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- What are proteins and amino acids?
- What do proteins do?
- How Proteins and Amino Acids Work
- The formation of amino acids plays a major role in the following systems and processes:
- Proteins and Amino Acids in the Oncology Landscape
- Special Attention: Bone Broth, Gelatin and Glutamine
- Specific Amino Acid Targets in Conventional Oncology
Macronutrients, Part 1: Amino Acids.
Requirements for Cancer Prevention and Management
What are proteins and amino acids?
Amino acids are molecules that link up to create proteins. Proteins are chains of amino acids that serve a particular function depending on what sequence they form. There are some 50,000 different proteins in the body. Dietary proteins are broken down in the course of digestion into amino acids, which reassemble into new proteins to suit the body’s specific needs.
What do proteins do?
Protein function includes:
- building material for growth and repair
- enzymes
- hormones
- antibodies
- transporters
- fluid balance regulators
- acid-base regulators
- sources of energy
How Proteins and Amino Acids Work
Cells are constantly in the process of synthesizing huge numbers of proteins, which go on to form other cells, which combine to form tissues and organs. The instructions for each protein are contained inside the nucleus of every cell in the form of DNA.
There are twenty different amino acids in the body that combine to make all of the different protein formations. The liver produces about 60% of the necessary amino acids, while the other 40% must be obtained from the diet. If any amino acids are missing from dietary intake, the body will break down its own tissue to make up for the shortage.
Amino acids fall into two main categories: essential and non-essential.
The essential group is comprised of nine amino acids that must come from our diet, and thenonessential group is comprised of eleven that are synthesized by the liver. The production of certain nonessential amino acids may be hindered by impaired physiological processes, such as imbalances in the microbiome or the depletion of certain vitamin or mineral cofactors. When this occurs, it creates aconditionally essential amino acid.
There are twenty different amino acids in the body that combine to make all of the different protein formations. The liver produces about 60% of the necessary amino acids, while the other 40% must be obtained from the diet. If any amino acids are missing from dietary intake, the body will break down its own tissue to make up for the shortage.
Amino acids fall into two main categories: essential and non-essential.
The essential group is comprised of nine amino acids that must come from our diet, and thenonessential group is comprised of eleven that are synthesized by the liver. The production of certain nonessential amino acids may be hindered by impaired physiological processes, such as imbalances in the microbiome or the depletion of certain vitamin or mineral cofactors. When this occurs, it creates aconditionally essential amino acid.
A conditionally essential amino acid is a nonessential amino acid that becomes essential because it is reliant on an amino acid precursor. For example, the body uses the essential amino acid phenylamine to synthesize the nonessential amino acid tyrosine. If the diet fails to offer enough phenylamine, or the body cannot make the conversion, then tyrosine becomes an essential amino acid that must be consumed in the diet.
Essential: Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine.
Nonessential: Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic acid, Glutamine, Glycine, Proline, Serine, Tyrosine.
Potentially conditionally essential: Arginine, Cysteine, Glutamine, Glycine, Proline, Serine, Tyrosine.
Essential: Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine.
Nonessential: Alanine, Arginine, Asparagine, Aspartic Acid, Cysteine, Glutamic acid, Glutamine, Glycine, Proline, Serine, Tyrosine.
Potentially conditionally essential: Arginine, Cysteine, Glutamine, Glycine, Proline, Serine, Tyrosine.
The formation of amino acids plays a major role in the following systems and processes:
- Immune system: production of antibodies, cytokines and other cytotoxic substances; cellular redox state; gene expression; lymphocyte proliferation; and other cell actions.
- DNA: in order to repair DNA damage, all 9 amino acids are required.
- Endocrine system (hormones): insulin and glucagon to regulate blood glucose; calcitonin and parathyroid hormone to regulate calcium levels; antidiuretic hormone to regulate fluid and electrolyte balance.
- Detoxification: liver detoxification phase 1 (generation of water-soluble intermediaries) and phase 2 (neutralization of toxic water-soluble intermediaries).
Proteins come in complete and incomplete forms. Complete proteins come from foods containing all nine essential amino acids. Sources of complete proteins include animal products, such as meat, fish, dairy, and eggs. Incomplete proteins come from foods that are missing one or more essential amino acids. These include plant foods, such as nuts, seeds, legumes, vegetables, and grains. In order to get a complete protein panel in a vegetarian diet, plant-based foods must be combined (e.g. rice and beans).
Legumes typically contain amino acids like isoleucine and lysine, and grains contain the amino acids methionine and tryptophan. This may be problematic for someone with cancer as it greatly increases carbohydrate levels and caloric intake, which is in direct opposition to the typical anticancerrecommendation of a low-glycemic, calorie-restricted, and/or ketogenic diet.
Proteins and Amino Acids in the Oncology Landscape:
What to Avoid, What to Focus On, and Why
When it comes to animal protein and supporting cancer treatment, there are five basic rules.
Steroid hormone drugs - including synthetic estrogen, progesterone and testosterone - are regularly used in non-organic cattle and sheep to fatten up the animals. The hormone residue in meat from these sources may lead to hormone imbalance in people who consume it, and potentially contribute to the development of breast, prostate, and colon cancers. The usage of antibiotics in non-organic animals also leads to antibiotic-resistant pathogens in animals and humans. Low-quality, genetically modified meat that is processed with additives can become carcinogenic. It has been linked to stomach, colorectal, and esophageal cancers. Animal products not only have to be organic, but also pasture-raised and wild in order to have higher Omega-3s, CLA, Vitamin E, and Vitamin D naturally.
Following biological rhythms when it comes to animal meat includes consuming it when it is fresh and sustainable. For example, eggs are best to consume during springtime; chicken and fish during summer; wild poultry and beef during fall; and wild game and shellfish during winter.
Balanced protein consumption must include muscle meats, organ meats, and gelatinous material from bones and connective tissue. However, the modern diet is dominated by muscle meat, and includes little organ meat or connective tissue. The result is that the methionine-rich muscle meats we consume are not able to fulfill their cellular functions, and instead produce toxic byproducts, leading to chronic disease and reduced lifespan.
Muscle meats are low in vitamins, minerals, and methyl cofactors (B12, Folate, B6, niacin and riboflavin), which are necessary for the methylation process. When the amino acid methionine is paired with its cofactors, it supports the growth and repair of tissues, antioxidant defense, detoxification, and cellular communication.
Once methylation has occurred, the body uses vitamin B6 and glycine to convert the extra methionine into glutathione, a powerful antioxidant. For this conversion, glycine (from bones and connective tissue), choline (from liver and egg yolks), and betaine (from spinach and beets) are needed to buffer the conversion.
Large doses of methionine, which is mostly found in muscle meat, will drain the body of glycine, choline ,and betaine. Eating muscle meats, organ meats, connective tissue, bone, and skin is a way to balance methionine’s important functions. Organ meats and connective tissue are generally higher on the vitamin and mineral spectrum.
Connective tissue such as cartilage is another powerful protein, since it has an immune-boosting effect and antimitotic properties (i.e. it inhibits the division of cancer cells, but not healthy cells). Consuming cartilage increases the number of macrophages that stimulate necrosis factor alpha, which causes the death of tumor cells. Cartilage also improves the immune system by activating immune system cells, including T-cells, B-cells, IgA, IgC, IgM, and NK.
Muscle meats are low in vitamins, minerals, and methyl cofactors (B12, Folate, B6, niacin and riboflavin), which are necessary for the methylation process. When the amino acid methionine is paired with its cofactors, it supports the growth and repair of tissues, antioxidant defense, detoxification, and cellular communication.
Once methylation has occurred, the body uses vitamin B6 and glycine to convert the extra methionine into glutathione, a powerful antioxidant. For this conversion, glycine (from bones and connective tissue), choline (from liver and egg yolks), and betaine (from spinach and beets) are needed to buffer the conversion.
Large doses of methionine, which is mostly found in muscle meat, will drain the body of glycine, choline ,and betaine. Eating muscle meats, organ meats, connective tissue, bone, and skin is a way to balance methionine’s important functions. Organ meats and connective tissue are generally higher on the vitamin and mineral spectrum.
Connective tissue such as cartilage is another powerful protein, since it has an immune-boosting effect and antimitotic properties (i.e. it inhibits the division of cancer cells, but not healthy cells). Consuming cartilage increases the number of macrophages that stimulate necrosis factor alpha, which causes the death of tumor cells. Cartilage also improves the immune system by activating immune system cells, including T-cells, B-cells, IgA, IgC, IgM, and NK.
Eating too much meat can have serious health consequences for patients with cancer. Amino acids are not just building blocks. In some cases, they act as nutrient signals that regulate important signaling pathways, such as the mTOR pathway that promotes cancer. The protein sensor mTOR monitors the body’s availability of proteins and amino acids for growth and reproduction. When protein levels exceed basic requirements, this up-regulates mTOR, stimulating cellular proliferation and adverse mitochondrial effects in the progression of cancer.
Too much protein can also stimulate gluconeogenesis in the body, which means that glucose is synthesized in the liver from non-carbohydrate sources, such as amino acids, lactate, or pyruvate. Most amino acids can be converted into glucose.
Excessive meat consumption in general can also be carcinogenic, especially given certain genetic factors that affect metabolism. Two genes to pay attention to are:
Too much protein can also stimulate gluconeogenesis in the body, which means that glucose is synthesized in the liver from non-carbohydrate sources, such as amino acids, lactate, or pyruvate. Most amino acids can be converted into glucose.
Excessive meat consumption in general can also be carcinogenic, especially given certain genetic factors that affect metabolism. Two genes to pay attention to are:
- ADIPOQ: Modulates numerous pathways related to fat storage and metabolism. Variants in this gene could result in a recommendation to decrease red meat intake as it may have significant prognostic value for colorectal cancer.
- ACAT-02: This gene is responsible for converting protein to fat to ATP in mitochondria and is important in cellular cholesterol homeostasis. Single nucleotide polymorphisms may indicate that more B vitamins are needed in order to metabolize dietary protein.
Cooking meat at temperatures over 300° F (~150° C) results in the formation of carcinogenic compounds, heterocyclic amines (HCAs), and polycyclic aromatic hydrocarbons, which damage DNA. The browning of meat forms advanced glycation endproducts (AGEs), which drain antioxidant stores and stimulate an inflammatory cascade.
There are a few foods that help to negate carcinogenic effects in meat, such as cruciferous vegetables. Eating cruciferous vegetables alongside meat protects against HCA mutagens. Taking chlorella before or with a meal containing HCAs also inhibits their mutagenic properties. Using rosemary and grapeseed gxtract in marinades inhibits HCA formation in fried beef patties.
Slow cooking methods include baking at low temperatures, braising, poaching, simmering, slow roasting, cooking in a crock pot, steaming, and stewing.
There are a few foods that help to negate carcinogenic effects in meat, such as cruciferous vegetables. Eating cruciferous vegetables alongside meat protects against HCA mutagens. Taking chlorella before or with a meal containing HCAs also inhibits their mutagenic properties. Using rosemary and grapeseed gxtract in marinades inhibits HCA formation in fried beef patties.
Slow cooking methods include baking at low temperatures, braising, poaching, simmering, slow roasting, cooking in a crock pot, steaming, and stewing.
Special Attention:
Bone Broth, Gelatin and Glutamine
Bone Broth improves overall digestion and assimilation, builds collagen and cartilage, and nourishesthe skin, joints, and bones.
Gelatin, the protein-rich principal constituent of the broth, is the denatured collagen that appears when bones are boiled. Gelatin is an incomplete protein, missing tryptophan and containing low amounts of cysteine, tyrosine, and histidine.
Gelatin, the protein-rich principal constituent of the broth, is the denatured collagen that appears when bones are boiled. Gelatin is an incomplete protein, missing tryptophan and containing low amounts of cysteine, tyrosine, and histidine.
Gelatin-rich bone broth must be consumed with other animal proteins in order to get a complete amino acid panel. Gelatin is a “protein sparer,” meaning it makes the body less likely to cannibalize the protein stores in its own muscles (as can happen in conditions like cachexia).
Homemade bone broths, consumed daily, are the best way to reap the health benefits of gelatin. The longer the broth is cooked (24 - 72 hours), the higher its amino acid panel will be.
Homemade bone broths, consumed daily, are the best way to reap the health benefits of gelatin. The longer the broth is cooked (24 - 72 hours), the higher its amino acid panel will be.
Glutamine, one of the amino acids in bone broth, has many important functions:
There is, however, a debate in the medical field concerning the inclusion of glutamine in an anticancer diet, with some research suggesting it should be avoided.
- Fuel source for enterocytes, lymphocytes and macrophages
- Enhancing gut integrity, immune function and protein synthesis
- Formation of glutathione
- Post-surgical support
- Reducing cachexia
- Decreasing chemotherapy and radiation side effects
There is, however, a debate in the medical field concerning the inclusion of glutamine in an anticancer diet, with some research suggesting it should be avoided.
Arguments for AVOIDING glutamine:
- It can fuel cancer growth. Glutamine assists rapidly dividing cells in their growth and development, so it may also promote the growth of cancer cells. Some studies have found that inhibiting glutamine’s cellular mechanism halts cancer growth.
- It can negate the effects of therapy. Glutamine increases the internal production of glutathione, a potent antioxidant, which could interfere with oxidative therapies such as radiation.
- It is the preferred fuel for some cancers. These include glioblastoma multiforme and pancreatic cancers.
Arguments for INCLUDING glutamine:
- It is essential. Glutamine, like water and oxygen, is a necessary external nutrient needed for all cells, and the body needs even more when fighting chronic illness.
- It supports survival rates of patients undergoing conventional therapy.
- It improves wellbeing. Glutamine may improve patient outcomes without increasing tumor growth.
Clinical studies on the role of nutritional glutamine in oncological treatment are still being carried out, and in the great majority, glutamine supplementation in patients with cancer improves host metabolism, as well as their clinical situation, without increasing tumor growth.
Many factors influence whether glutamine has positive or negative effects, such as dosage, timing, tumor type, nutritional intake, and the patient’s overall depletion of health.
Many factors influence whether glutamine has positive or negative effects, such as dosage, timing, tumor type, nutritional intake, and the patient’s overall depletion of health.
An article in Oxidative Medicine and Cellular Longevity (October 25, 2015), titled “Key Roles of Glutamine Pathways in Reprogramming the Cancer Metabolism” reported that the benefits of glutamine were most significant in the presence of “significant carbohydrate restrictions,” which reduce the use of the glutamine as a fuel for cancer cells.
In active cases, long term supplemental glutamine is contraindicated and should only be considered for short term acute GI repair or mitigation of side effects from treatment.
In active cases, long term supplemental glutamine is contraindicated and should only be considered for short term acute GI repair or mitigation of side effects from treatment.
Specific Amino Acid Targets in Conventional Oncology
New drugs are being developed that target and inhibit the metabolism of specific amino acids, including tryptophan, arginine, methionine, and glutamine.
Research on amino acid metabolism in cancer cells in the last decades has provided valuable insights into the potential impact of metabolic control and regulation on the tumor microenvironment. Amino acids are no longer regarded solely as building materials, but also as nutrient signals that regulate important signaling pathways.
Research on amino acid metabolism in cancer cells in the last decades has provided valuable insights into the potential impact of metabolic control and regulation on the tumor microenvironment. Amino acids are no longer regarded solely as building materials, but also as nutrient signals that regulate important signaling pathways.
Several amino acid metabolic enzymes are regulated by oncogenes and tumor suppression, and have been explored as targets for cancer therapies. Design and use of inhibitors targeting tryptophan, arginine and/or glutamine metabolism - either alone or in combination with anti-tumor drugs - has been introduced in clinical trials.
However, cancer and immune cells share similar requirements for amino acid metabolic enzymes, and often compete for the same nutrients. Therefore, therapeutic interventions in the tumor microenvironment must be cautiously explored in order to eliminate potential negative impacts on anti-tumor immunity. Understanding the underlying mechanisms of metabolic interplay between tumor and immune cells will provide new directions to manipulate the tumor microenvironment and unleash the anti-tumor immune response.
However, cancer and immune cells share similar requirements for amino acid metabolic enzymes, and often compete for the same nutrients. Therefore, therapeutic interventions in the tumor microenvironment must be cautiously explored in order to eliminate potential negative impacts on anti-tumor immunity. Understanding the underlying mechanisms of metabolic interplay between tumor and immune cells will provide new directions to manipulate the tumor microenvironment and unleash the anti-tumor immune response.
References
Ananieva, Elitsa. “Targeting Amino Acid Metabolism in Cancer Growth and Anti-Tumor Immune Response.” World Journal of Biological Chemistry, Baishideng Publishing Group Inc, 26 Nov. 2015.