Increased expression and retention of the secretory chaperone proSAAS following cell stress
JournalCell Stress and Chaperones
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AbstractThe secretory pathway of neurons and endocrine cells contains a variety of mechanisms designed to combat cellular stress. These include not only the unfolded protein response pathways but also diverse chaperone proteins that collectively work to ensure proteostatic control of secreted and membrane-bound molecules. One of the least studied of these chaperones is the neural- and endocrine-specific molecule known as proSAAS. This small chaperone protein acts as a potent anti-aggregant both in vitro and in cellulo and also represents a cerebrospinal fluid biomarker in Alzheimer's disease. In the present study, we have examined the idea that proSAAS, like other secretory chaperones, might represent a stress-responsive protein. We find that exposure of neural and endocrine cells to the cell stressors tunicamycin and thapsigargin increases cellular proSAAS mRNA and protein in Neuro2A cells. Paradoxically, proSAAS secretion is inhibited by these same drugs. Exposure of Neuro2A cells to low concentrations of the hypoxic stress inducer cobalt chloride, or to sodium arsenite, an oxidative stressor, also increases cellular proSAAS content and reduces its secretion. We conclude that the cellular levels of the small secretory chaperone proSAAS are positively modulated by cell stress. Copyright 2020, The Author(s).
DescriptionPublisher correction: Due to an unfortunate mistake in the production process, the the words ‘increases’ and ‘decreased’ were transposed in the penultimate citation of Viard et al. 1999. The original article has been corrected and the correct sentence is also published here and should read: “however, during heat shock stress, decreases in cellular clusterin occur in parallel with increased secretion (Viard et al. 1999)”. See at https://doi.org/10.1007/s12192-020-01128-7.
SponsorsNational Institutes of Health, NIH AG062222
Identifier to cite or link to this itemhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85087396336&doi=10.1007%2fs12192-020-01128-7&partnerID=40&md5=c494597b0f548b7dc1c52ddb2fca0448; http://hdl.handle.net/10713/13306
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