HSP70 has now been shown to interrupt several of these pathways and ultimately leads to improvements in neurological outcome. In acute brain injury models, many studies have reported that in addition to typical chaperone functions, HSP70 interrupted multiple cell death pathways, such as classical apoptosis, necrosis, and inflammation. HSP70, in concert with its co-chaperone HSP40, is a key HSP family member involved in the degradation of damaged proteins. Under conditions of cell stress or injury, these actions protect the cell by preventing the aggregation of damaged proteins and promote the assembly of nascent proteins. They are a family of proteins identified by their molecular weight, and possess chaperone functions for which they have been described to assist in protein folding, protein degradation and other related activities. These proteins were so named, as they were noted to be highly induced by heat stress. One of the most highly upregulated stress proteins are the heat shock proteins (HSPs).
The brain undergoes a stress response after cerebral ischemia (CI) and traumatic brain injury (TBI).
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