Calreticulin (crt-1) silencing reduces Aß1–42-induced toxicity and restores muscle function in C. elegans.

Accumulation of aggregated β-amyloid peptide is a key histopathological feature of Alzheimer's Disease (AD). Experimental models of AD based on β-amyloid peptide display calcium (Ca2+) signaling alterations, and targeting key components of the cellular Ca2+ signaling system has been postulated...

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Bibliographic Details
Authors: Caldero-Escudero, Elena, Romero-Sanz, Silvia, Alvarez-Illera, Pilar, Fuente, Sergio de la, García-Casas, Paloma, Fonteriz, Rosalba I., Montero, Mayte, Álvarez, Javier, Santo-Domingo, Jaime
Format: article
Status:Published version
Publication Date:2025
Country:España
Institution:Consejo Superior de Investigaciones Científicas (CSIC)
Repository:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/399697
Online Access:http://hdl.handle.net/10261/399697
Access Level:Open access
Keyword:C. elegans
Calreticulin
Crt-1
Alzheimer's disease
beta-amyloid
Mitochondria
Ca2+ signaling
Description
Summary:Accumulation of aggregated β-amyloid peptide is a key histopathological feature of Alzheimer's Disease (AD). Experimental models of AD based on β-amyloid peptide display calcium (Ca2+) signaling alterations, and targeting key components of the cellular Ca2+ signaling system has been postulated to modulate AD onset and progression. Here we have taken advantage of a C. elegans strain that over-expresses the most toxic human ß-amyloid peptide (Aß1–42) in body-wall muscle cells, to study the impact of calreticulin (crt-1) silencing on body-wall muscle performance. Crt-1 knockdown reduced the percentage of paralyzed worms in a dose-dependent manner and improved locomotion parameters in free-mobility assays in Aß1–42-overexpressing worms. At the cellular level, crt-1 silencing prevented Aß1–42-induced exacerbated mitochondrial respiration and mitochondrial ROS production without impacting mitochondrial sarcomere organization. Crt-1 knockdown reduced the number and size of Aß1–42 aggregates in body-wall muscle cells and prevented the formation of Aß1–42 oligomers. We propose that crt-1 depletion reduces the number of Aß1–42 aggregates, precluding Aß1–42-induced mitochondrial toxicity and improving muscle function. We identify C. elegans crt-1 as a gene involved in the toxicity associated with the expression of human Aß1–42, and thus a potential new target for treatment.