Activation of factor XIII is accompanied by a change in oligomerization state.

ABSTRACT: Factor XIII A (FXIIIA) is a member of the transglutaminase enzyme family that cross-links both intra- and extracellular protein substrates. To prevent undesired cross-linking, FXIIIA is expressed as an inactive zymogen and exists intracellularly as an A₂ homodimer. In plasma, FXIII A₂ is complexed with two protective factor XIII B subunits (A₂ B₂ ) that dissociate upon activation of the zymogen. Based on limited experimental data, activated FXIII was considered a dimer of two catalytically active A subunits. However, accumulating but indirect evidence has suggested activation may lead to a monomeric state instead. In the present study, we employed analytical ultracentrifugation (AUC) to directly explore the oligomerization state of zymogen as wel

SUBMITTER: Anokhin BA 

PROVIDER: S-EPMC6075653 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature