Collagen – A natural alternative for musculoskeletal conditions

Written by May 2016 Phoebe Wynne-Lewis, BHSc, Dip Nat Med, Dip Herb Med – FxMed Technical Support


The word “fibromyalgia” comes from the Latin term for fibrous tissue (fibro) and the Greek words for muscle (myo) and pain (algia). Fibromylgia is a disorder characterized by widespread musculoskeletal pain accompanied by fatigue, sleep, memory and mood issues. Researchers believe that fibromyalgia amplifies painful sensations by affecting the way our brain processes pain signals. Pain is often regional initially and then spreads to multiple locations over months. Some patients may present with pain in one or two regions, such as the back, neck or the chest area. Pain then becomes progressively widespread, severe, constant, nagging and disabling in a majority of people. Pain is the most common reason for consultation with a physician.

Symptoms sometimes begin after a physical trauma, surgery, infection or significant psychological stress. In other cases, symptoms gradually accumulate over time with no single triggering event. Many people who have fibromyalgia also have tension headaches, temporomandibular joint (TMJ) disorders, irritable bowel syndrome, anxiety and depression.


Collagen is a protein made up of amino-acids and makes up approximately 30% of the proteins within the body. Collagen is the major component of connective tissue in the body and is found in muscles, tendons, ligaments, organs, skin, arteries, veins, lymph vessels and joint cartilage.

Collagen types contain different proteins which serve separate purposes within the body; Collagen Types 1 & 3 support skin, muscles (including ligaments and tendons), bone density and hair and nail growth, and are produced by fibroblasts (cells in connective tissues) and osteoblasts (cells that make bones). Over 90% of collagen in the body is comprised of Type 1 & 3 Collagen. Proteins in these types include glycine, proline, alanine, and hydroxyproline.

Collagen Type 2 makes up the fluids and function in the cartilage and joints and is produced by chondrocytes (the non-cellular matrix of cartilage) – a liquid-like filling within the cartilage.
We are constantly involved in a game of catch up to do repairs. Through the years, we lose lean muscle mass, have less demand for energy and our metabolism adjusts and decreases. Therefore, it appears that providing the body with the collagen it needs for repairs and growth may help deficient areas to improve health.

According to Tim O’Shea, D.C., from California, a nutrition expert, it has been postulated that when collagen is absorbed on an empty stomach, it avoids anabolic competition from other amino acids, fatty acids, monosaccharides, sugars and other absorbable elements. The concentrated effect of select amino acids in the blood-stream allows targeting of specific organs.

Supplemental collagen has a specific amino acid formulation that targets the production of new collagen and thus supports natural function by providing in abundance long chain and branched chain amino acids necessary for connective tissue production.

Collagen and Muscle Pathology in Fibromyalgia Patients

A study was carried out by Oxford University to quantify collagen-related amino acids in muscle biopsies taken from Fibromyalgia (FM) patients’ non-tender-point areas, representing the perimysium (connective tissue surrounding a bundle of muscle fibres) and endomysium (connective tissue surrounding the individual muscular fibers), and to search for histological signs of connective tissue and general muscle pathology.

Muscle biopsies were obtained from 27 female fibromyalgia patients. A relationship between disorganization of myofibrils and muscle soreness, pain and stiffness after exercise showed. Signs of previous injury remained as deposits of collagen in the muscle interstitium. A change in collagen metabolism, which may reflect a similar development in FM muscle has been indicated by a decreased ratio between pyridinoline and deoxypyridinoline in urine and in serum, and a lower concentration of hydroxyproline in urine. Highly ordered collagen cuffs were found around terminal nerves in the tender-point areas in skin, and were suggested to be a result of neurogenic inflammation.

It may be speculated that the collagen defect is a general feature of FM, and not only related to tender points or to skin. This is supported by the finding of a low concentration of procollagen type III amino-terminal peptide (S-PIIINP) in serum of FM patients, and the known correlation between low S-PIIINP and high intensity of muscle pain.

In muscle, collagen is the major fraction of the non-contractile constituents. The organization and co-operation between muscle fibres and intramuscular connective tissue determine the properties of the whole muscle. Hydroxyproline mainly occurs in collagen and is routinely used as a collagen marker. The FM patients had lower hydroxyproline and lower total concentration of the major amino acids of collagen than the controls, and atrophied muscle fibrils were also found in FM patients.

In conclusion, fibromyalgia patients had a significantly lower amount of intramuscular collagen. This may lower the threshold for muscle micro-injury and thereby result in non-specific signs of muscle pathology.

The Effects of Collagen Hydrolysat on Symptoms of Chronic Fibromyalgia and Temporomandibular Joint Pain

Twenty people who had medically diagnosed fibromyalgia for 2 to 15+ years (aged 31-75) completed a 90-day evaluation to determine effects of collagen hydrolysat (hydrolysed collagen) on symptoms of chronic fibromyalgia, with 12 reporting temporomandibular joint pain (TMJ). Participants were evaluated initially and then at 30-, 60-, and 90-day periods. The study participants were instructed to take one tablespoon of collagen hydrolysat with a glass of water just before going to sleep. They were advised to take no food or other beverages except water for three hours before taking the supplement.

Final results were obtained and comparisons made. The average pain complaint levels decreased significantly in an overall group average, and dramatically with some individuals. It was concluded that patients with fibromyalgia and concurrent TMJ problems may gain symptomatic improvement in their chronic symptoms by taking collagen hydrolysat.



Osteoarthritis (OA) is a joint disease that mostly affects cartilage. The degeneration of articular cartilage as part of the clinical syndrome of osteoarthritis is one of the most common causes of pain and disability in middle-aged and older people. The strong correlation between increasing age and the prevalence of osteoarthritis, and recent evidence of important age-related changes in the function of chondrocytes, suggest that age-related changes in articular cartilage can contribute to the development and progression of osteoarthritis.

Articular cartilage consists of a cellular (chondrocyte) and an extracellular compartment. The extracellular compartment is composed of collagen, proteoglycans, and non collagenous matrix proteins. The structural backbone of this matrix is the collagen fibril, which is composed mainly of type II collagen.

The first sign of apparent degeneration characteristic of OA is the onset of fibrillation at the surface of articular cartilage as collagen fibrils are damaged. Proteoglycans are lost and contents increase deeper in the cartilage. An increase in type II collagen denaturation is seen in early OA with a net loss of this molecule accompanying this damage. The body cannot produce sufficient collagen to reverse this process. Supplementation of type ll collagen has shown to be effective in supporting the matrix that makes up articular cartilage.

Collagen Hydrolysat for the Treatment of Osteoarthritis and Other Joint Disorders

structure of articular cartilageAccording to published research, orally administered collagen hydrolysat has been shown to be absorbed intestinally and to accumulate in cartilage. Collagen hydrolysat ingestion stimulates a statistically significant increase in synthesis of extracellular matrix macromolecules by chondrocytes (p < 0.05 compared with untreated controls). These findings suggest mechanisms that might help patients affected by joint disorders such as OA. Four open-label and three double-blind studies were identified and reviewed; they showed collagen hydrolysat to be safe and to provide improvement in some measures of pain and function in some patients with OA or other arthritic conditions. 2collagen diagram