does not interfere with the ability of kallikrein to digest a synthetic substrate, suggesting that ferritin specifically impedes the ability of kallikrein to digest H-kininogen, perhaps by steric hindrance. Based on these results, we propose a model of sequential H-kininogen cleavage and ferritin binding. These results are consistent with the hypothesis that the binding of ferritin to H-kininogen may serve to modulate bradykinin release.

Indexed as

BradykininFerritinsHumansIn Vitro TechniquesKallikreinsKininogen, High-Molecular-WeightModels, BiologicalProtein BindingBradykininFerritinsKallikreinsKininogen, High-Molecular-Weight

Identifiers

PMID12071855
PMCPMC1222672
OpenAlexW2057138726

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.