Collagen: The Forgotten Superfood

A revival of ancient wisdom

braised diced pork

For thousands of years, collagen-rich foods supported human health around the globe. Broth, high in gelatin (cooked collagen) from long-simmered connective tissue, has a history dating back to the Paleolithic era. [1] Traditional dishes like boiled fish heads, Scottish haggis, head cheese, jellied pigs feet, Mexican menudo, French consommé, and various forms of aspic (meat jelly) served as staples in regional cuisines, utilizing collagen-rich animal parts to form unique and nutritious specialty foods.

green salad with a large gelatin mold in the center

Collagen even enjoyed a revival in midcentury America, when gelatin-based dishes took potlucks, dinner parties, and formal events by storm. A quick flip through vintage cookbooks and homemaking magazines reveals long-forgotten uses of this food—ranging from elaborate desserts to jiggly salads to meat-filled Jell-O molds.

Today, traditional sources of collagen have largely fallen by the wayside. In contrast to the nose-to-tail eating that characterized much of human history, muscle meat is now favored over cartilage-filled animal parts like tendons, skin, tail, hocks, trotters, tripe, ears, and various other offal. Broths brewed with bones or collagen-rich meat cuts—once used even in commercial soups—are often replaced with mixtures of isolated vegetable protein, MSG, and starch to mimic the texture of gelatin. While it’s unclear why this has become so common, we can only speculate that it allows food manufacturers to cut costs through the use of cheap ingredients.

Campbell_ox_tail_soup_ad

And while nutrition discourse often focuses on the problematic foods we’re eating more of, less discussed are the nourishing ingredients that have been disappearing from the menu—including collagen!

What is collagen?

Collagen is the most abundant protein in the human body. In fact, it makes up about 30% of the body’s total protein content. [2] Found predominantly in connective tissues like skin, bones, tendons, and ligaments, collagen acts as a scaffold that helps maintain the integrity and structure of these tissues. [3] [4]

Collagen is made up of long, intertwined chains of amino acids—primarily glycine, proline, and hydroxyproline. These chains form a triple helix structure, giving collagen its unique strength and resilience. [5]

Dozens of different types of collagen exist, each characterized by their molecular arrangement. But these 3 are most prevalent in human tissue:

What happens when we consume collagen?

woman running outside

Our bodies can’t absorb collagen in its whole form. Instead, our digestive system breaks it down into smaller pieces that can then be used to build our own collagen, as well as perform other important activities. These pieces include short protein fragments (amino acid strings) called bioactive peptides, as well as single amino acids.

Collagen peptides have well-studied benefits. These protein fragments interact with biological systems in ways that individual amino acids cannot, giving them unique functions and health effects. [11]

graphical drawing of human anatomy

For example, collagen peptides trigger the synthesis of extracellular matrix proteins, which form a supportive network outside of cells in tissues—akin to the “glue” that holds everything together in our bodies. [12] [13] Various collagen-derived peptides can also:

The amino acids in collagen have important biological roles as well! Glycine, for example, is particularly impressive, boasting effects such as:

When cooked, collagen breaks down into another protein called gelatin. While collagen and gelatin differ in their molecular structure, they contain the same mixture of amino acids, and both supply bioactive peptides that contribute to their wide-ranging health effects. [24] [25] [26] [27] Gelatin has the additional perk of being highly bioavailable, due to already being partly broken down and ready for absorption. [28]

An ancient food meets modern science

Today, we have a wealth of studies demonstrating the benefits of dietary collagen. Randomized controlled trials—the gold standard for scientific research—have shown that boosting our collagen intake can:

x ray of hand and arm with a fractured bone

How much collagen do we need?

In general, supplementing with 2.5 - 10 g of collagen daily produces significant, measurable benefits in studies. [46] [29] 15 g of collagen per day appears most helpful for increasing muscle mass and strength, especially in conjunction with resistance training. [29] Keep in mind, these amounts are in addition to the collagen from meat, poultry, and seafood already present in the average diet, which ranges from about 3 to 23 g. [47]

However, the optimal amount of collagen varies based on our individual circumstances. Extra collagen could be particularly helpful during times of increased bone or cartilage loss, such as from:

man in mountainous landscape jumping from one large rock to another

Factors like sun exposure, smoking, and air pollution can likewise deplete collagen levels, potentially raising our requirements for dietary collagen and its precursors. [51] [52] [53] [54] In addition, vitamin C, vitamin D, iron, copper, zinc, and silicon play important roles in collagen synthesis, and insufficient intakes can inhibit the body’s collagen production. [55] [56] [57] [58] [59] [60] [61] [62]

Our body’s natural collagen production also declines as we age, contributing to visible signs of aging (such as wrinkles and sagging skin) and physical impairments (such as joint pain and decreased mobility). [63] As a result, dietary collagen may help support healthy aging, and becomes increasingly beneficial as we get older. [29]

older adult woman next to phone showing image of a baby with a similar pose

Restoring collagen’s place at the table

Thanks to renewed interest in collagen and its benefits, collagen supplements are now widely available—sold under terms like “collagen peptides,” “hydrolyzed collagen,” or “collagen protein.” These are derived from animal parts like beef hide or fish scales, which are then processed into bioavailable collagen powders.

However, collagen supplements aren’t the only way to boost our collagen intake! In fact, consuming collagen from whole-food sources has the advantage of supplying additional nutrients, including those required for collagen production. Arginine, ornithine, and glutamine, abundant in many animal foods, also increase collagen synthesis by serving as precursors for the amino acids in collagen. [64] [65] [66] So, by consuming collagen as part of its natural food matrix (rather than as an isolated dietary supplement), we’re supporting collagen production in an even more powerful way.

barbecued ribs showing a mix of lean and fatty meat

That brings the question: how can we add collagen-rich foods to our modern diet? Some of the best sources include:

Bone broth has become particularly popular in recent years, with surging interest in its health benefits and versatility. And while it indeed contains collagen precursors (along with valuable nutrients like calcium and potassium), it can be difficult to obtain enough collagen from bone broth alone to receive maximum health benefits. [67] As a result, it’s helpful to include diverse collagen sources in your diet.

Roasted Chicken Soup on table

True Primal soups are packed with collagen not only from delicious bone broth, but also from additional grass-fed beef gelatin. In fact, each serving of soup contains more collagen than most supplements—at least 8 grams, which is over 3 times the amount shown to have anti-aging and joint pain-relieving benefits in human trials. [68] [69] Our chicken soups also use meat with skin, supplying additional collagen from connective tissue.

Incorporating collagen-rich foods into our diets is more than just a trend: it’s a return to a lost pillar of health, backed by both science and centuries of culinary tradition. True Primal soups are a delicious way to bring this superfood back to the table!


References

  1. Kosečková P, Zvěřina O, Letková K. Nutritional insights into broths in relation to elemental composition. Eur Food Res Technol. 2024 May 4; 250:2545-2551. doi: 10.1007/s00217-024-04556-2.
  2. Ricard-Blum S. The collagen family. Cold Spring Harb Perspect Biol. 2011 Jan 1;3(1):a004978. doi: 10.1101/cshperspect.a004978.
  3. Ricard-Blum S. The collagen family. Cold Spring Harb Perspect Biol. 2011 Jan 1;3(1):a004978. doi: 10.1101/cshperspect.a004978.
  4. Li P, Wu G. Roles of dietary glycine, proline, and hydroxyproline in collagen synthesis and animal growth. Amino Acids. 2018 Jan;50(1):29-38. doi: 10.1007/s00726-017-2490-6.
  5. Shenoy M, Abdul NS, Qamar Z, Bahri BMA, Al Ghalayini KZK, Kakti A. Collagen Structure, Synthesis, and Its Applications: A Systematic Review. Cureus. 2022 May 9;14(5):e24856. doi: 10.7759/cureus.24856.
  6. Naomi R, Ridzuan PM, Bahari H. Current Insights into Collagen Type I. Polymers (Basel). 2021 Aug 9;13(16):2642. doi: 10.3390/polym13162642.
  7. Wallace JM, Chen Q, Fang M, Erickson B, Orr BG, Banaszak Holl MM. Type I collagen exists as a distribution of nanoscale morphologies in teeth, bones and tendons. Langmuir. 2010 May 18;26(10):7349-54. doi: 10.1021/la100006a.
  8. Wu Z, Korntner SH, Mullen AM, Zeugolis DI. Collagen type II: From biosynthesis to advanced biomaterials for cartilage engineering. Biomater Biosyst. 2021 Nov 22;4:100030. doi: 10.1016/j.bbiosy.2021.100030.
  9. Kuivaniemi H, Tromp G. Type III collagen (COL3A1): Gene and protein structure, tissue distribution, and associated diseases. Gene. 2019 Jul 30;707:151-171. doi: 10.1016/j.gene.2019.05.003.
  10. Lovell CR, Smolenski KA, Duance VC, Light ND, Young S, Dyson M. Type I and III collagen content and fibre distribution in normal human skin during ageing. Br J Dermatol. 1987 Oct;117(4):419-28. doi: 10.1111/j.1365-2133.1987.tb04921.x.
  11. Zaky AA, Simal-Gandara J, Eun JB, Shim JH, Abd El-Aty AM. Bioactivities, Applications, Safety, and Health Benefits of Bioactive Peptides From Food and By-Products: A Review. Front Nutr. 2022 Jan 20;8:815640. doi: 10.3389/fnut.2021.815640.
  12. Zague V, do Amaral JB, Rezende Teixeira P, de Oliveira Niero EL, Lauand C, Machado-Santelli GM. Collagen peptides modulate the metabolism of extracellular matrix by human dermal fibroblasts derived from sun-protected and sun-exposed body sites. Cell Biol Int. 2018 Jan;42(1):95-104. doi: 10.1002/cbin.10872.
  13. Dierckx S, Patrizi M, Merino M, González S, Mullor JL, Nergiz-Unal R. Collagen peptides affect collagen synthesis and the expression of collagen, elastin, and versican genes in cultured human dermal fibroblasts. Front Med (Lausanne). 2024 May 1;11:1397517. doi: 10.3389/fmed.2024.1397517.
  14. Xing L, Fu L, Cao S, Yin Y, Wei L, Zhang W. The Anti-Inflammatory Effect of Bovine Bone-Gelatin-Derived Peptides in LPS-Induced RAW264.7 Macrophages Cells and Dextran Sulfate Sodium-Induced C57BL/6 Mice. Nutrients. 2022 Apr 1;14(7):1479. doi: 10.3390/nu14071479.
  15. Cadar E, Pesterau AM, Prasacu I, Ionescu AM, Pascale C, Dragan AL, Sirbu R, Tomescu CL. Marine Antioxidants from Marine Collagen and Collagen Peptides with Nutraceuticals Applications: A Review. Antioxidants (Basel). 2024 Jul 29;13(8):919. doi: 10.3390/antiox13080919.
  16. Chen X, Xia P, Zheng S, Li Y, Fang J, Ma Z, Zhang L, Zhang X, Hao L, Zhang H. Antioxidant Peptides from the Collagen of Antler Ossified Tissue and Their Protective Effects against H2O2-Induced Oxidative Damage toward HaCaT Cells. Molecules. 2023 Sep 30;28(19):6887. doi: 10.3390/molecules28196887.
  17. Balshaw TG, Funnell MP, McDermott E, Maden-Wilkinson TM, Abela S, Quteishat B, Edsey M, James LJ, Folland JP. The effect of specific bioactive collagen peptides on function and muscle remodeling during human resistance training. Acta Physiol (Oxf). 2023 Feb;237(2):e13903. doi: 10.1111/apha.13903. Epub 2022 Dec 13. Erratum in: Acta Physiol (Oxf). 2023 Apr;237(4):e13952. doi: 10.1111/apha.13952.
  18. Honvo G, Lengelé L, Charles A, Reginster JY, Bruyère O. Role of Collagen Derivatives in Osteoarthritis and Cartilage Repair: A Systematic Scoping Review With Evidence Mapping. Rheumatol Ther. 2020 Dec;7(4):703-740. doi: 10.1007/s40744-020-00240-5.
  19. Zdzieblik D, Oesser S, König D. Specific Bioactive Collagen Peptides in Osteopenia and Osteoporosis: Long-Term Observation in Postmenopausal Women. J Bone Metab. 2021 Aug;28(3):207-213. doi: 10.11005/jbm.2021.28.3.207. Epub 2021 Aug 31.
  20. Abrahams M, O'Grady R, Prawitt J. Effect of a Daily Collagen Peptide Supplement on Digestive Symptoms in Healthy Women: 2-Phase Mixed Methods Study. JMIR Form Res. 2022 May 31;6(5):e36339. doi: 10.2196/36339.
  21. Chen Q, Chen O, Martins IM, Hou H, Zhao X, Blumberg JB, Li B. Collagen peptides ameliorate intestinal epithelial barrier dysfunction in immunostimulatory Caco-2 cell monolayers via enhancing tight junctions. Food Funct. 2017 Mar 22;8(3):1144-1151. doi: 10.1039/c6fo01347c.
  22. Razak MA, Begum PS, Viswanath B, Rajagopal S. Multifarious Beneficial Effect of Nonessential Amino Acid, Glycine: A Review. Oxid Med Cell Longev. 2017;2017:1716701. doi: 10.1155/2017/1716701. Epub 2017 Mar 1. Erratum in: Oxid Med Cell Longev. 2022 Feb 23;2022:9857645. doi: 10.1155/2022/9857645.
  23. Aguayo-Cerón KA, Sánchez-Muñoz F, Gutierrez-Rojas RA, Acevedo-Villavicencio LN, Flores-Zarate AV, Huang F, Giacoman-Martinez A, Villafaña S, Romero-Nava R. Glycine: The Smallest Anti-Inflammatory Micronutrient. Int J Mol Sci. 2023 Jul 8;24(14):11236. doi: 10.3390/ijms241411236.
  24. Ho TJ, Lin JH, Lin SZ, Tsai WT, Wu JR, Chen HP. Isolation, Identification, and Characterization of Bioactive Peptides in Human Bone Cells from Tortoiseshell and Deer Antler Gelatin. Int J Mol Sci. 2023 Jan 16;24(2):1759. doi: 10.3390/ijms24021759.
  25. Lassoued I, Mora L, Barkia A, Aristoy MC, Nasri M, Toldrá F. Bioactive peptides identified in thornback ray skin's gelatin hydrolysates by proteases from Bacillus subtilis and Bacillus amyloliquefaciens. J Proteomics. 2015 Oct 14;128:8-17. doi: 10.1016/j.jprot.2015.06.016.
  26. Wang L, Wang X, Bai F, Fang Y, Wang J, Gao R. The anti-skin-aging effect of oral administration of gelatin from the swim bladder of Amur sturgeon (Acipenser schrenckii). Food Funct. 2019 Jul 17;10(7):3890-3897. doi: 10.1039/c9fo00661c.
  27. Xing L, Fu L, Cao S, Yin Y, Wei L, Zhang W. The Anti-Inflammatory Effect of Bovine Bone-Gelatin-Derived Peptides in LPS-Induced RAW264.7 Macrophages Cells and Dextran Sulfate Sodium-Induced C57BL/6 Mice. Nutrients. 2022 Apr 1;14(7):1479. doi: 10.3390/nu14071479.
  28. Wang L, Wang Q, Liang Q, He Y, Wang Z, He S, Xu J, Ma H. Determination of bioavailability and identification of collagen peptide in blood after oral ingestion of gelatin. J Sci Food Agric. 2015 Oct;95(13):2712-7. doi: 10.1002/jsfa.7008.
  29. Campos LD, Santos Junior VA, Pimentel JD, Carregã GLF, Cazarin CBB. Collagen supplementation in skin and orthopedic diseases: A review of the literature. Heliyon. 2023 Mar 28;9(4):e14961. doi: 10.1016/j.heliyon.2023.e14961.
  30. König D, Oesser S, Scharla S, Zdzieblik D, Gollhofer A. Specific Collagen Peptides Improve Bone Mineral Density and Bone Markers in Postmenopausal Women—A Randomized Controlled Study. Nutrients. 2018 Jan 16;10(1):97. doi: 10.3390/nu10010097.
  31. Lugo JP, Saiyed ZM, Lau FC, Molina JP, Pakdaman MN, Shamie AN, Udani JK. Undenatured type II collagen (UC-II®) for joint support: a randomized, double-blind, placebo-controlled study in healthy volunteers. J Int Soc Sports Nutr. 2013 Oct 24;10(1):48. doi: 10.1186/1550-2783-10-48.
  32. Martínez-Puig D, Costa-Larrión E, Rubio-Rodríguez N, Gálvez-Martín P. Collagen Supplementation for Joint Health: The Link between Composition and Scientific Knowledge. Nutrients. 2023 Mar 8;15(6):1332. doi: 10.3390/nu15061332.
  33. García-Coronado JM, Martínez-Olvera L, Elizondo-Omaña RE, Acosta-Olivo CA, Vilchez-Cavazos F, Simental-Mendía LE, Simental-Mendía M. Effect of collagen supplementation on osteoarthritis symptoms: a meta-analysis of randomized placebo-controlled trials. Int Orthop. 2019 Mar;43(3):531-538. doi: 10.1007/s00264-018-4211-5.
  34. Lin CR, Tsai SHL, Huang KY, Tsai PA, Chou H, Chang SH. Analgesic efficacy of collagen peptide in knee osteoarthritis: a meta-analysis of randomized controlled trials. J Orthop Surg Res. 2023 Sep 16;18(1):694. doi: 10.1186/s13018-023-04182-w.
  35. Reilly DM, Kynaston L, Naseem S, Proudman E, Laceby D. A Clinical Trial Shows Improvement in Skin Collagen, Hydration, Elasticity, Wrinkles, Scalp, and Hair Condition following 12-Week Oral Intake of a Supplement Containing Hydrolysed Collagen. Dermatol Res Pract. 2024 Jul 10;2024:8752787. doi: 10.1155/2024/8752787.
  36. Zdzieblik D, Oesser S, Baumstark MW, Gollhofer A, König D. Collagen peptide supplementation in combination with resistance training improves body composition and increases muscle strength in elderly sarcopenic men: a randomised controlled trial. Br J Nutr. 2015 Oct 28;114(8):1237-45. doi: 10.1017/S0007114515002810.
  37. Park J, Kim M, Shin H, Ahn H, Park YK. Low-Molecular Collagen Peptide Supplementation and Body Fat Mass in Adults Aged ≥ 50 Years: A Randomized, Double-Blind, Placebo-Controlled Trial. Clin Nutr Res. 2023 Oct 31;12(4):245-256. doi: 10.7762/cnr.2023.12.4.245.
  38. Jendricke P, Centner C, Zdzieblik D, Gollhofer A, König D. Specific Collagen Peptides in Combination with Resistance Training Improve Body Composition and Regional Muscle Strength in Premenopausal Women: A Randomized Controlled Trial. Nutrients. 2019 Apr 20;11(4):892. doi: 10.3390/nu11040892.
  39. Kouguchi T, Ohmori T, Shimizu M, Takahata Y, Maeyama Y, Suzuki T, Morimatsu F, Tanabe S. Effects of a chicken collagen hydrolysate on the circulation system in subjects with mild hypertension or high-normal blood pressure. Biosci Biotechnol Biochem. 2013;77(4):691-6. doi: 10.1271/bbb.120718.
  40. Jalili Z, Jalili F, Moradi S, Bagheri R, Moosavian SP, Naeini F, Mohammadi H, Mojtaba Ghoreishy S, Wong A, Travica N, Hojjati Kermani MA, Jalili C. Effects of collagen peptide supplementation on cardiovascular markers: a systematic review and meta-analysis of randomised, placebo-controlled trials. Br J Nutr. 2023 Mar 14;129(5):779-794. doi: 10.1017/S0007114522001301.
  41. Tomosugi N, Yamamoto S, Takeuchi M, Yonekura H, Ishigaki Y, Numata N, Katsuda S, Sakai Y. Effect of Collagen Tripeptide on Atherosclerosis in Healthy Humans. J Atheroscler Thromb. 2017 May 1;24(5):530-538. doi: 10.5551/jat.36293.
  42. Clark KL, Sebastianelli W, Flechsenhar KR, Aukermann DF, Meza F, Millard RL, Deitch JR, Sherbondy PS, Albert A. 24-Week study on the use of collagen hydrolysate as a dietary supplement in athletes with activity-related joint pain. Curr Med Res Opin. 2008 May;24(5):1485-96. doi: 10.1185/030079908x291967.
  43. Praet SFE, Purdam CR, Welvaert M, Vlahovich N, Lovell G, Burke LM, Gaida JE, Manzanero S, Hughes D, Waddington G. Oral Supplementation of Specific Collagen Peptides Combined with Calf-Strengthening Exercises Enhances Function and Reduces Pain in Achilles Tendinopathy Patients. Nutrients. 2019 Jan 2;11(1):76. doi: 10.3390/nu11010076.
  44. Kuwaba K, Kusubata M, Taga Y, Igarashi H, Nakazato K, Mizuno K. Dietary collagen peptides alleviate exercise-induced muscle soreness in healthy middle-aged males: a randomized double-blinded crossover clinical trial. J Int Soc Sports Nutr. 2023 Dec;20(1):2206392. doi: 10.1080/15502783.2023.2206392.
  45. Clifford T, Ventress M, Allerton DM, Stansfield S, Tang JCY, Fraser WD, Vanhoecke B, Prawitt J, Stevenson E. The effects of collagen peptides on muscle damage, inflammation and bone turnover following exercise: a randomized, controlled trial. Amino Acids. 2019 Apr;51(4):691-704. doi: 10.1007/s00726-019-02706-5.
  46. Choi FD, Sung CT, Juhasz ML, Mesinkovsk NA. Oral Collagen Supplementation: A Systematic Review of Dermatological Applications. J Drugs Dermatol. 2019 Jan 1;18(1):9-16. PMID: 30681787.
  47. Paul C, Leser S, Oesser S. Significant Amounts of Functional Collagen Peptides Can Be Incorporated in the Diet While Maintaining Indispensable Amino Acid Balance. Nutrients. 2019 May 15;11(5):1079. doi: 10.3390/nu11051079.
  48. Calleja-Agius J, Brincat M. The effect of menopause on the skin and other connective tissues. Gynecol Endocrinol. 2012 Apr;28(4):273-7. doi: 10.3109/09513590.2011.613970.
  49. Bagheri Miyab K, Alipoor E, Vaghardoost R, Saberi Isfeedvajani M, Yaseri M, Djafarian K, Hosseinzadeh-Attar MJ. The effect of a hydrolyzed collagen-based supplement on wound healing in patients with burn: A randomized double-blind pilot clinical trial. Burns. 2020 Feb;46(1):156-163. doi: 10.1016/j.burns.2019.02.015.
  50. Ouyang Z, Dong L, Yao F, Wang K, Chen Y, Li S, Zhou R, Zhao Y, Hu W. Cartilage-Related Collagens in Osteoarthritis and Rheumatoid Arthritis: From Pathogenesis to Therapeutics. Int J Mol Sci. 2023 Jun 7;24(12):9841. doi: 10.3390/ijms24129841.
  51. Jariashvili K, Madhan B, Brodsky B, Kuchava A, Namicheishvili L, Metreveli N. UV damage of collagen: insights from model collagen peptides. Biopolymers. 2012 Mar;97(3):189-98. doi: 10.1002/bip.21725.
  52. Yamauchi M, Prisayanh P, Haque Z, Woodley DT. Collagen cross-linking in sun-exposed and unexposed sites of aged human skin. J Invest Dermatol. 1991 Nov;97(5):938-41. doi: 10.1111/1523-1747.ep12491727.
  53. Knuutinen A, Kokkonen N, Risteli J, Vähäkangas K, Kallioinen M, Salo T, Sorsa T, Oikarinen A. Smoking affects collagen synthesis and extracellular matrix turnover in human skin. Br J Dermatol. 2002 Apr;146(4):588-94. doi: 10.1046/j.1365-2133.2002.04694.x.
  54. Fussell JC, Kelly FJ. Oxidative contribution of air pollution to extrinsic skin ageing. Free Radic Biol Med. 2020 May 1;151:111-122. doi: 10.1016/j.freeradbiomed.2019.11.038.
  55. Pinnel SR, Murad S, Darr D. Induction of collagen synthesis by ascorbic acid. A possible mechanism. Arch Dermatol. 1987 Dec;123(12):1684-6. doi: 10.1001/archderm.123.12.1684.
  56. Boyera N, Galey I, Bernard BA. Effect of vitamin C and its derivatives on collagen synthesis and cross-linking by normal human fibroblasts. Int J Cosmet Sci. 1998 Jun;20(3):151-8. doi: 10.1046/j.1467-2494.1998.171747.x.
  57. Li S, Niu G, Wu Y, Du G, Huang C, Yin X, Liu Z, Song C, Leng H. Vitamin D prevents articular cartilage erosion by regulating collagen II turnover through TGF-β1 in ovariectomized rats. Osteoarthritis Cartilage. 2016 Feb;24(2):345-53. doi: 10.1016/j.joca.2015.08.013.
  58. Schwartz Z, Schlader DL, Ramirez V, Kennedy MB, Boyan BD. Effects of vitamin D metabolites on collagen production and cell proliferation of growth zone and resting zone cartilage cells in vitro. J Bone Miner Res. 1989 Apr;4(2):199-207. doi: 10.1002/jbmr.5650040211.
  59. O'Dell BL. Roles for iron and copper in connective tissue biosynthesis. Philos Trans R Soc Lond B Biol Sci. 1981 Aug 14;294(1071):91-104. doi: 10.1098/rstb.1981.0091.
  60. Molenda M, Kolmas J. The Role of Zinc in Bone Tissue Health and Regeneration-a Review. Biol Trace Elem Res. 2023 Dec;201(12):5640-5651. doi: 10.1007/s12011-023-03631-1.
  61. Harris ED, Rayton JK, Balthrop JE, DiSilvestro RA, Garcia-de-Quevedo M. Copper and the synthesis of elastin and collagen. Ciba Found Symp. 1980;79:163-82. doi: 10.1002/9780470720622.ch9.
  62. Pritchard A, Nielsen BD. Silicon Supplementation for Bone Health: An Umbrella Review Attempting to Translate from Animals to Humans. Nutrients. 2024 Jan 24;16(3):339. doi: 10.3390/nu16030339.
  63. Marcos-Garcés V, Molina Aguilar P, Bea Serrano C, García Bustos V, Benavent Seguí J, Ferrández Izquierdo A, Ruiz-Saurí A. Age-related dermal collagen changes during development, maturation and ageing – a morphometric and comparative study. J Anat. 2014 Jul;225(1):98-108. doi: 10.1111/joa.12186.
  64. Barbul A, Lazarou SA, Efron DT, Wasserkrug HL, Efron G. Arginine enhances wound healing and lymphocyte immune responses in humans. Surgery. 1990 Aug;108(2):331-6; discussion 336-7.
  65. Shi HP, Fishel RS, Efron DT, Williams JZ, Fishel MH, Barbul A. Effect of supplemental ornithine on wound healing. J Surg Res. 2002 Aug;106(2):299-302. doi: 10.1006/jsre.2002.6471.
  66. Karna E, Miltyk W, Wołczyński S, Pałka JA. The potential mechanism for glutamine-induced collagen biosynthesis in cultured human skin fibroblasts. Comp Biochem Physiol B Biochem Mol Biol. 2001 Aug;130(1):23-32. doi: 10.1016/s1096-4959(01)00400-6.
  67. Alcock RD, Shaw GC, Burke LM. Bone Broth Unlikely to Provide Reliable Concentrations of Collagen Precursors Compared With Supplemental Sources of Collagen Used in Collagen Research. Int J Sport Nutr Exerc Metab. 2019 May 1;29(3):265-272. doi: 10.1123/ijsnem.2018-0139.
  68. Pu SY, Huang YL, Pu CM, Kang YN, Hoang KD, Chen KH, Chen C. Effects of Oral Collagen for Skin Anti-Aging: A Systematic Review and Meta-Analysis. Nutrients. 2023 Apr 26;15(9):2080. doi: 10.3390/nu15092080.
  69. ​​Devasia S, Joseph JT, P S S, Koizumi S, Clarke L, V T S, Kailas AP, Madhavan S. Management and Amelioration of Knee Joint Osteoarthritis in Adults Using a Novel High-Functional Bovine Collagen Peptide as a Nutritional Therapy: A Double-Blind, Prospective, Multicentric, Randomized, Active and Placebo Controlled, Five-Arm, Clinical Study to Evaluate the Efficacy, Safety, and Tolerability. Cartilage. 2024 Jan 18:19476035231221211. doi: 10.1177/19476035231221211.

Published , by .