Glycated albumin modulates the contact system with implications for the kallikrein-kinin and intrinsic coagulation systems.

ABSTRACT:

Background

Human serum albumin (HSA) is the most abundant plasma protein and is sensitive to glycation in vivo. The chronic hyperglycemic conditions in patients with diabetes mellitus (DM) induce a nonenzymatic Maillard reaction that denatures plasma proteins and forms advanced glycation end products (AGEs). HSA-AGE is a prevalent misfolded protein in patients with DM and is associated with factor XII activation and downstream proinflammatory kallikrein-kinin system activity without any associated procoagulant activity of the intrinsic pathway.

Objectives

This study aimed to determine the relevance of HSA-AGE toward diabetic pathophysiology.

Methods

The plasma obtained from patients with DM and euglycemic volunteers was probed for activation of FXII, prekallikrein (PK

SUBMITTER: Hardy LJ 

PROVIDER: S-EPMC10242648 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature