Typologie d'actualités: CBM

Neonicotinoids

A scientific article linking the contamination of soils by neonicotinoid pesticides and their presence in hair of people in the Philippines has just been published by Jean-Marc Bonmatin et al. (2020) in the journal Science of the Total Environment. This article is part of researches carried out on human health by the Task Force on Systemic Pesticides, which brings together more than sixty independent researchers (www.tfsp.info & Facebook TFSP). This article also sheds light on the exposure of populations, particularly in the context of the possible reintroduction of neonicotinoids for sugar beet in France.

This article is highlighted by the CNRS chemistry institute.

Detection of amyloid peptides: biomarkers for Alzheimer’s Disease and Diabetes

Metal chelates targeted to amyloid peptides are widely explored as diagnostic tools or therapeutic agents for amyloidogenic diseases. For example, gadolinium complexes can be used as MRI probes, while radiocomplexes (64Cu, 99mTc, etc) can be exploited for nuclear imaging. Other metal complexes capable of preventing aggregate formation are proposed to derive therapeutic strategies.

All these molecules are amphiphilic, composed of a hydrophilic part (containing the metal) and a hydrophobic one (capable of targeting the amyloid aggregates). This particular structure enables the formation of micelles in solution.

The groups of CBM and LCC (Toulouse) have found that this micellisation property has drastic and unexpected consequences on their ability to recognize amyloid peptides and a high impact on their in vivo biodistribution.

The researchers have developed a novel probe with nanomolar affinity towards Aβ and amylin, biomarkers of Alzheimer’s Disease and Ddiabetes, respectively.

This exceptional affinity for a metal complex is only obtained if the complex is present as “single molecule”. Once in the micellar form, this affinity drops by 1000-fold.

These results have a direct consequence for the design of novel imaging and therapeutic probes for amyloidogenic pathologies.

See the article

RNA Remodeling Proteins, Methods and Protocols

The second edition of the book “RNA Remodeling Proteins, Methods and Protocols” edited by Marc Boudvillain has just been published.

This volume of the “Methods in Molecular Biology” series compiles new methods to study RNA-protein complexes and the mechanisms leading to their structural remodeling. The volume includes 4 chapters written by CBM researchers and ideally complements the first edition published in 2015.

 

Targeting the LINGO-1 receptor and its hetero-complexes: new therapeutic perspectives for the treatment of demyelinating and neurodegenerative diseases

LINGO-1 is a transmembrane protein mainly expressed in neurons and oligodendrocytes where it negatively regulates regeneration, neuronal survival, oligodendrocyte differentiation and myelination. Its expression was shown to be dysregulated in several brain disorders, in particular, Parkinson's disease and multiple sclerosis, which makes LINGO-1 a particular interesting therapeutic target. Three homologs LINGO-2, LINGO-3 and LINGO-4 have been described in human but until now their functions remain largely unknown. In this article published in the FASEB Journal, the researchers evaluated the expression, the cerebral distribution and the colocalization of these different homologs in several brain areas. They also showed the formation of hetero-complexes of LINGO-1 with its homologs in the brain, revealing a new level of complexity in the regulation of the activity of these receptors. The demonstration of this LINGO-1 signaling opens the way to new strategies to modulate its activity for the treatment of brain disorders.

Guillemain, A., Y. Laouarem, L. Cobret, D. Stefok, W. Chen, S. Boch, A. Zahaf, L. Blot, F. Reverchon, T. Normand, M. Decoville, C. Grillon, E. Traiffort and S. Morisset (2020). "LINGO family receptors are differentially expressed in mouse brain and forms native multimeric complexes " FASEB J (2020) doi : 10.1096/fj.202000826R