Tuesday, February 14, 2017

Effective Of Collagen Peptide On Osteoarthritis



Osteoarthritis (OA) is the most common type of arthritis and the major cause of chronic musculo-skeletal pain and mobility disability in the elderly population worldwide. The characteristic features of this chronic, progressive and degenerative disorder of the entire joint include variable inflammation and changes in the structure of bone bordering the joint and in the protective cushion called articular cartilage. Clinical manifestations include joint pain, tenderness, limitation of movement, effusion and varying degrees of inflammation, and finally induce disability in many patients.


The principal components of articular cartilage are the insoluble fibrous protein collagen and the soluble proteoglycans. A complex organisation of collagen, proteoglycans and the fluid environment endows the tissue with the capacity for reversible deformability, a property essential for its physiological function. The integrity of cartilage tissue is dependent on the complex network of type II col-lagen, proteoglycans and accessory proteins such as fibronectin. These molecules are synthesised and integrated into the residual extracellular matrix (ECM) by chondrocytes. The loss of ECM in car-tilage is associated with an increased cleavage of type II collagen by collagenase and an aggrecan cleavage along with the degra-dation of small proteoglycans.1 Alterations in the collagen fibril network have been observed including extensive changes in the collagen fibril orientations, especially in the superficial zone and reduction in the collagen content.2,3 Although the loss of aggrecan in articular cartilage is essential for the progression of OA, the final cartilage damage is inflicted by the loss of the collagen network.4 Current pharmacological treatments widely use non-steroidal anti-inflammatory drugs (NSAIDs) as therapeutic agents for OA despite their adverse effects on long-term usage. An alterna-tive treatment with nutritional supplements with higher levels of safety and effectiveness attracts much attention. By nature nutri-tional supplements are better positioned to provide long-term health benefits.

Collagen-based peptides represent functional peptides that exhibit various physiological activities. Bone mineral density has been shown to be increased by the oral ingestion of gelatin.5 Folk medicines always mention the positive influence of collage-nous preparations as being beneficial to joint health, skin, hair and nails.6 –8

Several studies show that enzymatically hydrolysed collagen (known as gelatin hydrolysate or collagen hydrolysate or collagen peptide) is absorbed and distributed to joint tissues and has anal-gesic and anti-inflammatory properties. The protein has a typical and unique amino acid composition in that it is very rich in glycine, proline and hydroxyproline. Research in mice has demonstrated that after oral administration of radiolabelled gelatin hydrolysate the radioactivity was specifically found in cartilage.9 Animal exper-iments have suggested that oral ingestion of collagen peptide might have beneficial effects on joint health such as OA. A recent study in animal models demonstrated that collagen peptide reduced the morphological changes associated with osteoarthritic cartilage destruction in knee joints.10

Being a protein with rich source of amino acids specifically found in collagen, it is worthwhile performing a clinical evaluation of the substance to understand the health benefits in the manage-ment of OA. Hence the present study was planned with an aim to assess the effectiveness of pork skin collagen peptide (PCP) man-ufactured from pork skin and bovine bone collagen peptide (BCP) in subjects with clinically diagnosed knee OA.


CONCLUSION

Both pork skin collagen peptide (PCP) and bovine bone collagen peptide (BCP) are effective supplements for the improvement in overall physical problems associated with OA and thereby help to improve the quality of life. It is hypothesised that the supplementation of collagen peptide regulates chondrocyte differentiation and stimulates synthesis of proteoglycans, resulting in the initiation of repair processes in cartilage tissue.



REFERENCES

1 Felson DT, Lawrence RC, Dieppe PA, Hirsch R, Helmick CG, Jordan JM, et al., Osteoarthritis: new insights. Part 1: The disease and its risk factors. Ann Intern Med 133:635–646 (2000).

2 Bi X, Li G, Doty SB and Camacho NP, A novel method for determination of collagen orientation in cartilage by Fourier transform infrared imaging spectroscopy (FT-IRIS). Osteoarthritis Cartilage 13:1050–1058 (2005).

3 Buckwalter JA and Mankin HJ, Articular cartilage, part II. Degeneration and osteoarthrosis, repair, regeneration, and transplantation. J Bone Joint Surg Am 79:612–632 (1997).

4 Poole AR, An introduction to the pathophysiology of osteoarthritis. Front Biosci 4:662–670 (1999).

5 Nomura Y, Oohashi K, Watanabe M and Kasugai S, Increase in bone mineral density through oral administration of shark gelatin to ovariectomized rats. Nutrition 21:1120–1126 (2005).

6 Matsuda N, Koyama Y, Hosaka Y, Ueda H, Watanabe T, Araya J, et al., Effects of ingestion of collagen peptide on collagen fibrils and glycosaminoglycans in the dermis. J Nutr Sci Vitaminol 52:211–215 (2006).

7 Scala J, Hollies NRS and Sucher KP, Effect of daily gelatin ingestion on human scalp hair. Nut Rep Int 1:579–592 (1976).
8 Tyson TL, The effect of gelatin on fragile finger nails. J Invest Dermatol 14:323–325 (1950).

9 Oesser S, Adam M, Babel W and Seifert J, Oral administration of 14C labeled gelatin hydrolysate leads to an accumulation of radioactiv-ity in cartilage of mice (C57/BL). J Nutr 129:1891–1895 (1999).

10  Ohara H, Iida H, Ito K, Takeuchi Y and Nomura Y, Effect of Pro-HyP, a collagen hydrolysate derived peptide, on hyaluronic acid synthesis using in vitro cultured synovium cells and oral ingestion of collagen hydrolysate in a guinea pig model of osteoarthritis. Biosci Biotechnol Biochem 74:351–354 (2010).

11 Trc T and Bohmova J, Efficacy and tolerance of enzymatic hydrolysed collagen (EHC) vs. glucosamine sulphate (GS) in the treatment of knee osteoarthritis (KOA). Int Orthop 35:341–348 (2011).

12 Moskowitz RW, Role of collagen hydrolysate in bone and joint disease.
Semin Arthritis Rheum 30:87–99 (2000).

13  Bello AE and Oesser S, Collagen hydrolysate for the treatment of osteoarthritis and other joint disorders:a review of the literature. Curr Med Res Opin 22:2221–2232 (2006).

14  Iwai K, Hasegawa T, Taguchi Y, Morimatsu F, Sato K, Nakamura Y, et al., Identification of food derived collagen peptide in human blood after oral ingestion of gelatin hydrolysates, J Agric Food Chem 53:6531–6536 (2005).

15  Watanabe-Kamiyama M, Shimizu M, Kamiyama S, Taguchi Y, Sone H, Morimatsu F, et al., Absorption and effectiveness of orally adminis-tered low molecular weight collagen hydrolysate in rat. J Agric Food Chem 58:835–841 (2010).

16  Ohara H, Matsumoto H, Ito K, Iwai K and Sato K, Comparison of quantity and structures of hydroxyproline-containing peptides in human blood after oral ingestion of gelatin hydrolysates from different sources. J Agric Food Chem 55:1532–1535 (2007).

17  Liu C, Sugita K, Nihei K, Yoneyama K and Tanaka H. Absorption of hydroxyproline containing peptides in vascularly perfused rat small intestine in situ. Biosci Biotechnol Biochem 73:1741–1747 (2009).

18  Sugihara F, Inoue N, Kuwamori M and Taniguchi M. Quantification of hydroxyprolyl-glycine (Hyp-Gly) in human blood after ingestion of collagen hydrolysate. J Biosci Bioeng 113:202–203 (2012).

19  Oesser S and Seifert J. Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen. Cell Tissue Res 311:393–399 (2003).


20   Nakatani S, Mano H, Sampei C, Shimizu J and Wada M, Chondropro-tective effect of the bioactive peptide prolyl-hydroxyproline in mouse articular cartilage in vitro and in vivo. Osteoarthritis Cartilage 

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