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脂多糖结合蛋白 (LBP) 可逆转帕金森病中观察到或诱导的纤维蛋白的淀粉样状态。

Lipopolysaccharide-binding protein (LBP) can reverse the amyloid state of fibrin seen or induced in Parkinson's disease.

机构信息

Department of Physiological Sciences, Faculty of Science, Stellenbosch University, Stellenbosch, South Africa.

Department of Physiology, Faculty of Health Sciences, University of Pretoria, Arcadia, South Africa.

出版信息

PLoS One. 2018 Mar 1;13(3):e0192121. doi: 10.1371/journal.pone.0192121. eCollection 2018.

DOI:10.1371/journal.pone.0192121
PMID:29494603
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5832207/
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.

摘要

纤维蛋白原在凝血酶的诱导下聚合形成纤维蛋白,这是血液凝固的晚期阶段。众所周知,帕金森病(PD)伴随着凝血功能紊乱,但作为一种凝血障碍,它的知名度较低。在最近的研究中,我们发现健康个体中存在少量细菌脂多糖(LPS),可能导致血栓形成淀粉样纤维,这可以通过扫描电子显微镜(SEM)或通过硫黄素-T 的荧光来观察。预先加入脂多糖结合蛋白(LBP)可以预防这种情况。我们还通过 SEM 观察到帕金森病患者血液中的这种异常凝血。我们假设,在 PD 背景下,LBP 也可以预防这种情况。这进一步证明了炎症性微生物细胞壁产物伴随着这种疾病,可能是其发病机制的一部分。这可能会为 PD 设计针对微生物及其产物的新型治疗策略提供依据。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/375466d02f5c/pone.0192121.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/e18aee7f410f/pone.0192121.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/ee2b212438bd/pone.0192121.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/04096131c9fd/pone.0192121.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/375466d02f5c/pone.0192121.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/e18aee7f410f/pone.0192121.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/ee2b212438bd/pone.0192121.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/04096131c9fd/pone.0192121.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/4bd3/5832207/375466d02f5c/pone.0192121.g004.jpg

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