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Collagen Type II Shown to Reverse Skin and Joint Aging
by James South, M.A.
Aging is the common lot of all humanity. We are born. We live. We get older. We die. Yet some people age slowly, gracefully and healthfully, while others age rapidly, with accompanying pain and debility. Many factors contribute to our rate of aging : our genes, our hormone levels, our diet and exercise patterns, drug, alcohol and tobacco abuse, etc. Two extremes of aging are presented by progeriacs and the people of Yuzurihara, Japan. Progeria is a disorder that usually appears between birth and 18 months of age. It involves extremely accelerated aging. Progeriac children are bald, heavily wrinkled, have cataracts and usually die by the age of 12 or 13.1 The residents of Yuzurihara are extremely long-lived and show little skin wrinkling, even in old age. There are 10 times more people 80 and older in Yuzurihara than any community in the United States, and they usually are free of typical age-related diseases and live active lives.1 Surprisingly, there is a specific connection between the accelerated aging of progeria and the exceptional longevity of the Yuzuriharans. Children with progeria excrete up to 17 times more hyaluronic acid (hyaluronan, or HA) in their urine than normal children.1 The residents of Yuzurihara, through their unique diet, maintain high, youthful levels of HA throughout their long and healthy lives.1 Hyaluronan Hyaluronan & Type II Collagen BioCell Technologies has developed a patented, purified, enzymatically hydrolyzed (partially digested) type II collagen supplement, derived from the sternum (breastbone) of young chickens. This product provides at least 10 percent by weight of a low molecular weight HA, which is highly absorbable. Native collagen, which has not been predigested, also provides HA, but in the form of giant molecules that are too large for absorption. BioCell s collagen molecules have a typical molecular weight of only 1,500 to 2,500 Daltons, and thus are easy for the body to absorb. In February 2004 Dr. William Judy, senior scientist at SIBR Research, announced the results of a double blind clinical study with Collagen Type II . In a 36-hour peak absorption study using a single dose, Collagen Type II HA significantly increased in the blood at four hours after ingestion, and peaked at a level 7,000 percent above the placebo controls levels in 12 hours. In a 28-day steady state bioavailability study using a constant daily dose, after seven days the Collagen Type II HA levels became stabilized and remained so throughout the study at a level 3,543 percent higher than controls. Thus, regular use of Collagen Type II can be expected to provide a significant dose of HA to supplement the age-declining tissue levels of HA typical of most people. Type II Collagen CS also enhances the synthesis of HA and cartilage proteoglycans in osteoarthritis patients, improving the quality of their joint tissue.6 CS also inhibits enzymes such as collagenase, elastase and proteoglycanase that become overactive in joint degeneration and skin aging, destroying cartilage and connective tissue.6 Type II collagen also contains cartilage matrix glycoprotein (CMGP). CMGP enhances the antioxidant protection within joints by carrying the essential trace mineral copper to the chondrocytes. Chondrocytes are small cells interspersed within the cartilage matrix of joints. The chondrocytes produce new collagen and mucopolysaccharides to keep joints well cushioned and lubricated. The chondrocytes also produce and secrete copper SOD (superoxide dismutase), a free radical-destroying enzyme that is critical to protect joint tissue from the free radical damage that occurs as part of the process of joint degeneration.7 Duarte notes that various components of hydrolyzed type II collagen have multiple protective benefits. Collagen II components 1) resist cartilage protein digesting enzymes; 2) reprogram destructive chondrocytes to lessen inflammation; 3) promote new cartilage and proteoglycon synthesis; 4) enhance production of HA, producing a thick, effective, lubricating synovial fluid that protects and cushions joints; 5) protect the surface of cartilage from oxidative (free radical) damage and enzymatic digestion; and 6) act as powerful anti-inflammatory/pain modulators.7 Collagen Type II also provides 60 percent collagen protein. Collagen protein is unique in containing the amino acids hydroxylysine and hydroxyproline. In a study using hydrolyzed collagen, the subjects receiving collagen had significantly higher blood levels of hydroxyproline than those receiving placebo.10 As Moskowitz notes: The positive effect of the oral administration of [hydrolyzed collagen] on skin and organs attached to the skin has been observed for some time . These positive effects include improvement in nail quality ; an effect on the properties of hair and nail growth ; and in veterinary studies, improvement in hair and hoof quality and growth .10 Hydrolyzed vs. Native Collagen At the meeting, Dr. Oesser remarked: This is the first time a cell culture model has shown that collagen hydrolysate, known to play a role in degenerative joint disease, can lead to an increase in cartilage formation. It is very plausible that collagen hydrolysate, when taken as a supplement to our normal diet, may help activate the synthesis of collagen in cartilage. Particularly in situations in which cartilage is under massive stress [e.g., arthritis, obesity, sports injury, etc.], the intake of collagen hydrolysate could be highly significant and reduce degenerative changes. Collagen Type II vs. Skin Aging Collagen Safety Collagen Type II Dosage Regular use of Collagen Type II may also improve wound healing,2,3 as well as improve quality and growth of hair and nails.9,10 Side effects with collagen hydrolysates are rare, but may include a sensation of unpleasant taste, a feeling of heaviness in the stomach, a bloated feeling or burping.10 References Anderson, I. The properties of hyaluronan and its role in wound healing. Prof Nurse, 2001, 17:232-35. Greco, R. et al. Hyaluronic acid stimulates human fibroblast proliferation within a collagen matrix. J Cell Physiol, 1998, 177:465-73. Ghersetich, I. & Lotti, T. Hyaluronic acid in cutaneous intrinsic aging. Int J Dermatol, 1994, 33:119-22. Champe, P. & Harvey, R. Lippincott s Illustrated Reviews: Biochemistry. Philadelphia: J.B. Lippincott, 1994:147-55. Ronca, F. et al. Anti-inflammatory activity of chondroitin sulfate. Osteoartritis & Cartilage, 1998, 6 (Suppl A):14-21. Duarte, A. The Collagen Type II Cure for Arthritis and Heart Disease. 1997:39. Oesser, S. & Seifert, J. Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen. Cell Tissue Res, 2003, 311:393-99. Novick, N. Tips for at-home anti-aging skin care. Total Health for Longevity, 2003, 25:44-46. Moskowitz, R. Role of collagen hydrolysate in bone and joint disease. Semin Arthritis Rheum, 2000, 30:87-99. The information in this article is not intended to provide personal medical advice, which should be obtained from a medical professional, and has not been approved by the U.S. FDA. Copyright by Vitamin Research Products, Inc. The Vitamin Research News is intended solely for individual, non-commercial use. All other uses are prohibited without written permission from VRP. The Vitamin Research News is protected by U.S. and international copyright laws and may not be reproduced, distributed, transmitted, displayed, published or broadcast in any form, or by any means whether now known or hereinafter devised, without prior written permission from VRP. Requests for permission to reproduce all or part of the material or information contained in the Vitamin Research News should be directed by U.S. Post to Robert Watson at Vitamin Research Products 4610 Arrowhead Drive Carson City, NV 89706 or by fax to Robert Watson at 775.884.1336 or via e-mail to Robert Watson, at VRP.
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