Sulfenylation links oxidative stress to protein disulfide isomerase oxidase activity and thrombus formation.

ABSTRACT:

Background

Oxidative stress contributes to thrombosis in atherosclerosis, inflammation, infection, aging, and malignancy. Oxidant-induced cysteine modifications, including sulfenylation, can act as a redox-sensitive switch that controls protein function. Protein disulfide isomerase (PDI) is a prothrombotic enzyme with exquisitely redox-sensitive active-site cysteines.

Objectives

We hypothesized that PDI is sulfenylated during oxidative stress, contributing to the prothrombotic potential of PDI.

Methods

Biochemical and enzymatic assays using purified proteins, platelet and endothelial cell assays, and in vivo murine thrombosis studies were used to evaluate the role of oxidative stress in PDI sulfenylation and prothrombotic activity.

Results

PDI exposure to oxida

SUBMITTER: Yang M 

PROVIDER: S-EPMC10657653 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature