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Endoplasmic reticulum stress is transmissible in vitro between cells of the central nervous system

Endoplasmic reticulum stress is transmissible in vitro between cells of the central nervous system

Journal of Neurochemistry 2018

Improper protein folding and trafficking are common pathological events in neurodegenerative diseases that result in the toxic accumulation of misfolded proteins within the lumen of the endoplasmic reticulum (ER). While low-level stimulation of the unfolded protein response (UPR) is protective, sustained UPR activation resulting from prolonged ER stress can promote neurotoxicity. The cell-autonomous mechanisms of the UPR have been extensively characterized. However, the cell-extrinsic role of the UPR under physiological and pathological states in the central nervous system (CNS) remains to be elucidated. To begin to address this, we evaluated if transferring conditioned media between ER stressed astrocytes and neurons could modulate their functional characteristics. Our results indicate that ER stressed astrocytes and neurons secrete a molecule(s) with lipid characteristics which regulates both inflammatory and ER stress responses in other astrocytes, neurons, and microglia in vitro. Initial exposure to this stress factor(s) confers resistance against subsequent ER stress to neurons. However, persistent exposure to this unidentified mediator(s) suppresses the initial protective effect and becomes cytotoxic. Overall, these findings provide insight into the cell-nonautonomous influence of ER stress on cells of the central nervous system. This article is protected by copyright. All rights reserved.

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Accession: 065981638

Download citation: RISBibTeXText

PMID: 30520047

DOI: 10.1111/jnc.14642

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