Identification of cysteine thiol-based linkages in ADAMTS13 in support of a non-proteolytic regulation of von Willebrand factor.

ABSTRACT:

Background

ADAMTS13, a plasma metalloprotease, cleaves von Willebrand factor (VWF) to regulate its function. Additionally, ADAMTS13 is thought to regulate lateral association of VWF multimers to form fibrillar structures through its free thiols.

Objective

The purpose of the present study is to obtain direct evidence for ADAMTS13 to engage in thiol/disulfide exchange reactions.

Methods

Covalent complexes between ADAMTS13 and VWF were determined by agarose gel electrophoresis under nonreducing conditions. Free thiols in ADAMST13 were identified by a reversed phase high-performance liquid chromatography electrospray ionization quadrupole time-of-flight mass spectrometry system.

Results

We demonstrate formation of covalent linkage between ADAMTS13 and VWF, which is

SUBMITTER: Rottensteiner H 

PROVIDER: S-EPMC6916347 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature