Evidence map›Paper›PMID 32842150›Full record

ArticleBlood2021

Exposure of plasminogen and a novel plasminogen receptor, Plg-RKT, on activated human and murine platelets.

Claire S Whyte, Gael B Morrow, Nagyung Baik, Nuala A Booth, Mohammed M Jalal, Robert J Parmer, Lindsey A Miles, Nicola J Mutch

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2021. 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
1.6field-weighted citation impact, top 14% 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, 21 citations in OpenAlex.

  1. Plg-RMolecular medicine (Cambridge, Mass.) · 2026
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  13. Assessing Plasmin Generation in Health and Disease.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Plasminogen Receptors and Fibrinolysis.International journal of molecular sciences · 2021
    Review
  16. Article
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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

8 authors at 3 institutions in 3 countries.

Claire S WhyteAberdeen Cardiovascular & Diabetes Centre, School of Medicine, Medical Sciences and Nutrition, Institute of Medical Sciences, University of Aberdeen, Aberdeen, United Kingdom.
Gael B MorrowAberdeen Cardiovascular & Diabetes Centre, School of Medicine, Medical Sciences and Nutrition, Institute of Medical Sciences, University of Aberdeen, Aberdeen, United Kingdom.
Nagyung BaikDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA.
Nuala A BoothAberdeen Cardiovascular & Diabetes Centre, School of Medicine, Medical Sciences and Nutrition, Institute of Medical Sciences, University of Aberdeen, Aberdeen, United Kingdom.
Mohammed M JalalAberdeen Cardiovascular & Diabetes Centre, School of Medicine, Medical Sciences and Nutrition, Institute of Medical Sciences, University of Aberdeen, Aberdeen, United Kingdom.
Robert J ParmerDepartment of Medical Laboratory Technology, Faculty of Applied Medical Sciences, University of Tabuk, Tabuk, Saudi Arabia.
Lindsey A MilesDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA.
Nicola J MutchAberdeen Cardiovascular & Diabetes Centre, School of Medicine, Medical Sciences and Nutrition, Institute of Medical Sciences, University of Aberdeen, Aberdeen, United Kingdom.
University of Aberdeen · GBScripps Research Institute · USUniversity of California San Diego · US

Funding

Regulation of plasminogen-dependent cell functions by the novel receptor, Plg-RKTR01HL081046 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI MILES, LINDSEY A · 2007 to 2024
$8.7M
A Novel Plasminogen Receptor Promotes Adipose Function and Metabolic HomeostasisR01HL149511 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI MILES, LINDSEY A, PARMER, ROBERT J · 2019 to 2022
$3.0M
Regulation of Renal Injury and Fibrosis by the Plasminogen Receptor, Plg-RKTI01BX003933 · VA · VA SAN DIEGO HEALTHCARE SYSTEM · PI PARMER, ROBERT J · 2018 to 2021
–
BLRD VA I01 BX003933British Heart Foundation FS/11/2/28579British Heart Foundation PG/15/82/31721British Heart Foundation PG/20/17/35050NHLBI NIH HHS R01 HL081046NHLBI NIH HHS R01 HL149511
6 · The paper itself

Abstract

Plasminogen activation rates are enhanced by cell surface binding. We previously demonstrated that exogenous plasminogen binds to phosphatidylserine-exposing and spread platelets. Platelets contain plasminogen in their α-granules, but secretion of plasminogen from platelets has not been studied. Recently, a novel transmembrane lysine-dependent plasminogen receptor, Plg-RKT, has been described on macrophages. Here, we analyzed the pool of plasminogen in platelets and examined whether platelets express Plg-RKT. Plasminogen content of the supernatant of resting and collagen/thrombin-stimulated platelets was similar. Pretreatment with the lysine analog, ε-aminocaproic acid, significantly increased platelet-derived plasminogen (0.33 vs 0.08 nmol/108 platelets) in the stimulated supernatant, indicating a lysine-dependent mechanism of membrane retention. Lysine-dependent, platelet-derived plasminogen retention on thrombin and convulxin activated human platelets was confirmed by flow cytometry. Platelets initiated fibrinolytic activity in fluorescently labeled plasminogen-deficient clots and in turbidimetric clot lysis assays. A 17-kDa band, consistent with Plg-RKT, was detected in the platelet membrane fraction by western blotting. Confocal microscopy of stimulated platelets revealed Plg-RKT colocalized with platelet-derived plasminogen on the activated platelet membrane. Plasminogen exposure was significantly attenuated in thrombin- and convulxin-stimulated platelets from Plg-RKT-/- mice compared with Plg-RKT+/+ littermates. Membrane exposure of Plg-RKT was not dependent on plasminogen, as similar levels of the receptor were detected in plasminogen-/- platelets. These data highlight Plg-RKT as a novel plasminogen receptor in human and murine platelets. We show for the first time that platelet-derived plasminogen is retained on the activated platelet membrane and drives local fibrinolysis by enhancing cell surface-mediated plasminogen activation.

Indexed as

AnimalsBlood PlateletsHumansMicePlasminogenPlatelet ActivationReceptors, Cell SurfacePlasminogenPLGRKT protein, humanPLG-R(KT) protein, mouseReceptors, Cell Surface

Identifiers

PMID32842150
PMCPMC7820873
OpenAlexW3080628439

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.