Evidence map›Paper›PMID 22187433›Full record

ArticleThe Journal of biological chemistry2012

A high affinity interaction of plasminogen with fibrin is not essential for efficient activation by tissue-type plasminogen activator.

Paul Y Kim, Long D Tieu, Alan R Stafford, James C Fredenburgh, Jeffrey I Weitz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 12% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 47 citations in OpenAlex.

  1. Guideline
  2. A novel biosensor for measuring plasmin activity.Research and practice in thrombosis and haemostasis · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Protofibril packing density of individual fibers alters fibrinolysis.Research and practice in thrombosis and haemostasis · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Thrombus composition and thrombolysis resistance in stroke.Research and practice in thrombosis and haemostasis · 2023
    Article
  12. Review
  13. Fibrinolysis: an illustrated review.Research and practice in thrombosis and haemostasis · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Thrombin and plasmin generation in patients with plasminogen or plasminogen activator inhibitor type 1 deficiency.Haemophilia : the official journal of the World Federation of Hemophilia · 2019
    Article
  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

5 authors at 1 institution in 1 country.

Paul Y KimDepartments of Medicine and Biochemistry and Biomedical Sciences, McMaster University and Thrombosis and Atherosclerosis Research Institute, Hamilton, Ontario L8L 2X2, Canada.
Long D Tieu
Alan R Stafford
James C Fredenburgh
Jeffrey I Weitz
Thrombosis and Atherosclerosis Research Institute · CA

Funding

Medical Research Council
6 · The paper itself

Abstract

Fibrin (Fn) enhances plasminogen (Pg) activation by tissue-type plasminogen activator (tPA) by serving as a template onto which Pg and tPA assemble. To explore the contribution of the Pg/Fn interaction to Fn cofactor activity, Pg variants were generated and their affinities for Fn were determined using surface plasmon resonance (SPR). Glu-Pg, Lys-Pg (des(1-77)), and Mini-Pg (lacking kringles 1-4) bound Fn with K(d) values of 3.1, 0.21, and 24.5 μm, respectively, whereas Micro-Pg (lacking all kringles) did not bind. The kinetics of activation of the Pg variants by tPA were then examined in the absence or presence of Fn. Whereas Fn had no effect on Micro-Pg activation, the catalytic efficiencies of Glu-Pg, Lys-Pg, and Mini-Pg activation in the presence of Fn were 300- to 600-fold higher than in its absence. The retention of Fn cofactor activity with Mini-Pg, which has low affinity for Fn, suggests that Mini-Pg binds the tPA-Fn complex more tightly than tPA alone. To explore this possibility, SPR was used to examine the interaction of Mini-Pg with Fn in the absence or presence of tPA. There was 50% more Mini-Pg binding to Fn in the presence of tPA than in its absence, suggesting that formation of the tPA-Fn complex exposes a cryptic site that binds Mini-Pg. Thus, our data (a) indicate that high affinity binding of Pg to Fn is not essential for Fn cofactor activity, and (b) suggest that kringle 5 localizes and stabilizes Pg within the tPA-Fn complex and contributes to its efficient activation.

Indexed as

Enzyme ActivationEnzyme StabilityFibrinHumansKringlesPlasminogenProtein BindingSurface Plasmon ResonanceTissue Plasminogen ActivatorFibrinPlasminogenTissue Plasminogen Activator

Identifiers

PMID22187433
PMCPMC3281636
OpenAlexW2001821674

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.