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Shotgun analysis of plasma fibrin clot-bound proteins in patients with acute myocardial infarction

ABSTRACT: The presence and amount of the proteins within a plasma clot may influence clot properties, like susceptibility to fibrinolysis, however, the plasma clot proteome has not yet been extensively described. The aim of the study was to investigate the protein composition of clots prepared ex vivo from plasma of the peripheral blood of four patients with acute myocardial infarction (AMI) in two time points: in the acute ischemic phase and two months later during the standard therapy. Proteomic analysis revealed a total number of 62 proteins identified in all 8 samples grouping into several distinct functional clusters (e.g. cholesterol transporter activity, immunoglobulin binding and peptidase regulatory activity). The protein signatures of clots differed significantly depending on time after ACS, showing 30% greater variability in protein composition of the clots prepared in the plasma two months after the onset of AMI as compared to the clots generated at the time of admission to the hospital. Several proteins that could be involved in clot formation and resolution showed an interesting pattern of changes over time. For example α2-antiplasmin, which was robustly present in clots of all patients in acute phase of AMI, was detectable in lower abundance in only 2 clots prepared in plasma taken 8-12 weeks after AMI, whereas serotransferrin can be detected only in the clots prepared from plasma taken later during the therapy. In conclusion, we provided the first qualitative analysis of proteomes of fibrin clots generated ex vivo in plasma taken from patients with AMI showing differences in protein composition between clots generated in the acute ischemic phase and those prepared two months later. It might be hypothesized that differences involving several proteins of potential influence on within-clot fibrinolysis and clot stability may partially explain time-dependent changes in the clots structure and firmness in patients with AMI.

INSTRUMENT(S): Velos Plus

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Blood Plasma

DISEASE(S): Acute Myocardial Infarction

SUBMITTER: Maciej Suski

LAB HEAD: Rafał Olszanecki

PROVIDER: PXD001109 | Pride | 2016-12-08

REPOSITORIES: Pride

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Shotgun analysis of plasma fibrin clot-bound proteins in patients with acute myocardial infarction.

Suski Maciej M Siudut Jakub J Ząbczyk Michał M Korbut Ryszard R Olszanecki Rafał R Undas Anetta A

Thrombosis research 20150210 4

<h4>Introduction</h4>The presence and amount of the proteins within a plasma clot may influence clot properties, like susceptibility to fibrinolysis, however, the clot proteome has not yet been extensively described. The aim of the study was to investigate the protein composition of clots of four patients with acute myocardial infarction (AMI) in two time points: in the acute ischemic phase and two months later during the standard therapy.<h4>Materials and methods</h4>Shotgun proteomic method (2 ...[more]

PMID: 25686879

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Project description:Antiphospholipid syndrome (APS) is associated with arterial and venous thrombosis. The unfavorable fibrin clot phenotype, including formation of dense and poorly lysable clots, has been reported both in thrombotic APS and venous thromboembolism (VTE). The presence and amount of different proteins within a plasma clot, not only associated with the coagulation system, may influence clot properties. To our knowledge, there is a lack of data on plasma fibrin-clot bound proteins in patients with thrombotic APS or VTE. The aim of our study was to perform a quantitative proteomic analysis of fibrin clots prepared from citrated plasma from subjects with thrombotic APS and prior VTE, along with fibrin clot permeability (Ks) and clot lysis time (CLT) assessed ex vivo. We investigated 23 consecutive patients with APS, 18 with a history of first-ever VTE, and 20 age and sex matched healthy subjects. A multiple enzyme digestion filter aided sample preparation and a multienzyme digestion (MED) FASP method combined with LC-MS/MS analysis performed on a Proxeon Easy-nLC System coupled to the Q Exactive HF mass spectrometer were used. The proteomic analysis revealed that clot composition regarding 117 proteins in APS patients and 48 proteins in VTE patients was changed as compared to healthy controls, while 72 clot-bounded proteins differed between APS and VTE subjects. In healthy controls, Ks was associated with fibrinogen alpha and gamma chains (r=0.46 and r=0.46, both p<0.05, respectively) or apolipoprotein B-100 (r=-0.53, p<0.05), while CLT correlated with annexin A2 (r=-0.58, p<0.05), apolipoportein(a) (r=0.47, p<0.05), or platelet glycoprotein 4 (r=0.59, p<0.05). In VTE patients correlations of Ks with complement C1q and histone H2B, as factors closely linked with thrombosis, were observed (r=-0.52 and r=-0.47, both p<0.05, respectively). In patients with thrombotic APS all above-mentioned associations were not found. This study is the first to show that different proteins are able to influence the clot formation, structure, and properties. Since, prothrombotic conditions abolished associations observed in healthy subjects fibrin clots, differences in protein clot components might explain the links between prothrombotic fibrin clot phenotype and thromboembolic events.

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