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.  The cooking of meat includes the production of reactive oxygen species (ROS) that induce the oxidation of proteins leading to a reduction in protein digestibility and to the formation of amino acid–derived metabolites.

Undigested proteins in the intestines are fermented by gut bacteria and are able to generate compounds that are potentially harmful to the mucosa of the gut.

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

POTENTIAL BENEFITS OF THE RAW CARNIVORE DIET ON HEALTH

Meat is high in protein and fat content is satiating and generally, research supports the efficacy of low-carb diets, like keto and paleo type diets, in weight loss over and above the high-carb diets (1)(2).

A previous study carried out on heme iron concentration in meats (3) showed that heat treatments did not cause losses in total iron content but modified the heme to non-heme iron ratio. 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.

Native protein - raw meat diet

Native and functional protein that has not been exposed to heat. Can be degraded and digested by proteases in the small intestine (15).

Unfolded protein - raw meat diet

Heated and moderately oxidised protein with no activity. Completely unfolded protein.  Digestibility by proteases is increased (15).

raw 3

Heavily oxidised protein aggregate (no activity). Protein aggregates larger than 4 kDa will become resistant to digestion by proteases due to increased crosslinking and massive aggregation (15).

DOES EATING RAW MEAT INCREASE THE BIOAVAILABILITY OF PROTEIN?

Oxidation and subsequant protein aggregation, caused by the cooking process of meat, can lead to conformational changes in the meat that can lower the digestibilty of the protein in meat by digestive enzymes (4) from 94% to 90% (5).

The conformational changes are due oxidised sulfer containing amino acids (e.g cystiene). Oxidation and aggregation can lead to the reduced bioavailability of amino acids such as cysteine; adequate cysteine intake is crucial to healthy hair.

The decrease of meat protein digestibility by cooking processes may not only reduce the bioavailability of indispensable amino acids but also increase the quantity of protein that reaches the large intestine to be femented by bacteria in the colon.

Periodically, the fermentaion of these proteins leads to the release of harmful metabolites such as ammonia, hydrogen disulfide and phenolic compounds.

These metabolites have a negatove impact on the mucosa of the colon (6)(7)(8).  This impact is thought to be involved in the potential role of preocessed and red meat intake in the risk of corectal cancer (9)(10)(11).   The relationship between ccooked meat and colon cancer has been hotly debated (12).

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 (13).

THE FINAL WORD

Meat is highly nutritious but the body as a biological system requires other nutrients such as potassium.  Fibre, which is lacking in this diet, supports the bacterial population of the gastro-intestinal system.

A moderate version of the diet including high quality meat (that has not beeked cooked at high temperatures, fried or overcooked), fresh sashimi and ceviche as well as plenty of fresh fruit and veg will be more beneficial for hair growth.

REFERENCES

  1. Bazzano, L.A., Hu, T., Reynolds, K., Yao, L., Bunol, C., Liu, Y., Chen, C.S., Klag, M.J., Whelton, P.K. and He, J., 2014. Effects of low-carbohydrate and low-fat diets: a randomized trial. Annals of internal medicine, 161(5), pp.309-318.

  2. Boden, G., Sargrad, K., Homko, C., Mozzoli, M. and Stein, T.P., 2005. Effect of a low-carbohydrate diet on appetite, blood glucose levels, and insulin resistance in obese patients with type 2 diabetes. Annals of internal medicine, 142(6), pp.403-411.
  3. Lombardi-Boccia, G., Lanzi, S. and Aguzzi, A., 2005. Aspects of meat quality: trace elements and B vitamins in raw and cooked meats. Journal of food Composition and Analysis, 18(1), pp.39-46.

  4. Oberli, M., Lan, A., Khodorova, N., Santé-Lhoutellier, V., Walker, F., Piedcoq, J., Davila, A.M., Blachier, F., Tomé, D., Fromentin, G. and Gaudichon, C., 2016. 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 nutrition, 146(8), pp.1506-1513.

  5. Oberli, M., Marsset-Baglieri, A., Airinei, G., Santé-Lhoutellier, V., Khodorova, N., Rémond, D., Foucault-Simonin, A., Piedcoq, J., Tomé, D., Fromentin, G. and Benamouzig, R., 2015. 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 nutrition, 145(10), pp.2221-2228.
  6. Blachier, F., Mariotti, F., Huneau, J.F. and Tomé, D., 2007. Effects of amino acid-derived luminal metabolites on the colonic epithelium and physiopathological consequences. Amino acids, 33(4), pp.547-562.
  7. Geypens, B.A., Claus, D., Evenepoel, P., Hiele, M., Maes, B., Peeters, M., Rutgeerts, P. and Ghoos, Y., 1997. Influence of dietary protein supplements on the formation of bacterial metabolites in the colon. Gut, 41(1), pp.70-76.
  8. Hughes, R., Magee, E.A.M. and Bingham, S., 2000. Protein degradation in the large intestine: relevance to colorectal cancer. Current issues in intestinal microbiology, 1(2), pp.51-58.
  9. Pan, A., Sun, Q., Bernstein, A.M., Schulze, M.B., Manson, J.E., Stampfer, M.J., Willett, W.C. and Hu, F.B., 2012. Red meat consumption and mortality: results from 2 prospective cohort studies. Archives of internal medicine, 172(7), pp.555-563.
  10. Aune D, Chan DS, Vieira AR, Rosenblatt DA, Vieira R, Greenwood DC, Kampman E, Norat T. Red and processed meat intake and risk of colorectal adenomas: a systematic review and meta-analysis of epidemiological studies. Cancer causes & control. 2013 Apr 1;24(4):611-27.
  11. Rohrmann, S., Overvad, K., Bueno-de-Mesquita, H.B., Jakobsen, M.U., Egeberg, R., Tjønneland, A., Nailler, L., Boutron-Ruault, M.C., Clavel-Chapelon, F., Krogh, V. and Palli, D., 2013. Meat consumption and mortality-results from the European Prospective Investigation into Cancer and Nutrition. BMC medicine, 11(1), p.63.
  12. Tabatabaei, S.M., Fritschi, L., Knuiman, M.W., Boyle, T., Iacopetta, B.J., Platell, C. and Heyworth, J.S., 2011. Meat consumption and cooking practices and the risk of colorectal cancer. European journal of clinical nutrition, 65(6), pp.668-675.
  13. Oberli, M., Marsset-Baglieri, A., Airinei, G., Santé-Lhoutellier, V., Khodorova, N., Rémond, D., Foucault-Simonin, A., Piedcoq, J., Tomé, D., Fromentin, G. and Benamouzig, R., 2015. 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 nutrition, 145(10), pp.2221-2228.
  14. Popova, T. and Marinova, P., 2013. Lipid and protein oxidation during cooking in meat of lambs reared indoors and on pasture. Bulg J Agric Sci, 19, pp.590-4.
  15. Jung, T., Höhn, A. and Grune, T., 2014. The proteasome and the degradation of oxidized proteins: Part II–protein oxidation and proteasomal degradation. Redox biology, 2, pp.99-104.

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