What do you do when something is broken – there are two options – you fix it, or you throw it away.

Now, when you are speaking about your body throwing it away isn’t the best option.

You need your meat covered skeleton to carry ‘you’ around – for as long as is humanly possible.

Otherwise, there is place where you go which is the last place in the world you’ll ever go.

So, you’re left with – lets fix this thing we call the body – as fast as we can.

And over the past 3.5 billion years since life evolved on this third rock from the sun, life has been figuring out a way to fix itself.

And in humans, there is an incredibly complex system for fixing all the broken bits that’s based on heat.

Why does the body heat up when it gets sick or broken?

And the answer is: The increase in temperature triggers the body (on an individual cellular level) to produce a cascade of little beauties called Heat Shock Proteins

In the intricate workings of the human body, cells form the fundamental building blocks, carrying out vital functions that sustain life.

However, like any intricate machinery, cells are susceptible to damage, often caused by environmental stressors, aging, and even normal cellular processes.

And the body possesses an ingenious defense mechanism known as heat shock proteins (HSPs), which are specialized proteins that act as cellular protectors and repairmen.

If you thought that the fever you get when you get sick is, so the extra heat kills the germs and little critters that are causing the problem, think again.

Every time the body gets damaged it turns up the heat.

The rise in temperature of even a degree or two tells all the of the structures in the cell (and there are dozens of structures, called organelles in the cell) to start pumping out the repair proteins.

Heat Shock Proteins. HSPs

These proteins play a pivotal role in cellular protection and repair mechanisms.

They assist in the proper folding of newly synthesized proteins, refolding of misfolded proteins, and the degradation of irreparably damaged ones.

Essentially, HSPs act as quality control agents within cells, ensuring the proper functioning and survival of cellular proteins under stress.

The primary role of heat shock proteins is to ensure the correct folding of proteins within the cell.

Proteins are the workhorses of cellular function, responsible for countless biochemical processes.

For these processes to occur smoothly, proteins must be properly folded into specific three-dimensional shapes. And you thought origami was hard?

However, cellular stressors themselves can cause proteins to misfold or denature, leading to dysfunction and potential cellular damage.

Cellular damage is an inevitable part of life, but our cells have a repair and defense system that relies heavily on HSPs.

This is where HSPs step in. They act as molecular chaperones, guiding proteins through the folding process, preventing misfolding, and aiding in the refolding of denatured proteins. This critical function ensures that essential cellular processes continue to function optimally, even under adverse conditions.

Additionally, HSPs play a crucial role in protein quality control. They help identify and remove damaged or misfolded proteins, preventing the accumulation of toxic protein aggregates that can disrupt cellular function and lead to diseases such as Alzheimer’s and Parkinson’s.

In essence, heat shock proteins act as cellular “paramedics,” swiftly responding to the scene of cellular stress or damage, facilitating repairs, and maintaining the integrity and functionality of the cell.

Who would have known that the body has a fire brigade, an ambulance service and a team of electricians and plumbers sitting around ready to respond to emergencies.

You don’t call 911, or 999 or 111 (depending on where you live) – to access the emergency number in your body you simply need to get hot – a fever, and inflammation or a trip to the Far-Infrared Heat Therapy Center.

HSPs Science

For the scientifically minded here is a rundown on the families of HSPs – each family has dozens of different little workers who get out there and roll their sleeves up and fix the broken bits.

• HSP70 Family: HSP70 proteins are among the most extensively studied heat shock proteins. They play a central role in protein folding, refolding, and cellular protection. They are involved in preventing protein aggregation and promoting the breakdown of damaged proteins.
• HSP40 (or DNAJ) family: They act as co-chaperones to the HSP70 family and play essential roles in protein folding and translocation.
• HSP90 Family: HSP90 proteins assist in the folding and stabilization of specific client proteins that are crucial for cell growth and survival. They are often involved in processes related to cancer and other diseases.
• HSP60 Family (Chaperonins): HSP60 proteins are found within cellular organelles called mitochondria. They assist in the folding of proteins critical for mitochondrial function and energy production.
• Small HSPs (sHSPs): These smaller heat shock proteins are involved in preventing protein aggregation and maintaining cell structure. They are particularly abundant in the eye lens, where they help maintain transparency.
• HSP100 family: These are involved in disaggregating proteins and are crucial for thermotolerance in some organisms.
• HSP110 family: This family functions both as chaperones and as nucleotide exchange factors for the HSP70s.

Each of these families can have multiple members with specific cellular locations and functions. Additionally, the naming convention based on molecular weight (e.g., HSP70 or HSP90) does not always strictly correspond to the actual molecular weight of the proteins but is more indicative of the family to which they belong.

This is one big family – its really more like a tribe – you need more than one turkey for dinner when this family comes together on Thanksgiving Day.

Each family of HSPs has unique functions and is induced in response to specific stressors, contributing to the cell’s overall ability to adapt and survive under adverse conditions.