Evidence map›Paper›PMID 29779246›Full record

ReviewJournal of thrombosis and haemostasis : JTH2018

Regulation of plasminogen activation on cell surfaces and fibrin.

T Urano, F J Castellino, Y Suzuki

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of thrombosis and haemostasis : JTH, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
10.6field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 132 citations in OpenAlex.

  1. Guideline
  2. Article
  3. Article
  4. Review
  5. Plg-RMolecular medicine (Cambridge, Mass.) · 2026
    Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Profibrinolytic Factors and Cancer Progression, Metastasis, and Survival.Arteriosclerosis, thrombosis, and vascular biology · 2025
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

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

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.

T UranoDepartment of Medical Physiology, Hamamatsu University School of Medicine, Hamamatsu, Japan.
F J CastellinoW.M. Keck Center for Transgene Research, University of Notre Dame, University of Notre Dame, Notre Dame, IN, USA.
Y SuzukiDepartment of Medical Physiology, Hamamatsu University School of Medicine, Hamamatsu, Japan.
Hamamatsu University School of Medicine · JPUniversity of Notre Dame · US

Funding

STRUCTURE-FUNCTION STUDIES ON PLASMINOGEN AND PLASMINR01HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J, LEE, SHAUN · 1985 to 2021
$7.9M
Plasminogen and Plasmin: Structure and FunctionR56HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J, LEE, SHAUN · 2022 to 2022
$743k
STRUCTURE/FUNCTION STUDIES ON PLASMINOGEN AND PLASMINR37HL013423 · NHLBI · UNIVERSITY OF NOTRE DAME · PI CASTELLINO, FRANCIS J · 1990 to 1999
–
NHLBI NIH HHS R01 HL013423NHLBI NIH HHS R37 HL013423NHLBI NIH HHS R56 HL013423
6 · The paper itself

Abstract

The fibrinolytic system dissolves fibrin and maintains vascular patency. Recent advances in imaging analyses allowed visualization of the spatiotemporal regulatory mechanism of fibrinolysis, as well as its regulation by other plasma hemostasis cofactors. Vascular endothelial cells (VECs) retain tissue-type plasminogen activator (tPA) after secretion and maintain high plasminogen (plg) activation potential on their surfaces. As in plasma, the serpin, plasminogen activator inhibitor type 1 (PAI-1), regulates fibrinolytic potential via inhibition of the VEC surface-bound plg activator, tPA. Once fibrin is formed, plg activation by tPA is initiated and effectively amplified on the surface of fibrin, and fibrin is rapidly degraded. The specific binding of plg and tPA to lytic edges of partly degraded fibrin via newly generated C-terminal lysine residues, which amplifies fibrin digestion, is a central aspect of this pathophysiological mechanism. Thrombomodulin (TM) plays a role in the attenuation of plg binding on fibrin and the associated fibrinolysis, which is reversed by a carboxypeptidase B inhibitor. This suggests that the plasma procarboxypeptidase B, thrombin-activatable fibrinolysis inhibitor (TAFI), which is activated by thrombin bound to TM on VECs, is a critical aspect of the regulation of plg activation on VECs and subsequent fibrinolysis. Platelets also contain PAI-1, TAFI, TM, and the fibrin cross-linking enzyme, factor (F) XIIIa, and either secrete or expose these agents upon activation in order to regulate fibrinolysis. In this review, the native machinery of plg activation and fibrinolysis, as well as their spatiotemporal regulatory mechanisms, as revealed by imaging analyses, are discussed.

Indexed as

fibrinolysisplasminogenplasminogen inactivatorsthrombin-activatable fibrinolysis inhibitortissue-type plasminogen activator

Identifiers

PMID29779246
PMCPMC6099326
OpenAlexW2803278784

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.