University of Texas Health Science Center at Houston
Neurology
A postdoctoral Research Fellow at UTHealth Science Center at Houston, with a Ph.D. in Pharmacology and Toxicology from The University of Texas Medical Branch at Galveston. My PhD dissertation work concentrated on unraveling the mechanistic link between oxidative stress and insulin resistance in the liver. During my first postdoctoral fellowship at the Department of Obstetrics and Gynecology at UTMB, I worked on identifying placental barrier transporters involved in pravastatin trans-placental transport and their expression in healthy and preeclamptic placentas. After that I moved to Neurology Department where I worked on passive immunotherapy targeting tau oligomeric strains in aged transgenic animals of tauopathy. Currently, I am focusing on protein misfolding disorders, particularly Alzheimer's disease, Parkinson's disease and Diabetes. I was awarded the Alzheimer’s Association Research Fellowship to investigate the role of tau in peripheral insulin signaling in an attempt to understand the mechanistic link between AD and peripheral insulin resistance.

Presenter of 1 Presentation

PMCA AMPLIFIED ALPHA-SYNUCLEIN AGGREGATES FROM PD AND MSA CAN SEED AGGREGATION IN CELLS AND MAINTAIN THEIR STRAIN CHARACTERISTICS

Session Type
SYMPOSIUM
Date
Fri, 18.03.2022
Session Time
09:10 AM - 11:10 AM
Room
ONSITE: 114
Lecture Time
09:10 AM - 09:25 AM

Abstract

Aims

Parkinson’s disease (PD) and Multiple System Atrophy (MSA) are synucleinopathies with overlapping clinical symptoms, nevertheless, with different prognosis and neuropathological abnormalities. It is thought that the different disease characteristics are determined by distinct conformations of alpha-synuclein (αSyn) aggregates, which can self-propagate and spread between cells via a prion-like mechanism. Protein misfolding cyclic amplification (PMCA) is a technique that has been previously shown to detect with high sensitivity and specificity αSyn aggregates in cerebrospinal fluid and to discriminate between samples from patients diagnosed with PD and MSA. Our goal is to analyze whether PMCA amplification maintains the αSyn strain properties. For this purpose, we studied PMCA-amplified aggregates from patients’ CSF and brain samples in comparison with un-amplified patients’ brain homogenates.

Methods

We used biosensor HEK293T cell line stably expressing αSyn (A53T)-CFP/YFP fusion proteins to study αSyn seeding properties in cell culture.

Results

Our data show that PMCA-amplified αSyn aggregates from either CSF or brain homogenates were able to induce seeding in reporter cells. Importantly, differences in morphological features of αSyn accumulations in cells produced by PD or MSA amplified aggregates were indistinguishable from those observed when cells were exposed to un-amplified PD or MSA brain homogenates.

Conclusions

The present findings show that, regardless of the source of aggregates, PD and MSA seeds produce cellular accumulation of αSyn with different morphologies. These findings not only confirm the presence of different strains of αSyn in PD and MSA, but most importantly they also demonstrate that the seeding properties of PMCA amplified aggregates are maintained after amplification.

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