Raw carnovire diet and hair loss
RAw carnivore diet for hair loss

COULD THE RAW CARNIVORE DIET HELP WITH HAIR LOSS?

The raw carnivore diet is the practice of eating only raw meat to drastically increase the amount of protein available to the body.  A carnivore diet is made up exclusively of animal foods, all nutritional needs are met without fruits, vegetables or starchy plant foods.  A raw carnivore diet takes the carnivore diet a step further to conserve the native structure of animal proteins.

Proteins serve many critical functions in the human body.  They act as antibodies, enzymes, messengers, transporters on the surface of the cell membrane.  Proteins also provide structural integrity to the skin, muscle, tissue, organs and the hair fibre.

Maintaining adequate protein levels within the body is crucial for essential biological activities such as regulation of gene expression, cell signalling and the maintenance of metabolic pathways that are essential for hair growth.

As meat is a great source of B-complex vitamins, protein and iron; could a raw carnivore diet reverse hair loss by increasing nutritional intake when compared to eating cooked meat?

RAW MEAT VS COOKED MEAT: NUTRIENT AVAILIBILTY

Meat is an excellent source of five of the B-complex vitamins: vitamin B1 (thiamine), vitamin B2 (riboflavin), vitamin B3 (niacin), vitamin B6 and vitamin B12.  B–complex vitamins are water soluble vitamins that tend to be sensitive to light and heat.  B vitamins are essential for normal metabolism and hair health. The cooking process markedly reduces the content of B vitamins in food.

Meat is also a great source of minerals and elements such as iron, phosphorus, selenium and zinc.  Iron is present as heme iron or non-heme iron in food, heme iron is easier to absorb than non-heme diet.  Plants contain non-heme iron and meat contains heme-iron.  A previous study carried out on heme iron concentration in meats showed that heat treatments did not cause losses in total iron content but modified the heme to non-heme iron ratio [1]. The heme iron concentration decreased depending on the severity of the heat treatment. As heme iron is easier to absorb, it represents some nutritional loss.

DOES EATING RAW MEAT INCREASE THE BIOAVAILABILITY OF PROTEIN?

Oxidation and subsequent protein aggregation, caused by the cooking process of meat, can lead to conformational changes in the meat that can lower the digestibility of protein in meat by digestive enzymes from 94% to 90% [2, 3].  The decrease of meat protein digestibility by cooking processes reduces the bioavailability of indispensable amino acids and increase the quantity of protein that reaches the large intestine to be fermented by bacteria in the colon.

The fermentation of these proteins by gut bacteria leads to the release of harmful metabolites such as ammonia, hydrogen disulphide and phenolic compounds.  These metabolites have a negative impact on the mucosa of the colon [4, 5, 6].  Cooking meat at a high temperature for a long time tends to result in an additional 1 gram of proteins reaching the colon for an intake of 25–30 grams of protein from meat [7].

PROTEIN USEAGE; ANABOLIC COMPETENCE AND LEAN BODY MASS

Whilst most individual amino are simply building blocks to make protein, some have several specific roles.  A limited availability of specific amino acids will also lead to a stimulation of lean muscle mass breakdown.   If muscles are continuously broken down, then there will eventually be a loss of lean body mass.

Lean muscle mass directly impacts the basal metabolic rate, a higher lean muscle mass equates to a higher metabolism and leads to faster hair growth.  A study of over 13,000 completed over a 6-year timeframe showed low levels of muscle mass also contributes to increased insulin resistance [8].   Insulin resistance is directly linked to androgenic alopecia has been due to higher circulation of DHT [9].

Lean muscle mass and hair growth

PROTEIN METABOLISM AND UTILISATION IN THE BODY

Hair follicles are extremely sensitive to metabolic changes, if the body moves out of an anabolic state, hair will cease to grow.  Protein is required for a paradigm known as “anabolic competence”, the body needs to remain in an anabolic state to keep all cells of the body growing, dividing and differentiating as they should.  When this competence is lost or affected by nutritional deficiencies the body will go into a catabolic state.  In a catabolic state the body will start to break down cells within the body as they become an energy source.

Cooking protein rich food increases the availability of certain nutrients and simultaneously decreases the availability of certain amino acids within the food we eat.  Specific amino acids important to hair, like methionine and cysteine, with a very reactive sulphydryl groups oxidise easily when exposed to heat or mechanical force.

PROTEIN USEAGE; ANABOLIC COMPETENCE AND LEAN BODY MASS

Lean muscle mass directly impacts the basal metabolic rate, a higher lean muscle mass equates to a higher metabolism and leads to faster hair growth.  Lean supports immune activity and contributes to strong bones, the Mediterranean Intensive Oxidant Study found that lower levels of skeletal muscle mass (a major component of lean muscle mass) was correlated with thinner bones.

A study of over 13,000 completed over a 6-year timeframe showed low levels of muscle mass also contributes to increased insulin resistance [2].  The research showed showed for every 10% increase in skeletal muscle mass, there was an 11% decrease in insulin resistance.  Insulin resistance has been linked to higher levels of circulating androgen and DHT levels.  Early androgenic alopecia has been shown to be an indicator of insulin resistance [3].

PROTEIN METABOLISM AND UTILISATION IN THE HAIR FOLLICLE

The utilisation of proteins refers to the amount of ingested protein that can be digested and used in the body for protein synthesis.  To maintain adequate levels regular intake of protein is essential.

When a meal containing protein is consumed, the dietary proteins are broken down into constituent amino acids by digestive enzymes, after this point they are available for the building of proteins.

There is no way for the body to store proteins or amino acids, there is a tightly regulated pool of around 100 grams in cells and the blood stream.  This pool is maintained by the continuous breaking down and building of proteins within cells.  This pool can respond quickly to changes in demands of the cell, if the cell needs more protein than is available in the cell.

The cell can also respond to a limited availability of specific amino acids for  the production of all non-essential proteins like the keratin needed for hair growth. Keratin is a unique protein due to its high sulphur content, if sulphur containing amino acids are low in availability will cease.

It is likely there is an inherent hierarchy that allows reduction of keratin formation in the hair fibre before there is a reduction in the keratin fibre that make up the skin and nails.  If the cell does not have enough amino acids to make the protein it need it will instantly halt production until that amino acid is available.

Hair loss and cysteine sulphur group

MALABSORPTION OF SULPHUR CONTAINING AMINO ACIDS

The heating of methionine and cysteine leads to excessive cross-linking that eventually leads to some protein aggregates.  For a protein to be absorbed it must first be broken down by digestive enzymes into its constituent amino acids.

The strong sulphur-sulphur crosslinking prevents enzyme breakdown of protein aggregates, leading to a lower absorption or sulphur containing proteins and an increased amount of sulphur entities in the digestive tract.

The oxidation of proteins intrinsically lowers the nutritional value and specifically lowers the absorbability of amino acids crucial for detoxification process and the building of keratinous structures like the hair and skin.

Protein oxidation and cysteine linked to hair loss
Protein oxidation and cysteine linked to hair loss

SULPHUR IS ESSENTIAL FOR KERATIN SYNTHESIS

Although all amino acids can be modified by reactive oxidative species, cysteine and methionine are the most susceptible to oxidative changes due to high reaction susceptibility of the sulphur group in this amino acid. Cysteine and methionine have very reactive sulfhydryl group side chains, this puts them in special position that cannot be replaced or substituted by any other amino acid.

SULPHUR SUPPLEMENTATION INCREASES CYSTEINE LEVELS FOR THICKER HAIR

Cysteine is the main amino acid in nails, skin, and hair and it is especially important in the creation of collagen and other soft tissue structures such as the gut. Cysteine, because of disulphide bridges, plays very important role in stabilization of all protein structures. With cysteine being the most susceptible to strong sulphur to sulphur cross-linking that cannot be broken down by digestive enzymes, it naturally follows that there will be a reduced ability to absorb cysteine.

In cases of hair loss, adding sulphur to the diet can offset the effect of protein oxidation caused by cooking, by providing an alternative source of sulphur that can be incorporated into cysteine during protein manufacture by cells.

THE FINAL WORD

Meat is highly nutritious, but the body as a biological system, requires other nutrients not found in raw meat.  A moderate version of this diet including high quality meat, fresh sashimi and ceviche as well as plenty of fresh fruit and vegetables would be more beneficial for hair growth in the long term.  When cooking meat, avoid frying and excessively high temperatures.  For overall health, lowering the intake of processed meat would be of great benefit.

REFERENCES

  1. Aspects of meat quality: trace elements and B vitamins in raw and cooked meats. Journal of food Composition and Analysis18(1), pp.39-46.
  2. Compared with raw bovine meat, boiling but not grilling, barbecuing, or roasting decreases protein digestibility without any major consequences for intestinal mucosa in rats, although the daily ingestion of bovine meat induces histologic modifications in the colon. The Journal of nutrition146(8), pp.1506-1513.
  3. High true ileal digestibility but not postprandial utilization of nitrogen from bovine meat protein in humans is moderately decreased by high-temperature, long-duration cooking. The Journal of nutrition145(10), pp.2221-2228.
  4. Effects of amino acid-derived luminal metabolites on the colonic epithelium and physiopathological consequences. Amino acids33(4), pp.547-562.
  5. Influence of dietary protein supplements on the formation of bacterial metabolites in the colon. Gut41(1), pp.70-76.
  6. Protein degradation in the large intestine: relevance to colorectal cancer. Current issues in intestinal microbiology1(2), pp.51-58.
  7. High true ileal digestibility but not postprandial utilization of nitrogen from bovine meat protein in humans is moderately decreased by high-temperature, long-duration cooking. The Journal of nutrition145(10), pp.2221-2228.
  8. Relative muscle mass is inversely associated with insulin resistance and prediabetes. Findings from the third National Health and Nutrition Examination Survey. The Journal of Clinical Endocrinology & Metabolism96(9), pp.2898-2903.
  9. Early androgenetic alopecia as a marker of insulin resistance. The Lancet356(9236), pp.1165-1166.