Collagen Hydrolysate and its Relationship to Joint Health

A Scientific Compendium 2 The texts, figures, graphics and the layout of this publication are subject to the publisher's worldwide copyright. Unauthorized use, reproduction or dissemination of the publication in part or in whole will be consequently prosecuted. The information contained in this publication has been meticulously researched and is correct to the best of our knowledge and belief. Nevertheless, the publisher accepts no liability for damage of any kind that may occur directly or indirectly from application of the statements made in this publication. Foreword Collagen is a vital component of structural matrix throughout almost all tissues and organs of the body [1]. It is particularly concentrated in skin, bone, tendons and cartilage where it plays a major role in the integrity of joint-related connective tissues. Studies reflect a relationship with collagen not only to normal healthy joint metabolism, but also to collagen-related alterations related to the aging process [2-4]. Increased formation of advanced glycation end-products (AGEs) leads to significantly accelerated collagen cross-linking with increased susceptibility of cartilage to degenerative change in response to mechanical and nutritional stimuli. Collagen alterations also play a role in osteoarthritis wherein alterations in collagen structure result from an imbalance in synthesis versus catabolism with resultant articular hyaline cartilage breakdown1. The importance of normal collagen structure is vividly seen in the severe generalized arthritis associated with collagen gene mutations [5; 6]. Studies support a role for dietary collagen hydrolysate in maintaining healthy joints by nutritional support mechanisms; proline may be a dietary indispensable amino acid [7]. Studies by Oesser et al [8] which demonstrated a preferential uptake of 14 C-labelled proline suggest nutritional advantages to the use of collagen hydrolysate as a source of structurally important amino acids. Studies indicating that preexisting collagen might be translocated and utilized to form " new " fibrous tissue would support a role for exogenously administered collagen hydrolysate which might be utilized in an undigested form [9]. Of particular interest are recent studies which demonstrated stimulation of type II collagen biosynthesis by collagen hydrolysate [10]. In these studies, bovine chondrocytes were exposed to culture media with and without collagen hydrolysate. Utilizing immunocytochemical methods, it was demonstrated that type II collagen synthesis was stimulated in the presence of the collagen hydrolysate. It is postulated that collagen hydrolysate would accordingly add to anabolic reparative responses. Given the importance of collagen to joint-related connective tissues, and experimental data which support nutritional …