Evidence map›Paper›PMID 24478033›Full record

ArticleJournal of lipid research2014

Inhibition of plasminogen activation by apo(a): role of carboxyl-terminal lysines and identification of inhibitory domains in apo(a).

Rocco Romagnuolo, Santica M Marcovina, Michael B Boffa, Marlys L Koschinsky

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of lipid research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

37 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
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  4. The biology of lipoprotein(a): From genetics to molecular mechanisms.European journal of clinical investigation · 2026
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  14. Clot or Not? Reviewing the Reciprocal Regulation Between Lipids and Blood Clotting.Arteriosclerosis, thrombosis, and vascular biology · 2024
    Review
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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

4 authors at 2 institutions in 2 countries.

Rocco RomagnuoloDepartment of Chemistry & Biochemistry, University of Windsor, Windsor, ON, Canada; and.
Santica M Marcovina
Michael B Boffa
Marlys L Koschinsky
University of Windsor · CAUniversity of Washington · US

Funding

Canadian Institutes of Health Research MOP 126076
6 · The paper itself

Abstract

Apo(a), the distinguishing protein component of lipoprotein(a) [Lp(a)], exhibits sequence similarity to plasminogen and can inhibit binding of plasminogen to cell surfaces. Plasmin generated on the surface of vascular cells plays a role in cell migration and proliferation, two of the fibroproliferative inflammatory events that underlie atherosclerosis. The ability of apo(a) to inhibit pericellular plasminogen activation on vascular cells was therefore evaluated. Two isoforms of apo(a), 12K and 17K, were found to significantly decrease tissue-type plasminogen activator-mediated plasminogen activation on human umbilical vein endothelial cells (HUVECs) and THP-1 monocytes and macrophages. Lp(a) purified from human plasma decreased plasminogen activation on THP-1 monocytes and HUVECs but not on THP-1 macrophages. Removal of kringle V or the strong lysine binding site in kringle IV10 completely abolished the inhibitory effect of apo(a). Treatment with carboxypeptidase B to assess the roles of carboxyl-terminal lysines in cellular receptors leads in most cases to decreases in plasminogen activation as well as plasminogen and apo(a) binding; however, inhibition of plasminogen activation by apo(a) was unaffected. Our findings directly demonstrate that apo(a) inhibits pericellular plasminogen activation in all three cell types, although binding of apo(a) to cell-surface receptors containing carboxyl-terminal lysines does not appear to play a major role in the inhibition mechanism.

Indexed as

Apolipoproteins ACells, CulturedHumansHuman Umbilical Vein Endothelial CellsLeukocytes, MononuclearLysineMacrophagesPlasminogenPlasminogen ActivatorsProtein BindingProtein Interaction Domains and MotifsApolipoproteins ALysinePlasminogenPlasminogen Activatorsapolipoprotein(a)atherosclerosiscarboxypeptidase Bfibrinolysislipoprotein(a)thrombin-activatable fibrinolysis inhibitortissue-type plasminogen activator

Identifiers

PMID24478033
PMCPMC3966697
OpenAlexW2084425906

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.