Jean-Marc Taymans (France)
Univ Lille, Inserm, CHU Lille
UMR-S 1172 Lille Neuroscience & Cognition
Jean-Marc Taymans, PhD/Ir, is a Bio-engineer from the KU Leuven (Belgium, 1994). He started his professional career as a vaccine process engineer at SmithKline-Beecham Biologicals (Rixensart, Belgium, 1995-99) before starting PhD research at the graduate school of Neurosciences in Amsterdam (Free University of Amsterdam). He performed his doctoral research in the research labs of Johnson & Johnson Pharmaceutical Research and Development (Beerse, Belgium, 1999-2003), studying schizophrenia-related proteins in the basal ganglia. In 2004 Dr. Taymans joined the KU Leuven to research the molecular pathogenesis of Parkinson’s disease genes. From 2009-2010 he was a Fulbright scholar at the National Institutes of Health, working with Dr. Mark R. Cookson. He joined the Jean-Pierre Aubert Research Center in Lille (France), a mixed Inserm - Université de Lille - Lille University Hospital center, in October 2014 to further develop PD protein signaling studies while integrating clinical translation of experimental findings in patient biosamples. In September 2017, he was appointed Associate Professor in Neuroscience at the Université de Lille. Dr. Taymans’s research has focused since 2004 on the cellular signaling processes of LRRK2, using a multidisciplinary approach from biochemical analysis to cellular models to in vivo validation in models and the application of this knowledge to therapeutic and clinical biomarker applications.

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 Conference Calendar

LRRK2 AND RAB DETECTION IN BIOFLUIDS AS POTENTIAL BIOMARKER FOR PD

Session Name
1090 - FLUID BIOMARKERS 2 (ID 204)
Session Type
SYMPOSIUM
Date
Fri, 18.03.2022
Session Time
09:10 AM - 11:10 AM
Room
ONSITE: 131-132
Lecture Time
10:55 AM - 11:10 AM
Presenter

Abstract

Aims

Levels of expression or of phosphorylation of leucine-rich repeat kinase 2 (LRRK2) have the potential for use as disease or pharmacodynamic biomarkers. LRRK2 phosphorylation levels at the S910-S935-S955-S973 phosphosites are reduced for most disease mutant forms of LRRK2, while for phospho-S1292, phospho-Rab8 and phospho-Rab10, levels are increased for most mutants. Also, all of these 5 sites are rapidly dephosphorylated upon LRRK2 inhibitor treatment, considered potential therapeutics. The main objective of this study is therefore to characterize detection of leucine-rich repeat kinase 2 (LRRK2) in human and rat urine.

Methods

With urine collected from test individuals as well as rats, we have applied an ultracentrifugation based fractionation protocol to isolate exosome-enriched fractions. We used western blot with antibodies directed against LRRK2, LRRK2 phosphorylation sites as well as Rab8 and Rab10 total and phosphorylated proteins in order to measure these LRRK2 and Rab epitopes in urine.

Results

We confirm the presence of LRRK2 and Rab8/10 in human urinary exosomes, including total LRRK2 as well phosphorylated forms of LRRK2 pS910, pS935, pS955, pS973, pS1292 and phosphorylated Rab8 and Rab10. We also confirm LRRK2 and Rab expression in rodent urinary exosomes. We will aslo present work currently ongoing to assess changes in total-LRRK2 as well as pS935-LRRK2, pS1292-LRRK2, phospho-Rab8 and phospho-Rab10 in PD patient groups relative to controls.

Conclusions

This study assesses LRRK2 and Rabs as a disease and pharmacodynamic marker in human urine samples and our current analysis shows LRRK2 and Rab epitopes modified in patient groups.

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