Fibromyalgia: A Plausible Model for Cause and Cure

by John W. Cartmell, LMP, Diet Advisor

Fibromyalgia is a disease of widespread soft-tissue pain and stiffness. It often coincides with symptoms of persistent fatigue, exercise intolerance, disrupted and non-restorative sleep, tension headaches, migraines, blurred vision, abnormalities of the skin or fingernails, painful menstrual periods, numbness or tingling, heart palpitations, sleep apnea, temperature sensitivity, restless legs, impaired cognition, irritable bladder, and intestinal symptoms of irritable bowel, bloating, gas, belching, pain and distention.^{5, 6} Over the years, it's been referred to as myofibrocitis, myofascitis, myofascial pain syndrome, muscular rheumatism, and fibrocitis (inflammation of fibrous tissues).⁵ Because the soft-tissues are not really "inflamed", fibromyalgia is considered to be a more accurate term for the disease.

The word, fibromyalgia has Latin and Greek roots; fibra (fibrous), myo (muscle) and algos (pain), literally mean "pain of the fibrous tissues and muscles". The American Medical Association acknowledged the existence of fibromyalgia in 1987. The Arthritis Foundation classifies fibromyalgia as a form of soft-tissue rheumatism. In 1990 the American College of Rheumatology established criteria for its diagnosis, including 18 common tender points and a history of widespread pain for 6 month or longer. In 1992 a group of international experts established the formal definition of fibromyalgia in a report called the Copenhagen Declaration. This report endorsed the 18 tender points as criteria for diagnosis and formally acknowledged many of the other symptoms commonly seen with fibromyalgia.^{5, 6}

Fibromyalgia affects an estimated 6 million Americans and accounts for $9 billion annually in conventional medical care and another $13 billion in alternative treatments like naturopathy, acupuncture and massage therapy. Sixty percent of cases are diagnosed between ages 30 and 50, eighty to ninety percent of which are women.^{5, 6}

The exact cause of fibromyalgia is unknown. Nerve pathways somehow become sensitized and hyperactive to pain until nerve signals of pain become chronic.^{5, 6} Studies have shown that fibromyalgia patients have decreased levels of certain nerve transmitters and amino acids in their spinal fluid. Substance P and Serotonin are nerve transmitters for pain and sleep, respectively. Endorphins and Enkephalins are opiate-like nerve transmitters that dull the perception of pain.⁵ Substance P is composed of 11 amino acids, Serotonin is derived from Tryptophan, an essential amino acid, and Endorphins and Enkephalins are composed partly of proteins. It's believed that decreased levels of Serotonin may be a factor in the sleep disruption problems commonly seen in fibromyalgia patients. Essentially, fibromyalgia is a disease of biochemical imbalance, with soft-tissue symptoms of pain and stiffness that often coincide with other physiological disorders.^{5, 6} The tendency to develop the disease may be partially due to heredity.⁶

Soft-tissue changes seen in fibromyalgia are presumed to be the result of a self-perpetuating cycle of pain- activated spasms, causing more pain, which causes more spasms. The soft-tissue becomes chronically congested, and the delivery of oxygen and other nutrients, as well as the removal of metabolic wastes and acids, becomes impaired.⁶ Symptoms often manifest after trauma, infection, or stress, or are secondary to other diseases such as lupus or cancer.⁵ The symptoms of pain and stiffness may be the result of injury and insufficient tissue maintenance and repair in the muscles and the myofascia, a fibrous tissue that encapsulates muscles, individual muscle fibers, and is continuous with the tendonous bands that attach muscle to bone.⁶

A similar disorder, known as Myofascial Pain Syndrome (MPS), is associated with soft-tissue injury, repetitive strain, or long-term spinal misalignment. MPS is often found together with fibromyalgia.⁶ Myofascial pain syndrome differs from fibromyalgia in that the pain is localized rather than widespread, affects men and women equally, and has trigger points only in areas of past injury.^{5, 6} Fibromyalgia is considered a biochemical imbalance, whereas MPS is considered a neuro-muscular disorder.⁶ The fact that MPS and fibromyalgia often occur together may indicate a common factor in the cause of both disorders.

Scans of fibromyalgic muscle tissue by electron microscope reveal abnormalities of increased deposits of glycogen (muscle sugar), abnormal mitochondria (organelles that produce the cellular fuel, ATP), DNA fragmentation, and damaged muscle cell membranes. An enzyme needed for ATP production may also be defective in fibromyalgic muscles. Some muscles appear to be deficient in oxygen, perhaps from pain- activated muscles clamping down on normal blood circulation, or from abnormalities in the red blood cells themselves. The exaggerated pain signals associated with neuro-physiological imbalance may also contribute to micro trauma of muscle fibers that goes unrepaired.⁵ Growth hormone, a protein-based molecule needed for muscle maintenance and repair, is manufactured during deep sleep. Some researchers believe that decreased levels of growth hormone, due to disrupted sleep, may be part of the reason for the unrepaired muscle damage seen in fibromyalgia.^5,6

Conventional treatments for fibromyalgia focus on controlling pain symptoms with medications, and alleviating fatigue through exercise, stress management, and diet and lifestyle changes.⁵ Alternative treatments seek to promote and restore the normal state of health using herbal and natural medicines, spinal alignment, massage therapy, acupuncture, and nutrition. Neither conventional nor alternative treatments have been particularly effective in preventing or treating Fibromyalgia.

A proper diet is essential to maintain normal health and wellness. If the diet is insufficient to support health, the person will not be optimally well. Protein is one of many nutrients needed in a properly balanced diet for normal growth and maintenance. Proteins make up 10-20% of the mass of most cells and tissues, and provide for many of the functions and physical structure of cells, organs and tissues. Globular proteins, composed of one or more proteins, perform specific functions as enzymes, certain hormones, antibodies, and protein transport complexes, all needed for the normal operation of the body.^{2, 3, 8} If protein intake, digestion or assimilation is insufficient to maintain normal tissues and functions, then degenerative changes and tissue abnormalities result.²

Dietary proteins must be broken down by digestion into individual amino acids. The first stage of digestion occurs in the stomach where hydrochloric acid activates pepsin, an enzyme that breaks down large complexes of protein into smaller sized proteins. Pancreatic and intestinal enzymes then complete the digestion of proteins into individual amino acids that can be absorbed into the blood and reassembled by the body into the various body tissues.² How these amino acids are assembled into proteins, determines the structure and function of specific proteins and tissues.

Body proteins are composed of different combinations of twenty amino acids. Half of these amino acids can be synthesized by the body, but the other half are considered essential amino acids because they must be obtained from the diet.² Dietary proteins are classified as complete or incomplete, based on the amounts of essential amino acids they contain and provide. Animal-derived proteins like milk, meat, fish, poultry and eggs contain good amounts of all essential amino acids and are therefore considered complete. Vegetable proteins are generally considered incomplete because the amounts or availability of certain essential amino acids are inadequate to support normal tissue growth or maintenance. Vegetable proteins are usually combined, or animal protein included, to ensure the diet has sufficient amounts of all essential amino acids.²

Skeletal muscle is highly specialized tissue. The complexity of a muscle cell's structure coincides with its unique specialized function of contractibility, the result of an elaborate system of multiple protein interactions. The two primary types of proteins in a muscle cell, actin and myosin, are complexes of proteins with smaller specialized protein components. Essential amino acids make up approximately 38% of the individual protein components in Actin and Myosin, and 50% of the structure of myoglobin, a type of "muscle" hemoglobin.^{9, 10, 8} By comparison, the protein fibers that make up collagen, a general fibrous protein, are composed of approximately 20% essential amino acids.^{12, 13} It's not surprising that soft-tissue degeneration and ill health result when protein ingestion, digestion or assimilation are deficient.

Both fibromyalgia and MPS may be related to protein deficiency. If the availability of essential amino acids is insufficient to adequately maintain or repair muscle tissue, then collagen may be the body's best alternative for providing structural support in spite of a loss of normal muscle structure and function. The irritation, stiffness and pain associated with trigger points in fibromyalgia and MPS may be the result of structural abnormalities resulting from the replacement of one tissue type with another. Indeed, the 18 tender points used to diagnose fibromyalgia are located precisely in areas where muscles and myofascial tissues merge one into another, where collagen based myofascial tissue, with it's lower content of essential amino acids, may increase disproportionately during times of protein insufficiency.

As a massage therapist, I specialize in the treatment of soft-tissue abnormalities. In my 15 years of practice, the majority of my clients have had fibromyalgia or other problems of myofascial abnormalities. I've worked with some of these clients for as long as 10 years. One of the more effective massage techniques for myofascial problems is deep-tissue massage; a vigorous type of massage used to loosen areas of hardened or inflexible muscles and associated tissues. Deep-tissue massage improves some of the symptoms of fibromyalgia and MPS, but the effects are generally temporary and maintenance treatments are usually needed indefinitely.

In 1999, I solved a five-year problem of chronic fatigue by revising my diet. In the process, I noticed that soft-tissue abnormalities improved or disappeared.1 Where the tissue had previously been hardened and painful, it was now much more flexible and normal. A muscle injury that had failed to heal for 6 months, healed completely in two weeks. Keratosis-like skin abnormalities of 15-years duration also cleared up in weeks. When my clients with fibromyalgia or MPS similarly revised their diets, they all experienced decreased pain, and improvements in energy, sleep, bowel function, and soft-tissue structure. The high rate of response in these clients to improvements in protein nutrition suggests a plausible model for the cause and cure of Fibromyalgia, and other conditions associated with soft-tissue abnormalities.

When protein ingestion and digestion are optimized in clients with fibromyalgia or MPS, there is a consistent and dramatic decrease in pain, stiffness, and soft-tissue abnormalities. In my small group of 30 clients, all responded positively to this approach within 4-8 weeks, with substantial decreases in pain and stiffness, and 50% or more improvement in soft-tissue structure. The tissue feels more normal and seems to melt under the hands during massage. The pain these clients used to experience during deep-tissue massage is now minimal or nonexistent. Their muscles loosen and respond to massage now much more like normal tissue.

The following cases are typical: Jolyn is 40 years old and has been a client for over 5 years. She has been diagnosed as having fibromyalgia, and credits the deep tissue massage with preventing her from being disabled by her stiffness and pain. One day she was much worse than I had seen her in some time. When I questioned her about her diet and protein, she related that her primary source of protein was 3 to 5 glasses of milk a day, and that she didn't think she'd had any protein at all in the last 3 days. Her sole source of protein from milk was providing 40 grams or less of protein per day; 2/3 of the 55 grams generally recommended for adult females. When she increased her daily intake of protein to 55 grams or more, and supplemented her meals with pancreatic enzymes (pancreatin), her pain and stiffness decreased, and her chiropractor was able to make certain spinal adjustments for the first time in 5 years. When she added hydrochloric acid (Betaine-HCl) to her supplement regimen, her soft-tissue improved even more.

Louise is 35 years old and has been a client for 4 years. Her MPS symptoms had worsened over the years and in the last two years, she had gained about 20 lbs. She had tried a high protein diet to lose weight, but it didn't seem to make any difference and the extra protein made her feel stuffed and bloated. When she supplemented with Betaine-HCl and pancreatic enzymes, digestion was better and her soft-tissue improved substantially towards normal. A few weeks later she began to lose weight.

Lois is 70 years old and has been a client for 7 years. Her soft-tissue has always been "as hard as a rock" and very resistant to massage. I discussed with her the importance of protein for proper muscle structure and she subsequently increased the amount of protein in her diet. When I saw her two months later, her soft- tissue was better than I'd ever seen it. When I saw her again seven months later, she was still continuing the high protein diet, and her soft- tissue was sill improved.

Betty, age 79, has been a client for five years. She had hip replacement surgery three years ago for problems related to osteoporosis. A year after the surgery the soft-tissue around the site of surgery became once again hardened and inflexible. Then suddenly, the tissue improved. When I asked her what might account for this improvement, she said the only change in her diet or lifestyle had been the recent addition of pancreatic enzymes to ease a chronic problem of feeling stuffed and bloated. A review of her diet indicated she had been getting approximately 2/3 the daily recommended amount of protein. When she increased her dietary protein intake in addition to supplementing with digestive enzymes, her tissue improved even more. Over the next several months, her arthritis symptoms decreased significantly and she was able to discontinue her arthritis medication.

Rebecca, age 28, is a recent client. She had experienced a lot of intestinal problems over the last 8 years. Her soft-tissue was hardened and sometimes swollen, and she suffered from bouts of exhaustion. She also had muscle injuries that had not healed in eight years, various joint pains, and sometimes felt "spacey". These symptoms all improved when she increased protein digestion by supplementing with Betaine-HCl and pancreatin. A few months later, her soft-tissue became hardened again and she complained of a relapse of symptoms. When I asked if she had made any changes to her diet, she said she had run out of Betaine-HCl about a week earlier and hadn't yet replaced it. When she added the Betaine-HCl to her diet again, her symptoms abated once more. Her physician later confirmed by clinical tests that her stomach hydrochloric-acid production was almost nonexistent.

Fred, age 68, has been a client for 14 years. A car struck him 5 years ago causing an injury to his right shoulder. Physical therapy, massage, and remedial exercises were unsuccessful in restoring the joint to its normal structure or function. He had problems of chronic pain and stiffness in the shoulder, and the soft-tissue had become hardened and abnormal. I suggested he assess the protein content of his diet and consider adding supplements of both Betaine-HCl with pepsin, and pancreatin. After 12 weeks, his soft tissue was much improved in texture and response to massage. The pain and stiffness in his shoulder had decreased, and his soft tissue was more normal. The injury appeared to have healed completely, with normal soft-tissue replacing abnormal.

A well balanced diet is only as beneficial as your ability to digest what you eat. It's not unusual for the middle-aged or elderly to have problems digesting protein. Low stomach-acid is common in about 50% of people over age sixty, particularly women.¹ As part of the natural aging process, a decrease in stomach-acid production may be a common factor in the development of age-related degenerative changes, including weight gain, vision problems, arthritis, cardio-vascular disease, high blood pressure, sleep disruptions, prostate hypertrophy, intestinal problems, decreased hormones, emotional depression, fatigue, diabetes, cancer, disc degenerative disease and other soft-tissue abnormalities. If these diseases can be caused or aggravated by deficiencies in protein nutrition, then the prevention, treatment or cure for these maladies may require protein nutritional support.

The structure and function of different proteins in soft-tissues, enzymes, brain-transmitters, and certain hormones, requires proper protein nutrition. If protein nutrition is inadequate due to low dietary intake, maldigestion, or malabsorption, then the potential for degenerative disease can increase. The symptoms of Fibromyalgia; abnormal soft-tissue, persistent fatigue, exercise intolerance, disrupted and non-restorative sleep, tension headaches, migraines, blurred vision, abnormalities of the skin or fingernails, painful menstrual periods, numbness or tingling, heart palpitations, sleep apnea, temperature sensitivity, restless legs, impaired cognition, irritable bladder, and intestinal symptoms of irritable bowel, bloating, gas, belching, pain and distention, can all be caused or made worse if protein nutrition is insufficient to support the repair and maintenance of normal, healthy tissues.

When I ask clients with fibromyalgia or myofascial pain syndrome about their diets, I usually find they are getting significantly less protein than the recommended daily amount of 50 grams for women and 60 grams for men. Assuring that dietary protein is balanced, and that the ingestion, digestion and assimilation of protein is adequate, may provide an effective alternative approach to the treatment of fibromyalgia and other soft-tissue degenerative diseases.

References:

1. Cartmell, John W., Nutritional Considerations in Chronic Fatigue Syndrome, Frontier Perspectives, The Center for Frontier Sciences, Philadelphia, PA, Summer-2000

2. Mahan, L. Kathleen, Escott-Stump, Sylvia, Krause's Food, Nutrition, & Diet Therapy, 9th Edition, W.B. Saunders Company, Division of Harcourt Brace & Co., Philadelphia, PA, 1996

3. Caret, Robert L., Denniston, Katherine J., Topping, Joseph J., Principles & Applications Of Organic & Biological Chemistry, Times Mirror Higher Education Group, Inc, Dubuque, Iowa, 1997

4. Murray, Michael T, Natural Alternatives to Over-the-Counter and Prescription Drugs, William Morrow and Co. Inc., New York, 1994

5. Wallace, Daniel and Janice, Making Sense of Fibromyalgia, Oxford University Press, New York, 1999

6. Starlanyl, Devin, Copeland, Mary Ellen, Fibromyalgia & Chronic Myofascial Pain Syndrome, New Harbinger Publications, Inc., Oakland, CA, 1996

7. Braverman, Eric R., Pfeiffer, Carl C., The Healing Nutrients Within, Keats Publishing Inc, New Canaan, Connecticut, 1987

8. Guyton, Arthur C., Hall, John E., Textbook of Medical Physiology, 10th Edition, W.B. Saunders Company, Division of Harcourt Brace & Co., Philadelphia, PA, 2000

9. Dayhoff, Margaret O., Atlas of Protein Sequence and Structure, v. 5 suppl. 2 National Biomedical Research Foundation, Silver Spring, MA, 1976

10. Beggs A. H., Byers T.J., Knoll J.H.M., Boyce F.M., Bruns G.A.P., and Kunkel L.M., Cloning and Characterization of Two Human Skeletal Muscle Alpha-Actinin Genes, Journal of Biological Chemistry, 267: 9281-9288, 1992

11. Wu Q.L., Jha P.K., Raychowdhury M.K., Du Y., Leavis P.C., and Sankar S., Isolation And Characterization Of Human Fast Skeletal Beta Troponin T, DNA and Cell Biology, 13: 217-233, 1994

12. Zhuang J., Tromp G., Kuivaniemi H., Castells S., and Prockop D.J., Substitution Of Arginine For Glycine At Position 154 Of The Alpha 1 Chain Of Type I Collagen, American Journal of Medical Genetics, 61: 111-116, 1996

13. Dalgleish R., The Human Type I Collagen Mutation Database, Nucleic Acids Research, 25: 181-187, 1997

© 2002 John W. Cartmell, LMP

John W. Cartmell, LMP has been a Licensed Massage Practitioner in Washington State since 1985, and has published articles on massage, health and nutrition in numerous professional journals. He specialized in the treatment of people with chronic and acute pain, fibromyalgia, chronic fatigue, migraines, hip and shoulder problems, arthritis and trauma injuries. He is currently completing work on a Master's degree in nutritional research. This article was originally published in the Townsend Letter for Doctors and Patients, Nov. 2001. Visit the author's web site at http://www.dietadvisor.com.