Collagen Peptides powder

The most absorbable form of collagen is peptides which are ten times higher than regular collagen. Type 1 collagen.

Collagen supplements good for

Skin and hair

• It may decrease the depth of larger wrinkles and help remove small wrinkles                        
• It may increase hydration and firmness of the skin                                                                    
• Increases levels of collagen and elastin in the skin, providing   greater  elasticity        
• It might increase the measured level of haemoglobin in the skin, resulting, in better microcirculation
• It may reduce facial sebum and thus reduces the occurrence and  severity of acne
• It may enhance and speed hair growth resulting in thicker and  stronger hair                           
• It might reduce seborrhea (greasiness of hair) and decrease  dandruff                                     
• It might reduce androgenic thinning and hair loss (in both men and women)                 

Miscellaneous

• It may reduce joint pain                                                                                                            
• It may increase the efficacy of sleep (due to its glycine content)                                               
• It might increase learning abilities, memory and recall functions without stimulation (glycine)         
• Recent studies indicate it might increase in the production of new neural cells in the cerebrum   
• It may help to decrease appetite by balancing the hormones produced in the digestive system
• It might improve peripheral blood circulation (scalp and fingers)

Recommended consumption for adults: 10g (1 heaped tablespoon.) 1 or two times per day. It is best consumed with breakfast and/or before going to bed. It can be mixed into any kind of liquid, even into a hot soup. Its taste can be easily masked. A tasty drink can be made by mixing the product into warm water, milk or coconut milk, sweetened or flavoured with vanilla.

Collagen supplements are important as collagen proteins are almost totally absent from the modern western diet, as most of our protein sources are muscle meat and not the animal parts that contain lots of collagen (bones, skin, joints, etc.). Of course, as today we eat less and less tripe, aspic, bone stock, pig’s trotters and such. That is a big mistake! As the protein content of animal, bodies are also mostly collagens, and as the source of the protein intake of our ancestors and modern hunters-gatherers is almost exclusively of animal origin, it is only logical that a large majority of their protein supply should be collagen proteins. Our ancestors and modern hunters-gatherers did use every part of an animal, they did not just eat its meat. For me, it follows from the above that during our evolution we adapted for high consumption of collagen proteins: it is the healthy way of living for us. It is unusual for our body and should cause problems if only a small part of the consumed proteins are collagens. In the following, I will attempt to support this idea.

Caloric restriction (CR) results in a significant increase in the life span and a decrease in the risk of diseases in animals. This was easy to confirm in animals. They simply gave less food to the animals in the study and observed how long they lived compared to the control group and what the decrease was in the occurrence of diseases. Well, it is obviously hard to set up such an experiment for humans. Thus, in this case, researchers can only measure markers and reach some conclusions. The positive effects of CR on longevity and health is generally considered to result from the decrease of IGF-1 or inslin-like growth factor levels and the increase in IGFBP-3, with the latter being the protein that binds IGF-1 and thus neutralizing its negative effects. Only short term studies were conducted on human CR until 2008 (several weeks-months). These concluded that the levels of IGF-1 are reduced also in humans, thus CR appeared to be effective. However, the results of the first study on long term CR in humans were published in 2008. Here it was found that CR results in a lower IGF-1/IGFBP-3 ratio only for 3 months; afterwards the ratio increases. At the same time, the IGF-1/IGFBP-3 ratio remained low in the long term in the vegan group with high calorie and carbohydrate intake and low protein intake. Some members of the CR group were then asked to continue their CR diet while keeping their protein intake low, similar to that of the vegan group after their IGF-1/IGFBP-3 ratio returned to its original, high level. As a result, the ratio decreased again to the favourable level. The researchers concluded that, contrary to the findings in animal studies, CR will only result in an increased life span in humans if both their caloric and protein intake are restricted (~0.8 g protein/body weight kg).

Another study in 2012 found that a so-called mTORC protein complex is strongly and directly activated by BCAA amino acids, especially by leucine. These amino acids are only found in large amounts in milk proteins and meat. The increased activity of mTORC is a big problem as both IGF-1 and insulin exert their negative effects through this complex. The activity of mTORC is increased by IGF-1 and insulin as well. Thus it is harmful if they are present at high levels. Increased mTORC activity reduces life expectancy and increases the risk of lifestyle diseases. Today, medicinal products are being developed against cancer and cardiac attack based on the inhibition of mTORC activation. These researchers concluded that a palaeolithic type diet that lacks meat and is based on vegetables and complex carbohydrates would be the most appropriate.

Animal studies were conducted where researchers eliminated specific amino acids from the diet. Both the elimination of methionine and tryptophan resulted in a longer life span of animals, though they did not reduce caloric intake.

All this supports the importance of the predominance of collagen proteins. Why is that? As I have mentioned at the beginning of the article, collagen proteins hardly contain any of the problematic amino acids (BCAAs, tryptophan, methionine), while meat and milk proteins have plenty of them. Modern hunter-gatherers eat much more protein than the 0.8 g per body weight kilogram recommended by the 2008 study, and it is also impossible to follow a diet based almost solely on vegetables, proposed by the 2012 study. Such a low intake of proteins would be unhealthy anyway, resulting in muscle degradation, weakening of the immune system and indirectly in the reduction of bone density.

Collagen proteins, therefore, reduce the activity of mTORC and help decrease the levels of tryptophan and methionine. All this results in better health and longer life. What is more, a new study in 2014 may also suggest that even the level of IGF-1 can be reduced with collagen proteins without side effects, which in turn increases life expectancy.

Thus we can eat lots of protein, but be careful to provide only half of our intake from muscle meat, and the other half from animal parts with high collagen content (or with collagen supplements).

Let us see now what the direct supplementation of collagen is good for.
First, it is important to clarify that the normal edible gelatine (such as aspic) is made up of giant proteins, hardly digestible at all. Pre-digested (hydrolyzed) gelatine/collagen was used in each study (mostly in the form of a powder that can be mixed in drinks). These contain collagen peptides instead of intact proteins. There is no evidence if normal gelatine is effective or not.

Warnings

KEEP OUT OF REACH OF CHILDREN. DO NOT EXCEED RECOMMENDED DOSE.

If you are undergoing treatment for a medical condition or if you are pregnant or lactating, please consult your medical practitioner before introducing supplementary foods to your normal routine. The dietary supplement should not be used as a substitute for a varied and balanced diet or a healthy lifestyle. Store tightly closed in a cool and dry place.

Studies:
1. Sylvie Ricard-Blum: The Collagen Family. Cold Spring Harb Perspect Biol. 2011 Jan; 3(1): a004978.
2. Szpak, Paul (2011). "Fish bone chemistry and ultrastructure: implications for taphonomy and stable isotope analysis". Journal of Archaeological Science 38 (12): 3358–3372.
3. Fontana et al. (Long-term effects of calorie or protein restriction on serum IGF-1 and IGFBP-3 concentration in humans. Aging Cell. 2008 Oct; 7(5): 681–687.
4. Bodo Melnik: Dietary intervention in acne - Attenuation of increased mTORC1 signaling promoted by Western diet. Dermatoendocrinol. 2012 Jan 1; 4(1): 20–32.
5. Trepanowski et al.: Impact of caloric and dietary restriction regimens on markers of health and longevity in humans and animals: a summary of available findings. Nutrition Journal 2011, 10:107
6. C.Y. Ewald et al., “Dauer-independent inuln/IGF-1-signalling implicates collagen remodelling in longevity,” Nature, doi:10.1038/nature14021, 2014.
7. Proksch et al.: Oral intake of specific bioactive collagen peptides reduces skin wrinkles and increases dermal matrix synthesis. Skin Pharmacol Physiol. 2014;27(3):113-9.
8. Schwartz et al.: Ingestion of BioCell Collagen(®), a novel hydrolyzed chicken sternal cartilage extract; enhanced blood microcirculation and reduced facial aging signs . Clin Interv Aging. (2012)
9. Kantor, I et al. 2002. Results of a Study Evaluating the Use of a Dietary Supplement Formula in the Management of Age-Related Skin Changes in Women with Moderate to Severe Wrinkling of the Periorbital Area. Journal of the American 10. Nutraceutical Asscociation. Vol 5, No.2
11. DERMSCAN study, 2008, Lyon France. Cutaneous properties of hydrolyzed collagen
12. Ito et al.: Sebum secretion-blocking composition, and food or beverage containing same. US 8,969,523 B2 (2015 március 3.)
13. MorgantiP.,RandazzoS.D.,BrunoC,(1982)"effectofgelatincysteineonhairafterathreemonthstreatment“, J.Soc.Cosmet.Chemists33,95.
14. RandazzoS.D.,MorgantiP.,(1982)titled:"Theinfluenceofgelatincysteinesupplementationontheaminoacidscompositionofhumanhair",acceptedforpresentationonXVIintern.CongressofDermatology May23-28Tokyo.
15. Morganti P., Bruno C. Colelli G (1983) Geltina-cistina. Cheratogenesies trutturapilifcra Boil, Soc, It. Biol.Sper 59:20.
16. M.P. DE Padova, A. TOSTI, titled: “Gelatin -Cyctine in Seborrheic Alopecia”, department of dermatology university of Bologna –Italy, February 15, 1985. J Appl. Cosmetol 1968;4;55-60 (April/June 1986).
17. Morganti P., G. Fabrizl. B james, C. Bruno, titled: “Effect of gelatin-cystine and serenoa repens extract on free radicals level and hair growth”, Presented at Singapore clinical dermatology 2000 –Singapore 18-20 June, 1998
18. Pam Z., Wikonkal N., Pam N., -15th Annual Meeting of the European Hair Research Society (EHRS) , Jerusalem, Israel, July 6-9, 2011.
19. Benito-Ruiz et al.: A randomized controlled trial on the efficacy and safety of a food ingredient, collagen hydrolysate, for improving joint comfort. International Journal of Food Sciences and Nutrition, 2009, Vol. 60, No. s2 : Pages 99-113
20. Schauss et al.: Effect of the novel low molecular weight hydrolyzed chicken sternal cartilage extract, BioCell Collagen, on improving osteoarthritis-related symptoms: a randomized, double-blind, placebo-controlled trial. J Agric Food 21. Chem. 2012 Apr 25;60(16):4096-101.
22. Jing et al. 2014.
23. Bannai M, Kawai N. New therapeutic strategy for amino acid medicine: glycine improves the quality of sleep. J Pharmacol Sci. 2012;118(2):145-8.
24. File et al.: Beneficial effects of glycine (bioglycin) on memory and attention in young and middle-aged adults. J Clin Psychopharmacol. 1999 Dec;19(6):506-12.
25. Kakoi C. et al.: Collagen peptides enhance hippocampal neurogenesis and reduce anxiety related behavior in mice . Biomed Res. (2012)
26. Rubio et al.: Oral ingestion of a hydrolyzed gelatin meal in subjects with normal weight and in obese patients: Postprandial effect on circulating gut peptides, glucose and inuln. Eat Weight Disord. 2008 Mar;13(1):48-53.

27. THE SPECIFIC DYNAMIC ACTION OF GELATIN HYDROLYSATES by DAVID RAPPORT, From the Department of Physiology, Western Reserve University Medical School, Cleveland. Received for publication, October 8, 1926. Published the American Society 28. of Biological Chemists, Inc., Vol 71. p. 75-86 in English.