Evidence map›Paper›PMID 40492181›Full record

ArticleJournal of lipid and atherosclerosis2025

Investigation of the Influence of Lipoprotein(a) and Oxidized Lipoprotein(a) on Plasminogen Activation and Fibrinolysis.

Matthew Yao, S Kent Dickeson, Karthik Dhanabalan, Sergey Solomevich, Connor Dennewitz, David Gailani, Wen-Liang Song

Erratum issuedAbstract read
In one paragraph

Article in Journal of lipid and atherosclerosis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Matthew YaoCollege of Arts and Sciences, Vanderbilt University, Nashville, TN, USA.ORCID https://orcid.org/0009-0005-0009-4638
S Kent DickesonDepartment of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.ORCID https://orcid.org/0000-0003-2766-4061
Karthik DhanabalanDepartment of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.ORCID https://orcid.org/0000-0002-6619-6363
Sergey SolomevichCardiovascular Research Center, Brown University Health, Providence, RI, USA.ORCID https://orcid.org/0000-0001-9053-4855
Connor DennewitzDepartment of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.ORCID https://orcid.org/0009-0001-2715-6262
David GailaniDepartment of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA.ORCID https://orcid.org/0000-0001-8142-8014
Wen-Liang SongCardiovascular Research Center, Brown University Health, Providence, RI, USA.ORCID https://orcid.org/0000-0002-1866-0635

Funding

Biochemistry and Pathophysiology of Factor XI and Contact ActivationR35HL140025 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI GAILANI, DAVID · 2018 to 2024
$5.5M
Differential thrombogenesis effects of EPA and DHA mediated by HDLR01HL159204 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI WENLIANG SONG · 2023 to 2026
$2.1M
NHLBI NIH HHS R01 HL159204NHLBI NIH HHS R35 HL140025
6 · The paper itself

Abstract

Objective: In the present study, we compare the influence of oxidized lipoprotein(a) [Lp(a)] and unoxidized Lp(a) on plasminogen activation in the process of fibrinolysis and elucidate the potential atherogenic mechanisms of oxidized Lp(a), focusing on its role in thrombosis. Methods: Chromogenic substrate assays were conducted to study the kinetics of plasminogen activation. Fibrin clots were generated by incubating fibrinogen with thrombin, and plasminogen activation was triggered with tissue plasminogen activator (tPA). Experiments were performed in low and high concentrations of Lp(a) or oxidized Lp(a) to evaluate their respective effects on plasmin generation. Oxidized Lp(a) was prepared by chemical oxidation of isolated Lp(a) samples. Results: Low concentrations of Lp(a) enhanced plasminogen activation and fibrinolysis, reflecting its physiological role. However, at higher concentrations, oxidized Lp(a) exhibited a significant inhibitory effect on plasminogen activation. Compared to unoxidized Lp(a), oxidized Lp(a) led to earlier plateauing of plasmin generation and reduced overall plasmin levels. The inhibitory effects of oxidized Lp(a) are likely due to its structural similarity to plasminogen and higher oxidized phospholipid content, which competes with plasminogen for fibrin binding-the enhanced competition with fibrin fragments and tPA by oxidized Lp(a) further impaired fibrinolysis. Conclusion: This study demonstrates that while low levels of Lp(a) may support fibrinolysis, oxidized Lp(a) impairs this process by inhibiting plasminogen activation through structural and functional competition. These findings highlight the atherogenic potential of oxidized Lp(a) and its contribution to thrombotic cardiovascular risk.

Indexed as

FibrinolysisLipoprotein(a)PlasminogenThrombosis

Identifiers

PMID40492181
PMCPMC12145965

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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.