Abstract
The heat shock response in pancreatitis that is activated via HSP70 protects acinar cells through multiple simultaneous mechanisms. It inhibits trypsinogen activation and modulates NF-κB signaling to limit acinar cell injury. On the other hand, HSP70 is overexpressed in pancreatic cancer and is hijacked by the cellular machinery to inhibit apoptosis. Inhibition of HSP70 in pancreatic cancer by a novel compound, Minnelide, has shown considerable clinical promise.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 114-122 |
| Number of pages | 9 |
| Journal | Journal of Surgical Oncology |
| Volume | 116 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jul 1 2017 |
Keywords
- calcium
- HSP70
- lysosomes
- minnelide
- pancreatic cancer
- pancreatitis
- triptolide
ASJC Scopus subject areas
- Surgery
- Oncology
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Cite this
Giri, B., Sethi, V., Modi, S., Garg, B., Banerjee, S., Saluja, A., & Dudeja, V. (2017). “Heat shock protein 70 in pancreatic diseases: Friend or foe”. Journal of Surgical Oncology, 116(1), 114-122. https://doi.org/10.1002/jso.24653