Prion protein fragment (106-126) activates NLRP3 inflammasome and promotes platelet-monocyte/neutrophil interactions, potentially contributing to an inflammatory state.

ABSTRACT:

Introduction

Prion diseases are neurodegenerative disorders where infectious prion proteins (PrP) featuring an amyloidogenic amino acid sequence, PrP (106-126), accumulate in the brain leading to neuroinflammation while it can also access circulation by breaching the blood-brain barrier. Platelets are highly sensitive cells in blood, which have been widely employed as "peripheral" model for neurons. In addition to their stellar roles in hemostasis and thrombosis, platelets are also known to function as immune cells and possess necessary components of functional inflammasome. This study demonstrates that prion proteins drive inflammasome assembly in platelets and upregulate activity of caspase-1, a critical readout of functional inflammasomes.

Methods

Flow cytometric analysis

SUBMITTER: Verma R 

PROVIDER: S-EPMC11895701 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature