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- W4213322073 abstract "Genetic, environmental, and aging-related insults can promote the misfolding and subsequent aggregation of secreted proteins implicated in the pathogenesis of numerous diseases. This has led to considerable interest in understanding the molecular mechanisms responsible for regulating proteostasis in extracellular environments such as the blood and cerebrospinal fluid (CSF). Extracellular proteostasis is largely dictated by biological pathways comprising chaperones, folding enzymes, and degradation factors localized to the ER and extracellular space. These pathways limit the accumulation of nonnative, potentially aggregation-prone proteins in extracellular environments. Many reviews discuss the molecular mechanisms by which these pathways impact the conformational integrity of the secreted proteome. Here, we instead focus on describing the stress-responsive mechanisms responsible for adapting ER and extracellular proteostasis pathways to protect the secreted proteome from pathologic insults that challenge these environments. Further, we highlight new strategies to identify stress-responsive pathways involved in regulating extracellular proteostasis and describe the pathologic and therapeutic implications for these pathways in human disease." @default.
- W4213322073 created "2022-02-24" @default.
- W4213322073 creator A5050150743 @default.
- W4213322073 creator A5063536940 @default.
- W4213322073 creator A5083999892 @default.
- W4213322073 date "2022-02-22" @default.
- W4213322073 modified "2023-10-16" @default.
- W4213322073 title "Stress-responsive regulation of extracellular proteostasis" @default.
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