SERCA Silencing Alleviates Aß(1-42)-Induced Toxicity in a C. elegans Model

The Sarco Endoplasmic Reticulum Ca2+-ATPase (SERCA) pumps cytosolic Ca2+ into the endoplasmic reticulum lumen (ER) to maintain cytosolic and ER Ca2+ levels under physiological conditions. Previous reports suggest that cellular Ca2+ homeostasis is compromised in Alzheimer’s Disease (AD) and that SERC...

Descripción completa

Detalles Bibliográficos
Autores: Caldero-Escudero, Elena, Romero-Sanz, Silvia, Alvarez-Illera, Pilar, Fernandez-Martinez, Silvia, Fuente, Sergio de la, García-Casas, Paloma, Fonteriz, Rosalba I., Montero, Mayte, Álvarez, Javier, Santo-Domingo, Jaime
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/423180
Acceso en línea:http://hdl.handle.net/10261/423180
Access Level:acceso abierto
Palabra clave:C. elegans
SERCA
sca-1
Alzheimer’s disease
Beta-amyloid
Mitochondria
ER Ca2+ signaling
Descripción
Sumario:The Sarco Endoplasmic Reticulum Ca2+-ATPase (SERCA) pumps cytosolic Ca2+ into the endoplasmic reticulum lumen (ER) to maintain cytosolic and ER Ca2+ levels under physiological conditions. Previous reports suggest that cellular Ca2+ homeostasis is compromised in Alzheimer’s Disease (AD) and that SERCA activity can modulate the phenotype of AD mouse models. Here, we used a C. elegans strain that overexpresses the most toxic human ß-amyloid peptide (Aß(1-42)) in body-wall muscle cells to study the effects of SERCA (sca-1) silencing on Aß(1-42)-induced body-wall muscle dysfunction. sca-1 knockdown reduced the percentage of paralyzed worms, improved locomotion in free-mobility assays, and restored pharynx pumping in Aß(1-42)-overexpressing worms. At the cellular level, sca-1 silencing partially prevented Aß(1-42)-induced exacerbated mitochondrial respiration and mitochondrial ROS production and restored mitochondrial organization around sarcomeres. sca-1 knockdown reduced the number and size of Aß(1-42) aggregates in body–wall muscle cells and prevented the formation of Aß(1-42) oligomers. Aß(1-42) expression induced a slower kinetics of spontaneous cytosolic Ca2+ transients in muscle cells and sca-1 partially restored these changes. We propose that partial sca-1 loss of function prevents the toxicity associated with beta-amyloid accumulation by reducing the formation of Aß(1-42) oligomers and improving mitochondrial function, in a mechanism that requires remodeling of cytosolic Ca2+ dynamics and partial ER Ca2+ depletion.