Lipopolysaccharide-binding protein (LBP) can reverse the amyloid state of fibrin seen or induced in Parkinson's disease
Loading...
Date
Authors
Pretorius, Etheresia
Page, Martin J.
Mbotwe, Sthembile
Kell, Douglas B.
Journal Title
Journal ISSN
Volume Title
Publisher
Public Library of Science
Abstract
The thrombin-induced polymerisation of fibrinogen to form fibrin is well established as a late
stage of blood clotting. It is known that Parkinson's Disease (PD) is accompanied by dysregulation
in blood clotting, but it is less widely known as a coagulopathy. In recent work, we
showed that the presence of tiny amounts of bacterial lipopolysaccharide (LPS) in healthy individuals
could cause clots to adopt an amyloid form, and this could be observed via scanning
electron microscopy (SEM) or via the fluorescence of thioflavin-T. This could be prevented by
the prior addition of lipopolysaccharide-binding protein (LBP). We had also observed by SEM
this unusual clotting in the blood of patients with Parkinson's Disease. We hypothesised, and
here show, that this too can be prevented by LBP in the context of PD. This adds further evidence
implicating inflammatory microbial cell wall products as an accompaniment to the disease,
and may be part of its aetiology. This may lead to novel treatment strategies in PD
designed to target microbes and their products.
Description
Keywords
Fibrin, Coagulopathy, Lipopolysaccharide-binding protein (LBP), Parkinson’s disease (PD), Lipopolysaccharide (LPS), Scanning electron microscopy (SEM)
Sustainable Development Goals
Citation
Pretorius E, Page MJ, Mbotwe S, Kell DB
(2018) Lipopolysaccharide-binding protein (LBP)
can reverse the amyloid state of fibrin seen or
induced in Parkinson's disease. PLoS ONE 13(3):
e0192121. https://DOI.org/10.1371/journal.pone.0192121.