Denatured Albumin Gains a Function of Regulating Platelet Activity
Year: 2026
Type: preprint
Abstract: Platelets are blood cells that play a critical role in hemostasis and thrombosis. Serum albumin, which constitutes approximately 50% of plasma proteins, has traditionally been considered non-interactive with platelets and not involved in platelet function. Here, using a molecular force sensor and platelet adhesion and aggregation assays, we show that serum albumin, if denatured, specifically binds to integrin α IIb β 3 in platelets and transmits platelet contractile forces, regulating platelet activation, adhesion and aggregation as effectively as fibrinogen (the clotting factor I). 0.1% ethanol or 10 µM hydrogen peroxide, physiologically attainable in blood through alcohol intake or disease-elevated oxidative stress, are sufficient to denature albumin into a functional platelet ligand. These findings revealed albumin as a previously unrecognized but important regulator of platelet functions, with broad implications for the thrombotic risk in the context of physiological conditions that induce albumin denaturation.
Authors: Vivek Pandey, Subhankar Kundu, Sarah J Wang, Arghajit Pyne, Long Que, Xuefeng Wang
Institutions: University of Cincinnati, Iowa State University
Language: English
Subfield: Hematology
Field: Medicine
Domain: Health Sciences
Open Access status: green
Funder: National Science Foundation
OpenAlex ID: W7147164142