ArticleJournal of thrombosis and thrombolysis2025
Proteomics of arterial thrombi in acute limb ischemia.
Article in Journal of thrombosis and thrombolysis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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.
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.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Acute limb ischemia (ALI) is characterized by a sudden decrease in limb perfusion due to arterial occlusion. Without urgent revascularization, patients are at risk of ischemic damage and amputation. This study uses novel proteomic techniques to investigate the molecular architecture of ALI thrombi, identifying key proteins that may influence coagulation dynamics and fibrinolysis resistance. Arterial thromboemboli (n = 12) collected after revascularization procedures were analyzed and compared to in vitro clots (n = 10) generated from healthy donor blood via tissue factor‒induced coagulation. Proteins were identified and quantified via liquid chromatography‒mass spectrometry (LC-MS/MS). A comprehensive literature review of the most abundant proteins allowed for categorization based on their functional roles in fibrinolysis, red blood cell (RBC) degradation, complement activation, and platelet activation. Compared to in vitro clots, ALI clots contained 141 proteins with significantly increased abundance (fold change) and 38 with decreased abundance (p < 0.05). These include 17 fibrinolysis regulators, 8 RBC-related proteins, 6 complement proteins, and 36 platelet regulators. The antifibrinolytic protein vitronectin (VTN) was strikingly enriched (1067-fold), suggesting a substantial role in fibrinolysis resistance and clot stability. Scavengers of heme/hemoglobin, thromboinflammatory complement proteins, and platelet activators were highly abundant. This proof-of-concept study introduces novel proteomic methods for arterial thrombus analysis and identifies key proteins involved in ALI pathology. Our findings reveal a delicate balance between antifibrinolytic and profibrinolytic proteins, offering potential therapeutic targets to enhance thrombolysis and improve ALI management.
Indexed as
Identifiers
40544393What OpenQuestion holds
Registered trials
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.