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

ABSTRACT: 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 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

SUBMITTER: Sprenkle NT 

PROVIDER: S-EPMC6379102 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature