Optimization of quantitative proteomic analysis of clots generated from plasma of patients with venous thromboembolism.

ABSTRACT:

Background

It is well known that fibrin network binds a large variety of proteins, including inhibitors and activators of fibrinolysis, which may affect clot properties, such as stability and susceptibility to fibrinolysis. Specific plasma clot composition differs between individuals and may change in disease states. However, the plasma clot proteome has not yet been in-depth analyzed, mainly due to technical difficulty related to the presence of a highly abundant protein-fibrinogen and fibrin that forms a plasma clot.

Methods

The aim of our study was to optimize quantitative proteomic analysis of fibrin clots prepared ex vivo from citrated plasma of the peripheral blood drawn from patients with prior venous thromboembolism (VTE). We used a multiple enzyme digestion filter a

SUBMITTER: Stachowicz A 

PROVIDER: S-EPMC5706328 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature