Role of calcium in the conformational dynamics of factor XIII activation examined by hydrogen-deuterium exchange coupled with MALDI-TOF MS.

ABSTRACT: Factor XIII catalyzes formation of γ-glutamyl-ε-lysyl crosslinks within fibrin clots. FXIII A(2) can be activated proteolytically with thrombin and low mM Ca(2+) or nonproteolytically with high monovalent/divalent cations along with low mM Ca(2+). Physiologically, FXIII A(2) is poised to respond to transient influxes of Ca(2+) in a Na(+) containing environment. A successful strategy to monitor FXIII conformational events is hydrogen-deuterium exchange (HDX) coupled with mass spectrometry. FXIII A(2) was examined in the presence of different cations (Ca(2+), Mg(2+), Ba(2+), Cu(2+), Na(+), TMAC(+), and EDA(2+)) ranging from 1 to 2mM, physiological Ca(2+) concentration, to 50-500mM for nonproteolytic activation. Increases in FXIII solvent exposure could already be observed at 1mM Ca(2+) for t

SUBMITTER: Woofter RT 

PROVIDER: S-EPMC3645313 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature