Scholars@Duke
Arpine Leblanc

Scholarly Works

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.

Journal article Sci Adv · November 2024 The intricate process of α-synuclein aggregation and fibrillization holds pivotal roles in Parkinson's disease (PD) and multiple system atrophy (MSA). While mouse α-synuclein can fibrillize in vitro, whether these fibrils commonly used in research to induc ... Full text Link to item Cite

Gut mucosal cells transfer α-synuclein to the vagus nerve.

Journal article JCI Insight · December 8, 2023 Epidemiological and histopathological findings have raised the possibility that misfolded α-synuclein protein might spread from the gut to the brain and increase the risk of Parkinson's disease. Although past experimental studies in mouse models have relie ... Full text Link to item Cite

Anionic nanoplastic contaminants promote Parkinson's disease-associated α-synuclein aggregation.

Journal article Sci Adv · November 15, 2023 Recent studies have identified increasing levels of nanoplastic pollution in the environment. Here, we find that anionic nanoplastic contaminants potently precipitate the formation and propagation of α-synuclein protein fibrils through a high-affinity inte ... Full text Link to item Cite

Repetitive mild TBI causes pTau aggregation in nigra without altering preexisting fibril induced Parkinson's-like pathology burden.

Journal article Acta Neuropathol Commun · November 26, 2022 Population studies have shown that traumatic brain injury (TBI) is associated with an increased risk for Parkinson's disease (PD) and among U.S. Veterans with a history of TBI this risk is 56% higher. The most common type of TBI is mild (mTBI) and often oc ... Full text Link to item Cite

Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain.

Journal article Mol Neurodegener · January 10, 2022 BACKGROUND: Leucine rich repeat kinase 2 (LRRK2) and SNCA are genetically linked to late-onset Parkinson's disease (PD). Aggregated α-synuclein pathologically defines PD. Recent studies identified elevated LRRK2 expression in pro-inflammatory CD16+ monocyt ... Full text Link to item Cite

Evaluation of ABT-888 in the amelioration of α-synuclein fibril-induced neurodegeneration.

Journal article Brain Commun · 2022 The accumulation of α-synuclein inclusions in vulnerable neuronal populations pathologically defines Lewy body diseases including Parkinson's disease. Recent pre-clinical studies suggest poly(ADP-ribose) polymerase-1 activation and the subsequent generatio ... Full text Link to item Cite

Structural and functional landscape of α-synuclein fibril conformations amplified from cerebrospinal fluid

Preprint · 2022 Lewy body dementias are pathologically defined by the deposition of α-synuclein fibrils into inclusions throughout the brain. Cerebrospinal fluid(CSF) in disease harbors circulating α-synuclein-fibril seeds, and parental α-synuclein fibrils can template co ... Full text Cite

Heterogeneity in α-synuclein fibril activity correlates to disease phenotypes in Lewy body dementia.

Journal article Acta Neuropathol · April 2021 α-Synuclein aggregation underlies pathological changes in Lewy body dementia. Recent studies highlight structural variabilities associated with α-synuclein aggregates in patient populations. Here, we develop a quantitative real-time quaking-induced convers ... Full text Link to item Cite