Cross-linking by tissue transglutaminase-2 alters fibrinogen-directed macrophage proinflammatory activity.

ABSTRACT:

Background

The blood coagulation factor fibrin(ogen) can modulate inflammation by altering leukocyte activity. Analyses of fibrin(ogen)-mediated proinflammatory activity have largely focused on leukocyte integrin binding activity revealed by conversion of fibrinogen to a stabilized fibrin polymer by blood coagulation enzymes. In addition to coagulation enzymes, fibrinogen is a substrate for tissue transglutaminase-2 (TG2), a widely expressed enzyme that produces unique fibrinogen Aα-γ chain cross-linked products.

Objectives

We tested the hypothesis that TG2 dependent cross-linking alters the proinflammatory activity of surface-adhered fibrinogen.

Methods

Mouse bone marrow-derived macrophages (BMDMs) were cultured on tissue culture plates coated with fibrinogen or TG2-

SUBMITTER: Poole LG 

PROVIDER: S-EPMC9035112 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature