Citrullinated fibrinogen forms densely packed clots with decreased permeability.

ABSTRACT:

Background

Fibrin, the main scaffold of thrombi, is susceptible to citrullination by PAD (peptidyl arginine deiminase) 4, secreted from neutrophils during the formation of neutrophil extracellular traps. Citrullinated fibrinogen (citFg) has been detected in human plasma as well as in murine venous thrombi, and it decreases the lysability and mechanical resistance of fibrin clots.

Objective

To investigate the effect of fibrinogen citrullination on the structure of fibrin clots.

Methods

Fibrinogen was citrullinated with PAD4 and clotted with thrombin. Scanning electron microscopy (SEM) and atomic force microscopy (AFM) were used to measure fiber thickness, fiber height/width ratio, and fiber persistence length in clots containing citFg. Fiber density was measured with l

SUBMITTER: Varju I 

PROVIDER: S-EPMC9828116 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature