What Type of Collagen Do I Need?

Types of Collagen:

There are numerous types of collagen found in the body, and, numerous amino collagen supplements on the market. When it comes to choosing a collagen supplement, you should first know what part of the body you want to benefit.

1. Type I Collagen
   Skin, hair, nails, organs, bone, ligaments.
2. Type II Collagen
   Cartilage and joints.
3. Type III Collagen
   Gut and organs.

For skin and beauty (i.e. anti-aging), Type I Collagen is considered to be the best.

Research in dermatology has shown that when type I collagen is increased, the results are visible in the skin. (see Collagen Supplement Studies below)

Related: Benefits of Collagen Supplements

Sources of Collagen:

Dietary collagen is available from the following sources:

• Marine (fish)
  • PROS: Marie collagen peptides, from fish skins, are considered to be superior in raising overall body collagen (Type 1) and improving skin, hair, nail, and bone quality for a number of reasons. More about marine collagen. (2)
  • CONS: Wild caught fish collagen peptides generally cost more than other sources of collagen.
• Bovine (cow)
  • PROS: Bovine collagen peptides are usually lower cost, and can provide good results. These comprise a wide array of collagen supplements on the market due to the high accessibility of of bovine materials.
  • CONS: Lower absorption makes bovine collagen less effective than marine collagens. Also, bovine collagen comes with higher risk depending on how the cows were raised. For this reason, we only recommend products from grass fed cows.
• Porcine (pig)
  
  • PROS: Like bovine products, pig collagen peptides are usually lower cost, and comprise a wide array of collagen supplements on the market due to the high accessibility of of porcine materials.
  • CONS: For the same reasons as bovine, including some individuals have personal or religious restraints pertaining to pig products.
• Fowl (chicken)
  • PROS: Chicken collagen peptides are known to be most effective for supporting cartilage in the body. For this reason, type II collagen supplements are usually derived from chicken.
  • CONS: Not considered effective at raising overall body collagen levels, or as an ingredient in a beauty supplement.

Supporting Nutrients:

• What to Look For:
  • Vitamin C
    Vitamin C plays a critical role in collagen synthesis.⁽⁹⁾. When taken orally, as well as applied topically, it activates the body's own mechanisms for producing collagen.
  • Hyaluronic Acid
    HA is shown to have a durable effect to retain moisture in the skin from inside the body.⁽¹⁰⁾ In a double-blind, 4 week study, individuals who added hyaluronic acid to their diet showed significant reductions in skin dryness, wrinkles, and improvements in skin moisture and fullness.
    (Asethetic Dermatology Vol.12 :109~120, 2002)
    Read about HA on Amazon
• What to Avoid:
  • Collagen supplements with fillers (i.e. maltodextrin), flavors or sugars, oils, artificial ingredients, and unnecessary ingredients should be avoided. Basically, read the label to make your judgment.
  • Branched-Chain Amino Acids, while effective with aiding recovey from muscle trauma, will not offer significant benefit in raising overall body collagen (Type 1).⁽⁷⁾

Because of the dramatic "anti-aging" results, we consider that Vitamin C and Hyaluronic Acid are absolutely integral ingredients for maximizing the benefits of a collagen supplement.

While other ingredients, such as, CoQ10, glucosamine, and arginine may be beneficial on their own, the inclusion of these low-value ingredients in a collagen supplement may add a lot of cost relative to the benefit they can provide in the formula itself.

While most dietary collagen taken on a daily basis can benefit your health, not all collagen supplements will bring maximum results for beauty. Knowing the types of collagen, sources of collagen, and supporting ingredients of these supplements will help you make an informed decision when it comes to choosing the right supplement.

See the Comparison Guide below.

Product Comparison Guide

The following comparison values may help you make your decision when choosing a collagen supplement. Since there are too many collagen supplements to list them all, we have comprised a chart which includes the main supplements of interest (rated 4 stars or higher). The information above can help guide your decision for other collagen supplements which are not listed on this chart.
(Information on this chart deemed accurate as of October 2013 based on online research)

DISCLAIMER: Prices are based on published MSRP (as of: Oct 2018). Pros and Con, and opinions herein, are the opinions of Elavonne experts and their conclusions based on provided scientific and dermatologic research. Reviews are excerpts found on manufacturer or distributor websites from verified purchases.

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Vital Proteins Marine Collagen

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Cites and References

1. Iwal K., Hasegawa T., Taguchi Y., et al., (2006) Identification of food-derived collagen peptides in human blood after oral ingestion of gelatin hydrolysates. J Agric Food Chem 53: 6531-6535

2. J Pept Sci. 2010 Nov;16(11):652-8. doi: 10.1002/psc.1277. Elastin peptides prepared from piscine and mammalian elastic tissues inhibit collagen-induced platelet aggregation and stimulate migration and proliferation of human skin fibroblasts. Shiratsuchi E, Ura M, Nakaba M, Maeda I, Okamoto K.

EXCERPT: We obtained pure elastin peptides from bovine ligamentum nuchae, porcine aorta, and bonito bulbus arteriosus. The inhibitory activity of these elastin peptides on platelet aggregation induced by collagen and the migratory and proliferative responsivenesses of human skinfibroblasts to these elastin peptides were examined. All of bonito, bovine, and porcine elastin peptides found to inhibit platelet aggregation, but bonito elastin peptides showed a higher inhibitory activity than bovine and porcine elastin peptides did. All elastin peptides enhanced the proliferation of fibroblasts 3.5- to 4.5-fold at a concentration of 10 µg/ml. Bovine and porcine elastin peptides stimulated the migration of fibroblasts, with the optimal response occurring at 10(-1) µg/ml, while maximal response was at 10(2) µg/ml for bonito elastin peptides. Furthermore, pretreatment of fibroblasts by lactose depressed their ability to migrate in response to all elastin peptides, suggesting the involvement of elastin receptor in cell response. These results suggest that both mammalian and piscine elastin peptides can be applied as useful biomaterials in which elasticity, antithrombotic property, and the enhancement of cell migration and proliferation are required.

3. Hitoshi Matsumoto, et al., (2006) Clinical effects of fish type I collagen hydrolysate on skin properties. ITE Letters on batteries, new technologies and medicine, 7 (4)

4. Matsuda, et al., (2006) Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis. J Nutri Sci Vitaminol 52: 211-215

5. "Exercise Promotes BCAA Catabolism: Effects of BCAA Supplementation on Skeletal Muscle during Exercise". J. Nutr. 134 (6): 1583S–1587S. 2004. Retrieved 22 March 2011.

6. Therapeutic use of branched-chain amino acids in burn, trauma, and sepsis". J. Nutr. 1 Suppl 136 (30): 8S–13S. 2006. Retrieved 22 March 2011.

7. Karlsson HK, Nilsson PA, Nilsson J, Chibalin AV, Zierath JR, Blomstrand E (2004). "Branched-chain amino acids increase p70S6k phosphorylation in human skeletal muscle after resistance exercise". Am. J. Physiol. Endocrinol. Metab. 287 (1): E1–7. doi:10.1152/ajpendo.00430.2003.

8. Blomstrand E, Eliasson J, Karlsson HK, Köhnke R (2006). "Branched-chain amino acids activate key enzymes in protein synthesis after physical exercise". J. Nutr. 136(1 Suppl): 269S–73S.

9. Int J Cosmet Sci. 1998 Jun;20(3):151-8. doi: 10.1046/j.1467-2494.1998.171747.x. Effect of vitamin C and its derivatives on collagen synthesis and cross-linking by normal human fibroblasts. Boyera N, Galey I, Bernard BA.

10. Kajimoto O, Odanaka W, Sakamoto W, Yoshida K, Takahashi T.: Clinical Effects of Hyaluronic acid diet for dry skin. J. New Rem & Clin: 90-102, 2001.