Dr. Georges Lévesque received his B.Sc. in Biochemistry from the Université du Québec à Montréal (UQAM). He continued his studies at Laval University, where he obtained a certificate in pedagogy, a Master’s degree in medical biochemistry, and a Ph.D. in cellular and molecular biology. He then embarked on a postdoctoral fellowship on the molecular genetics of Alzheimer’s disease at the Centre for Research in Neurodegenerative Diseases at the University of Toronto. He is a co-discoverer of the presenilin 1 and 2 genes, along with their mutations that lead to the development of an early, familial form of Alzheimer’s disease. Dr. Lévesque received the first Frist-Jus Memorial Award for Neurodegenerative Disease Research from the University of Toronto. He joined Laval University in late 2001. He is currently Assistant Director and Full Professor in the Department of Psychiatry and Neuroscience of the Faculty of Medicine, and continues his basic research activities on Alzheimer’s disease within the neuroscience axis of the CHU de Québec.

Presenilin, amyloid and the genetics of Alzheimer’s disease;

Dr. Lévesque’s research interests focus on the molecular aspects of Alzheimer’s disease. This disease is characterized by the degeneration of the central nervous system. The biochemical mechanisms leading to Alzheimer’s disease are not fully known. His team is studying the biochemical pathways by which the mutated form of presenilin leads to the degeneration of nerve cells and an early and aggressive form of Alzheimer’s disease. Dr. Lévesque has shown that presenilin is partly responsible for amyloid peptide synthesis, the accumulation of which causes neuronal damage to Alzheimer’s patients. Presenilin mutations amplify amyloid levels. In parallel with the studies on the fundamental role of presenilin, and in order to counter amyloid peptide synthesis, Dr. Lévesque began developing a therapeutic molecule, a ribozyme, to reduce levels of amyloid precursor mRNA and in turn block the accumulation of this peptide, which is responsible for neuronal degeneration. Dr. Lévesque, in collaboration with Dr. Emmanuel Planel, is also interested in creating a ribozyme directed against Tau protein mRNA, which is responsible for neurofibrillary tangles associated with cognitive deficits in Alzheimer’s pathology. Dr. Lévesque is also studying the role of genetic markers associated with Alzheimer’s disease, identified via genome analysis of a French Canadian population.

The role of FUS protein in lateral amyotrophic sclerosis;

Most recently, Dr. Lévesque initiated a project on amyotrophic lateral sclerosis, aimed at recreating the FUS protein mutations responsible for this pathology in iPS cells, using CRISPR- Cas9 technology. These modified cells will be used to screen libraries of molecules that may interfere with the toxicity of the mutated FUS protein.

CHUL
2705, boulevard Laurier
P-09602
Québec, Québec
Canada G1V 4G2

Latest news

Data not available

19 entries « 2 of 2 »

Ziane R, Huang H, Moghadaszadeh B, Beggs AH, Levesque G, Chahine M

Cell membrane expression of cardiac sodium channel Na(v)1.5 is modulated by alpha-actinin-2 interaction.

Journal Article

Biochemistry, 49 (1), pp. 166-78, 2010, ISSN: 0006-2960.

Abstract | Links:

Tremblay CS, Huard CC, Huang FF, Habi O, Bourdages V, Levesque G, Carreau M

The fanconi anemia core complex acts as a transcriptional co-regulator in hairy enhancer of split 1 signaling.

Journal Article

J Biol Chem, 284 (20), pp. 13384-95, 2009, ISSN: 0021-9258.

Abstract | Links:

Tremblay CS, Huang FF, Habi O, Huard CC, Godin C, Levesque G, Carreau M

HES1 is a novel interactor of the Fanconi anemia core complex.

Journal Article

Blood, 112 (5), pp. 2062-70, 2008, ISSN: 0006-4971.

Abstract | Links:

Larbi A, Levesque G, Robert L, Gagne D, Douziech N, Fulop T Jr

Presence and active synthesis of the 67 kDa elastin-receptor in human circulating white blood cells.

Journal Article

Biochem Biophys Res Commun, 332 (3), pp. 787-92, 2005, ISSN: 0006-291X.

Abstract | Links:

Mastrangelo P, Mathews PM, Chishti MA, Schmidt SD, Gu Y, Yang J, Mazzella MJ, Coomaraswamy J, Horne P, Strome B, Pelly H, Levesque G, Ebeling C, Jiang Y, Nixon RA, Rozmahel R, Fraser PE, St George-Hyslop P, Carlson GA, Westaway D

Dissociated phenotypes in presenilin transgenic mice define functionally distinct gamma-secretases.

Journal Article

Proc Natl Acad Sci U S A, 102 (25), pp. 8972-7, 2005, ISSN: 0027-8424.

Abstract | Links:

Hebert SS, Godin C, Levesque G

Oligomerization of human presenilin-1 fragments.

Journal Article

FEBS Lett, 550 (1-3), pp. 30-4, 2003, ISSN: 0014-5793.

Abstract | Links:

Godin C, Auclair A, Ferland M, Hebert SS, Carreau M, Levesque G

Presenilin-1 is indirectly implicated in Notch1 cleavage.

Journal Article

Neuroreport, 14 (12), pp. 1613-6, 2003, ISSN: 0959-4965.

Abstract | Links:

Hebert SS, Bourdages V, Godin C, Ferland M, Carreau M, Levesque G

Presenilin-1 interacts directly with the beta-site amyloid protein precursor cleaving enzyme (BACE1).

Journal Article

Neurobiol Dis, 13 (3), pp. 238-45, 2003, ISSN: 0969-9961.

Abstract | Links:

Hebert SS, Godin C, Tomiyama T, Mori H, Levesque G

Dimerization of presenilin-1 in vivo: suggestion of novel regulatory mechanisms leading to higher order complexes.

Journal Article

Biochem Biophys Res Commun, 301 (1), pp. 119-26, 2003, ISSN: 0006-291X.

Abstract | Links:

19 entries « 2 of 2 »
Signaler des ajouts ou des modifications

Active projects

  • Centre de recherche du CHU de Québec - Université Laval, Subvention, Centre hospitalier universitaire de Québec - Université Laval, Centres de recherche affiliés, from 2017-01-01 to 2099-12-31
  • Centre thématique de recherche en neurosciences, Subvention, Institutionnel - BDR, BDR - Centres de recherche reconnus, from 1999-06-01 to 2023-05-01
  • Discovery of Therapeutic Targets for FUS-Dependant Forms of ALS., Subvention, Société canadienne de la sclérose latérale amyotrophique, Arthur J. Hudson translational team grant program-2015, from 2015-10-01 to 2020-09-30
Data provided by the Université Laval research projects registery