Business
ProMIS Neurosciences Publishes in the Journal of Biological Chemistry on the Interaction Between Pathogenic Proteins as a Treatment Target for ALS
Study results support ProMIS’ TDP-43 misfolding-specific epitope as a potential therapeutic target for Amyotrophic Lateral Sclerosis (ALS) CAMBRIDGE,
About this update from Promis Neurosciences Inc.
[{"type":"text","content":"Study results support ProMIS’ TDP-43 misfolding-specific epitope as a potential therapeutic target for Amyotrophic Lateral Sclerosis (ALS)\nCAMBRIDGE, Massachusetts and TORONTO, Ontario, April 09, 2024 (GLOBE NEWSWIRE) -- ProMIS Neurosciences Inc.(Nasdaq: PMN), a biotechnology company focused on the generation and development of antibody therapeutics targeting toxic misfolded proteins in neurodegenerative diseases such as Alzheimer’s disease (AD), amyotrophic lateral sclerosis (ALS) and multiple system atrophy (MSA), today announced the publication of supportive preclinical data in the Journal of Biological Chemistry in an article titled, “Tryptophan residues in TDP-43 and SOD1 modulate the cross-seeding and toxicity of SOD1.\" ProMIS is developing antibodies selectively targeting misfolded forms of TDP-43 and SOD1. ALS is a fatal neurodegenerative disease of motor neurons. Toxic aggregates of superoxide dismutase-1 (SOD1) and TAR DNA-binding protein 43 (TDP-43) in motor neurons are characteristic of ALS.The study showed that these two proteins interact such that misfolding of TDP-43 leads to misfolding and aggregation of SOD1 in a cell system and promotes motor neuron damage in zebrafish. “Publication of these data underscores the connection of misfolded proteins and ALS and supports targeting our TDP-43-specific epitope with PMN267 as a potential therapeutic approach,” stated Neil Warma, Chief Executive Officer of ProMIS Neurosciences. “PMN267 is advancing through preclinical development and is showing promise as a potential treatment for ALS. We are particularly pleased to have our data published in this well-regarded, peer-reviewed journal as it adds to the growing body of scientific knowledge on the pathogenic role of misfolded proteins in neurodegenerative diseases.” The study demonstrated a pathologic synergy between SOD1 and TDP-43 in cell culture and in zebra fish.The interaction between these 2 proteins was characterized at the molecular level.The results indicated that the misfolded TDP-43 epitope previously identified by ProMIS and targeted by PMN267 contains a tryptophan amino acid critical to the pathogenic interaction with SOD1 thereby providing further biological support for the potential of therapeutic intervention with PMN267. “These findings provide an important contribution to our understanding of ALS/FTLD mo...