ISSN:
1573-4919
Keywords:
transglutaminase
;
factor XIII
;
fibrinogen
;
fibrin
;
fibronectin
;
binding
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Abstract The affinities of Factor XIII (FXIII), Factor XIIIa (FXIIla), and cellular transglutaminase (Tg) for fibrinogen (Fgn), fibrin (Fbn), and fibronectin (Fn) were compared using a solid-phase binding assay. Initial rates of binding were as follows: FXIII bound Fbn 3-fold more than Fgn. FXIII did not bind Fn till 20 min. Increasing the ligands concentrations and binding time, resulted in weak binding of FXIII to Fn. FXIIla bound Fbn 2-fold more than Fgn and 28-fold more than Fn. Tg bound Fn ∼ 130-fold more than either Fgn or Fbn. At equilibrium, the extent of binding was determined to be as follows: FXIII bound Fbn 3–15-fold more than Fgn and 8-fold more than Fn. FXIIIa bound Fgn and Fbn equally and 12–25-fold more than Fn. FXIIla bound Fgn or Fbn 2-fold and 25-fold greater than FXIII-Fbn and FXIII-Fgn interactions, respectively. Tg bound about equally to Fgn and Fbn and 10–20-fold less than Fn. The K d s′ for FXIIla binding to Fn, Fgn, and Fbn were 100, 23, and 19 nM, respectively. The K d for Tg binding to Fn was 6.5 nM. The binding hierarchies are: [Tg-Fn]〉[FXIIIa-Fgn]=[FXIIIa-Fbn]〉[FXIII-Fbn]〉[FXIIIFgn]=[FXIIIa-Fn]〉[Tg-Fbn]=[Tg-Fgn]〉[FXIII-Fn]. Such hierarchies could regulate the cross-linkings by FXIIIa and Tg during hemostasis, wound healing, and cell adhesion.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00250994
Permalink
