Angiopoietin-2 binds to multiple interactive sites within von Willebrand factor.

ABSTRACT:

Background

Biosynthesis of von Willebrand factor (VWF) in endothelial cells drives the formation of storage-organelles known as Weibel-Palade bodies (WPBs). WPBs also contain several other proteins, including angiopoietin-2 (Ang-2).

Objectives

At present, the molecular basis of the VWF-Ang-2 interaction is poorly understood. Here, we used immunosorbent-binding assays and specific recombinant VWF fragments to analyze VWF-Ang-2 interactions.

Results

We found that VWF bound to immobilized Ang-2 most efficiently (half-maximal binding at 0.5 ± 0.1 μg/mL) under conditions of high CaCl₂ (10 mM) and slightly acidic pH (6.4-7.0). Interestingly, several isolated recombinant VWF domains (A1/Fc, A2/Fc, D4/Fc, and D'D3-HPC4) displayed dose-dependent binding to immobiliz

SUBMITTER: Texier A 

PROVIDER: S-EPMC10579536 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature