| Dietary sources | |
| Collagen is an animal protein contained in the cartilage, bones, skin and rind of domesticated and wild animals. Cooking these animal components dissolves collagen in water purified and dried collagen is known as “gelatine“. This is used to bind various creams and mousses or for jelly and aspic. | |
| Physiological effects | |
| Connective tissue |
|
| Native Collagen (Type II) in degenerative joint diseases |
| Combination preparations are gaining ground in the nutritional therapy of degenerative joint diseases. Besides glucosamine, chondroitin and hyaluronic acid, native collagen has moved into the focus of the scientific community.1 Native collagen (type II) is an essential component of cartilage tissue. Only native type II collagen has the special triple helix required for tear-resistant collagen fibers. As a catalyst, native collagen (type II) also stabilizes tendons and connective tissue. In contrast to chondroitin and glucosamine, which act slowly, native collagen (type II) exhibits a clear improvement of all parameters after only 90 days of use. Among other effects, oral administration led to a 33 % reduction on the WOMAC scale.2 In a study of 40 knee osteoarthritis patients, the combination of native collagen (type II) and Boswellia serrata resulted in a significant reduction in pain, stiffness and improvement in physical function.3 |
| Collagen type I for degenerative tendon diseases |
| Type I collagen is mainly responsible for the structure and loading capacity of the tendon. Over 95% of the collagen of the tendons is collagen type I.3 The intake of collagen type I induces a significant increase in collagen fibril diameter and also alters the mucopolysaccharide composition in the extracellular region of the tenocytes, resulting in improved tendon function.4 |
| Copper - Cofactor of connective tissue synthesis |
| Copper status probably also plays a role in joint inflammation. Lower copper values are associated with an increased incidence of inflammation. In addition, copper deficiency impairs collagen and elastin metabolism.5 The copper-containing enzyme lysyl oxidase is essential for the formation and cross-linking of collagen and elastin, which is why a copper deficit can lead to connective tissue disorders. For the optimal effect of collagen, sufficient copper levels should therefore be ensured. |
| Effect | Indication | Dosage |
| Physiological effects at a low intake |
For support in degenerative and/or inflammatory joint diseases such as osteoarthritis or osteochondritis | 3 mg/d (collagen type 2) |
| For nutritive support of the skin structure |
3 mg/d |
|
| General mode of administration | |
| When |
Collagen should be taken between meals. |
| Side effects | |
| No side effects are known to date. | |
| Contraindications | |
| No contraindications are known to date. | |
| Drug interactions | |
| None | No interactions are known to date. |
| Nutrient interactions | |
| None | No interactions are known to date. |
| Description |
| Structural protein of connective tissue, e.g. for building tendon (collagen type I) and cartilage tissue (collagen type II) |
| Related substances |
| Type I: skin, tendons, bones etc. Type II: hyaline and elastic cartilage Type III: vessel walls, internal organs Type IV and Type V: basal lamina |
| References |
|
1 Crowley, D. C., Lau, F. C. 2009. Safety and efficacy of undenatured type II Collagen in the treatment of osteoarthritis of the knee: a clinical trial. Int J Med Sci. 6(6):312-21. |
