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Intracellular Refolding Assay
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Molecular Chaperone Accumulation in Cancer and Decrease in Alzheimer's Disease: The Potential Roles of HSF1.
Stuart K Calderwood1, Ayesha Murshid1
1Molecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Center for Life Sciences 610, Harvard Medical SchoolBoston, MA, USA.
Frontiers in Neuroscience
|May 10, 2017
Summary
Molecular chaperones, or heat shock proteins (HSP), decline with aging, impacting Alzheimer's disease (AD) and cancer. Dysregulation of the HSF1 factor may be key in these age-related diseases.
Area of Science:
- Cellular Biology
- Neuroscience
- Oncology
Background:
- Molecular chaperones, including heat shock proteins (HSP), maintain cellular proteostasis.
- Cellular aging typically reduces HSP synthesis, but this decline is variable in age-related diseases.
- Alzheimer's disease (AD) shows reduced neuronal heat shock response, while cancer cells exhibit increased HSP levels.
Purpose of the Study:
- To investigate the role of heat shock protein (HSP) dysregulation in Alzheimer's disease (AD) and cancer.
- To explore the mechanisms of heat shock factor 1 (HSF1) regulation in the context of these diseases.
Main Methods:
- Literature review and discussion of existing research on HSPs, aging, AD, and cancer.
- Analysis of HSF1 regulation pathways in relation to observed HSP changes.
Main Results:
- HSP synthesis generally decreases with aging, but this is altered in AD and cancer.
- AD exhibits reduced neuronal HSP expression, potentially due to aging or AD-specific metabolic changes.
- Cancer cells show increased HSP levels, possibly due to higher folding demands or adaptive mechanisms.
Conclusions:
- Dysregulation of the transcription factor HSF1 is implicated in the altered HSP expression seen in AD and cancer.
- Understanding HSF1 regulation is crucial for comprehending the pathogenesis of these age-related diseases.
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