Heat Shock Proteins: Cellular Resilience

Resilience. Survival. Flexibility. Our cells need to be able to survive in all kinds of conditions – from cold to heat, nutrient deprivation to toxic insults. Heat shock proteins are at the heart of cellular resilience.

Here we will cover the essentials of heat shock proteins, including how to activate them and the genetic variants that impact how well they work.

What are heat shock proteins?

Heat shock proteins are activated by cells in response to a stressful condition, such as exposure to high heat. They were named ‘heat shock’ due to their discovery in the 1960s as a protein that is elevated under heat stress. But it isn’t only heat that activates these proteins. Stressors such as cold, UV light, ethanol, arsenic, oxidative stress, exercise, wounds, infections, nutrient deprivation, and tissue remodeling also involve these proteins.[ref]

Heat shock proteins act as ‘chaperones’, which is a cell biology term meaning that they help to stabilize or ensure the correct folding of other proteins under stress conditions. These resilience champions come alongside and help the other proteins which are needed in cellular function.

In humans, the heat shock proteins include Hsp27, Hsp40, Hsp60, Hsp70 (or Hsp72), and Hsp90. (The numbers stand for their molecular weight.) We humans aren’t special here: heat shock proteins are actually found in all eukaryotes – from plants to animals to fungi. The HSPs help to promote survival everywhere.

” As a stress protein, heat shock protein 70 (HSP70) plays a pivotal role in protecting cells against apoptosis, oxidative damage and genetic damage. In humans, three genes encode members of the HSP70 class: HSPA1A, HSPA1B and HSPA1L.”[ref]

Hsp90 is found in most cell types and makes up about 1-2% of total cellular proteins in the body. When cells are put under stress, though, the amount of Hsp90 can rise to 4-6% of the cellular protein content.[ref]

The heat shock proteins can work together to help with the folding of a ‘client’ protein. Protein folding is essential to the function of the protein, and misfolded proteins can have detrimental effects.

Diagram of heat shock proteins interacting to help chaperone the folding of a client protein. PMC7356129

“To date, Hsp90 has been found to interact with over 200 client proteins, as well as ∼50 co-chaperones, making it a cornerstone in the cellular protein-folding machinery and an emerging target for the treatment of various disease states.”[ref]

What induces heat shock proteins?

I mentioned above that many different stressors can activate heat shock proteins.

Activators of heat shock proteins include:[ref][ref][ref]

  • bacterial or viral infection
  • oxidative stress
  • elevated temperature
  • DNA damage
  • glyphosate
  • arsenic
  • long term cold exposure
  • calorie restriction/starvation

Higher levels of heat shock protein increase resilience to stressors.[ref][ref]

What temperature activates heat shock proteins?

Heat, of course, is an activator of heat shock proteins. Another protein, heat shock factor 1, regulates the heat shock response and activates the HSPs.

Animal studies show that repeated exposure to mild heat stress (40°C or 104°F) for two hours a day for six days increased both Hsp70 and Hsp90 by around 40%. These increases caused beneficial mitochondrial adaptations.[ref]

Another study showed that exercising in the heat (42.5°C or 108°F) for 100 minutes for 10 days in a row caused an increase in Hsp72. The study concluded that the elevations from day 6 through 10 show that repeated heat exposure improves heat tolerance and reduces the risk of heat illness.[ref]

In healthy young adults, 30 minutes in a sauna increases HSP72 levels.[ref]

Mood disorders and heat shock proteins

Research points to neuroinflammation and/or mitochondrial dysfunction as a root cause of mood disorders.

Related article: Mitochondrial dysfunction and Depression

Upregulation of heat shock proteins may help to decrease oxidative stress in neurons, acting in an anti-inflammatory manner.

Repeated heat exposure, such as through using a sauna several times a week, increases heat shock proteins.

A study that looked at sauna habits of over 2,000 men found that sauna use 4+ times per week reduced the risk of mood disorder by almost 80%.[ref]

Valproic acid, which is a prescription medication used as a mood stabilizer, increases heat shock protein 70.[ref]

Neurodegenerative diseases and HSPs

Protein misfolding is at the heart of several neurodegenerative diseases including Alzheimer’s, Parkinson’s, and Huntington’s disease.

Heat shock protein 90 plays a key role in helping proteins fold correctly. In the brain, HSP90 interacts as a chaperone to prevent the misfolding of many different proteins including tau, huntingtin, and α-synuclein.[ref][ref] These are the proteins that are misfolded in Alzheimer’s (tau), Huntington’s (huntingtin), and Parkinson’s (α-synuclein) diseases.

On the other hand, the heat shock proteins may also help to stabilize and aggregate the already misfolded proteins in people who are already at a certain stage of neurodegeneration.[ref]

Whether increasing HSPs is beneficial in neurodegenerative diseases may depend on the stage of the disease. Researchers have found that Hsp90 helps to clear out amyloid-beta plaque initially, but the chronic activation in the microglia leads to a pro-inflammatory cascade.[ref]

Double-edged sword: Cancer and Heat Shock Proteins

Heat shock protein 70 is great for protecting cells from toxins and stress. But when it comes to cancer, this can be a problem. Hsp70 (aka Hsp72) can interfere with chemotherapy, preventing it from working well. Within tumor cells, Hsp70 can work to protect the cancerous cells from apoptosis and radiation therapy.[ref]

Similarly, heat shock protein 90 inhibition is another target for reducing cancer cell growth. Hsp90 is essential for numerous proteins involved in malignant progression. Clinical trials are ongoing for Hsp90 inhibitors to facilitate cancer treatments.[ref][ref]

You may be wonder, as I was, whether increasing HSPs through sauna use could increase the risk of cancer. Two studies show opposite results:

  • A study of Finnish sauna users found no increase (and no decrease) in cancer risk from sauna use in men.[ref]
  • Another Finnish study, though, found that smokers who were frequent sauna users had a 70% increased relative risk of lung cancer, compared with non-sauna users.[ref]

One difference in the studies is that people who smoke are more likely to have cancerous or pre-cancerous cells in the body.

If you are undergoing treatment for cancer, talk with your oncologist before initiating any lifestyle changes aimed at increasing heat shock proteins.

HSPs and Viral Infections:

Viruses cannot replicate on their own. Instead, they use the host’s cellular replication pathways in order to reproduce the virus. One mechanism that is co-opted by some viruses is heat shock proteins, acting as chaperones to help the viral proteins replicate.

In addition to its role in protein folding, Hsp70 is also important in viral infections. This heat shock protein helps to facilitate viral replication for certain viruses, including cytomegalovirus, rabies, RSV, HPV, and herpes simplex.[ref]

Enterovirus 71 causes hand, foot, and mouth disease. Hsp27 is upregulated by this viral infection, and this heat shock protein facilitates viral replication. Interestingly, certain traditional Chinese medicine herbs block Hsp27 and may work as antivirals in this way.[ref]

SARS-CoV-2 (COVID-19), and other coronaviruses, utilize Hsp90 for quick viral replication in cells. Inhibitors of HSP90 have been shown to inhibit SARS-CoV-2 replication in cell studies.[ref][ref]

Genetic variants that impact heat shock proteins:

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HSPA1L gene encodes part of the HSP70 protein

Check your genetic data for rs2227956  T2437C (23andMe v4, v5; AncestryDNA):

  • A/A: typical genotype
  • A/G: somewhat decreased HSP70, increased risk of male infertility
  • G/G: increased risk of male infertility[ref]; decreased HSP70[ref]

Members: Your genotype for rs2227956 is .

Check your genetic data for rs2075800 (23andMe v4, v5; AncestryDNA):

  • C/C: typical
  • C/T: increased relative risk of lupus
  • T/T: increased relative risk of lupus[ref]; increased risk of foot ulcers in diabetes[ref] likely decreased HSP70 function[ref]

Members: Your genotype for rs2075800 is .

Check your genetic data for rs2763979 (23andMe v4, v5; AncestryDNA):

  • C/C: typical
  • C/T: typical risk of noise-induced hearing loss
  • T/T: significantly increased risk of noise-induced hearing loss.[ref]

Members: Your genotype for rs2763979 is .

Check your genetic data for rs1043618 (23andMe v4):

  • C/C: increased risk of heart disease[ref]
  • C/G: typical risk of heart disease
  • G/G: typical

Members: Your genotype for rs1043618 is .

 

HSPA5 gene: encodes GRP78, a part of heat shock protein 70

Check your genetic data for rs391957 (23andMe v5; AncestryDNA):

  • C/C: typical
  • C/T: higher risk in certain cancers, increased risk of peripheral neuropathy in diabetes
  • T/T: higher risk in certain cancers[ref][ref][ref] increased risk of peripheral neuropathy in diabetes[ref]

Members: Your genotype for rs391957 is .

 

TRAP1 gene encodes a type of heat shock protein 90 found in the mitochondria

Check your genetic data for rs113476582 Il2253Val (23andMe v5):

  • C/C: really rare, likely increased pain, fatigue, gastrointestinal symptoms
  • C/T: increased risk of chronic pain, fatigue, and gastrointestinal dysmotility[ref]
  • T/T: typical

Members: Your genotype for rs113476582 is .

 


Lifehacks:

In certain situations, upregulating heat shock proteins can be very beneficial. HSPs may promote longevity, protecting against neurodegenerative diseases and muscle mass loss.[ref]

But…always keep in mind that heat shock proteins can promote viral replication, so upregulation during an infection may not be smart. Additionally, HSPs play a role in helping tumors to survive. In someone with cancer, inhibiting HSPs is an option that some cancer treatments employ.

Upregulating Heat shock proteins: More than just saunas

Repeated heat exposure, either through exercising in the heat or through sauna exposure, increases heat shock proteins.[ref]

  • If you don’t have access to a sauna, regularly soaking in a hot bath or hot tub is also beneficial. [ref]
  • Hot yoga also increases heat shock proteins.[ref]
  • The key seems to be the repeated exposure to cause a consistent increase in heat shock proteins.
  • Lavender essential oil increases Hsp70 expression.[ref]
  • Sulforaphane, a compound in broccoli sprouts, upregulates Hsp70.[ref]

Inhibiting HSPs (in cancer)

An Hsp900 inhibitor, 17-AAG, has been investigated in phase I and phase II cancer clinical trials by a large pharmaceutical company. This substance is a type of antibiotic, but since it was going to be off-patent soon, trials were stopped. Certain other antibiotics also inhibit Hsp90, but the side effects may outweigh any benefits.[ref]

EGCG, a component of green tea, is a natural Hsp90 inhibitor.[ref]

Other natural inhibitors of Hsp90 include Gedunin and Celastrol, which are related compounds from the Indian neem tree and other plants species, such as the root of the Thunder god vine. [ref]


Member’s Blueprint: Next Steps and Experiments

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Author Information:   Debbie Moon
Debbie Moon is the founder of Genetic Lifehacks. She holds a Master of Science in Biological Sciences from Clemson University and an undergraduate degree in engineering from Colorado School of Mines. Debbie is a science communicator who is passionate about explaining evidence-based health information. Her goal with Genetic Lifehacks is to bridge the gap between the research hidden in scientific journals and everyone's ability to use that information. To contact Debbie, visit the contact page.