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 |
Bibliographical note
Publisher Copyright:© 2017 Wiley Periodicals, Inc.
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- HSP70
- calcium
- lysosomes
- minnelide
- pancreatic cancer
- pancreatitis
- triptolide
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