The idea that fasting may have some effect on cancer cells in the body is not new. Ancient cultures went through periods without a single morsel of food for a number of days, and those periods often coincided with periods of high mortality from cancer. A number of studies have been performed looking at fasting as a treatment for cancer, with conflicting outcomes.

It’s called the “immortal body” for a reason, and it’s easy to forget that our bodies are more than just a fleshy collection of cells. We do have a body, but it’s also a system that houses all of the systems that we depend on, including our brain. This is why the topic of fasting and cellular cleansing comes up on many health forums. After all, if we think of our body as an immortal being, then we’d want it to remain healthy as long as possible.

Note – If you’re a regular reader, you know that I like to label my blogs by topic – for example, there are about 40 posts on fasting, about 30 posts on diabetes, about 50 posts on obesity/calories. I do this because I blog about what interests me at the moment, and that may change. This new section on mTOR, autophagy and mitochondrial diseases, which you will see later, is very closely linked to cancer development.

Throughout history, fasting has been one of the most important traditional methods for health and healing. This is true for virtually every region of the world and for virtually every religion in the world. The roots of this ancient healing tradition may lie in a subcellular autophagic cleansing process that science is only now beginning to discover. Autophagy is one of the most evolutionarily conserved metabolic pathways known to date and is observed in almost all multicellular organisms and in many unicellular organisms. Autophagy is the response of the organism to the absence of food (starvation), which stimulates the breakdown of subcellular components.

When the cell digests its own parts, it does two things. First, it removes excess proteins that may be damaged or not functioning properly. It then recycles these amino acid parts into new cell components. This is one of the biggest misconceptions about normal protein turnover, namely that these broken down proteins are somehow flushed out of the body, even in total malnutrition. This leads to hysterical complaints that starvation burns the muscles. OMG. If you don’t eat 96 meals a day, you will wither and die! Die! Your body stores food energy as fat, but as soon as you don’t eat, you burn muscle. You will die.

In fact, our bodies are not as stupid as they pretend to be. Once the old proteins are broken down to their constituent amino acids, our bodies decide whether to excrete these proteins as waste through the kidneys or leave them to make new proteins. Proteins are made up of building blocks called amino acids. It’s like Lego. You can take apart your old, strangely shaped Lego airplane and build a new, more powerful one with the same bricks. This also applies to our bodies. We can break down an old rotten protein into its individual amino acids and build a new, more functional protein from it.

Yoshinori Osumi, winner of the 2016 Nobel Prize in Medicine for his research on autophagy, titled his Nobel lecture Autophagy – Intracellular Processing System, not Autophagy – How the human body flushes much-needed proteins down the toilet because Mother Nature is very, very stupid. When you need protein, your body repairs broken down amino acids to make new proteins.

If your body has ingested more protein than it needs, it can naturally excrete the excess amino acids or convert them into energy. While most people think size is always good, the truth is that for adults, size is almost always a bad thing. Cancer is too much growth. Alzheimer’s disease is the accumulation of too many unhealthy proteins (neurofibrillary tubes) in the brain. Heart attacks and strokes are caused by atherosclerotic plaques. It is an excessive accumulation of many elements, but especially smooth muscle cells, connective tissue and degenerative material. Yes. Too much smooth muscle growth contributes to the development of atherosclerosis, which causes heart attacks. Polycystic kidneys and ovaries, for example, are the result of too much growth. Obesity is increasing too much.

What affects autophagy?

Certain forms of cellular stress, including nutrient deficiency, aggregation or unfolding of proteins (protein accumulation), or infection, activate autophagy to counteract these problems and keep the cell in good condition. Initially, this process was thought to have no distinguishing effect, but later it was shown to selectively attack damaged organelles (subcellular components) and invading pathogens. This process has been described in mammals, but also in insects and yeast, and much of Dr. Osumi’s work has focused on autophagy-related genes (ATGs). He confirmed that this purification and recycling pathway exists for most life forms on Earth, from single-celled organisms to humans.

Autophagy occurs at a low basal level in almost all cells and plays an important role in protein and organelle changes. However, it can be grown for its nutrients and energy. In other words, if needed, protein can be burned for energy as part of the gluconeogenesis process. Nutritional status, hormones, temperature, oxidative stress, infections and protein aggregates can affect autophagy in different ways.

The main regulator of autophagy is the target kinase rapamycin (TOR). It is also called mammalian TOR (mTOR) or mechanistic TOR. When mTOR is high, it blocks autophagy. mTOR is highly sensitive to dietary amino acids (proteins).

The other important regulator is the 5′ AMP-activated protein kinase (AMPK). It is a sensor of intracellular energy known as adenosine triphosphate or ATP. When a cell stores a lot of energy, it has a lot of ATP, which is a type of energy currency. If you have a lot of dollars, you’re rich. If you have lots of ATP, your cell has lots of energy to do something.

AMPK determines the ratio of AMP/ATP, and when this ratio is low (low cellular energy), AMPK is activated. Low cellular energy = high AMPK, so sort of a reverse fuel indicator of cellular energy status. When AMPK is elevated (in need of fuel), it blocks fatty acid synthesis and activates autophagy. That makes sense. When your cells don’t have enough energy, they don’t want to store energy (create fat) and instead activate autophagy, which means they get rid of excess protein and potentially burn it for energy.

Once autophagy is activated (decrease in mTOR or increase in AMPK), about twenty genes (ATGs) are activated to carry out the cleaning process. They code for the proteins that carry out the actual process. Since mTOR is a potent inhibitor of autophagy (mTOR acts as an inhibitor of autophagy), blocking mTOR increases autophagy (i.e. takes the foot off the brake). The drug rapamycin, first used as an immuno-blocker in transplantation, can be used for this purpose. This drug was discovered in 1972, isolated from the Streptomyces Hygroscopicus bacteria from Easter Island, also known as Rapa Nui (hence the name Rapamycin). It was developed as an antifungal agent, but it was found to have immunosuppressive properties, so it was used as an anti-rejection agent.

Almost all anti-rejection drugs increase the risk of cancer. The immune system goes out like a sentinel looking for cancer cells and destroys them, day after day. These cells are not called natural killer cells for nothing. If you destroy the sentinels with powerful anti-reactive drugs, the cancer can spread like crazy. And that’s exactly what happens with most of these drugs.

But not rapamycin. Interestingly, this drug reduced the risk of cancer. The mechanism of action was virtually unknown when it was widely introduced in the 1990s. Eventually the target of rapamycin (TOR) was identified using yeast models, and shortly thereafter a human analogue was discovered – hence the mammalian TOR, which now goes by the catchy name mTOR.

mTOR is present in virtually all multicellular organisms and also in many unicellular organisms such as yeast (where most of the research on autophagy is conducted). This protein is so important for survival that no living organism can live without it. The technical term for this is conserved by evolution. What’s he doing? Simply put, it’s a power sensor.

One of the most important tasks for survival is the sequestration of available nutrients in the environment and the growth of the cell or organism. In other words, if there is no food, the cells must stop growing and go into a dormant state (like yeast). When mammals have too little food, they also stop the excessive growth of their cells and begin to break down certain proteins. If you haven’t done it, you haven’t survived.

mTOR integrates signals between nutrition (nutrient availability) and cell growth. If there is food, grow it. If there is no food, you will stop growing. This is an essential task that is at the root of all the overgrowth diseases we have already discussed. It’s similar to, but much older than, the other food sensor we’ve talked a lot about, insulin.

But this knowledge opens up a whole new therapeutic potential. If there are many diseases with excessive growth (cancer, atherosclerosis, obesity, polycystic ovary disease), we have a new goal. If we can turn off the food sensors, we can stop much of this growth that makes us sick. A new era is dawning.

Dr. Jason Fung

Would you like to know more about Dr. Fung’s work? Here are his most popular posts about cancer:

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