Redox control of β2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1.

ABSTRACT:

Background

 β(2) -Glycoprotein I (β(2) GPI) is an abundant plasma protein that is closely linked to blood clotting, as it interacts with various protein and cellular components of the coagulation system. However, the role of β(2) GPI in thrombus formation is unknown. We have recently shown that β(2) GPI is susceptible to reduction by the thiol oxidoreductases thioredoxin-1 and protein disulfide isomerase, and that reduction of β(2) GPI can take place on the platelet surface.

Methods

 β(2) GPI, reduced by thioredoxin-1, was labeled with the selective sulfhydryl probe N(a)-(3-maleimidylpropionyl)biocytin and subjected to mass spectrometry to identify the specific cysteines involved in the thiol exchange reaction. Binding assays were used to examine the affinity of reduced β(2)

SUBMITTER: Passam FH 

PROVIDER: S-EPMC3017748 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature