caa a22 4500 60552064X CHVBK 20210128100736.0 cr unu---uuuuu 210128e20150901xx s 000 0 eng 10.1007/s00223-015-9985-5 doi (NATIONALLICENCE)springer-10.1007/s00223-015-9985-5 Effects of Collagen Crosslinking on Bone Material Properties in Health and Disease [Elektronische Daten] [Mitsuru Saito, Keishi Marumo] Data have accumulated to show that various types of collagen crosslinking are implicated in the health of individuals, as well as in a number of disease states, such as osteoporosis, diabetes mellitus, chronic kidney disease, inflammatory bowel disease, or in conditions of mild hyperhomocysteinemia, or when glucocorticoid use is indicated. Collagen crosslinking is a posttranslational modification of collagen molecules and plays important roles in tissue differentiation and in the mechanical properties of collagenous tissue. The crosslinking of collagen in the body can form via two mechanisms: one is enzymatic crosslinking and the other is nonenzymatic crosslinking. Lysyl hydroxylases and lysyl oxidases regulate tissue-specific crosslinking patterns and quantities. Enzymatic crosslinks initially form via immature divalent crosslinking, and a portion of them convert into mature trivalent forms such as pyridinoline and pyrrole crosslinks. Nonenzymatic crosslinks form as a result of reactions which create advanced glycation end products (AGEs), such as pentosidine and glucosepane. These types of crosslinks differ in terms of their mechanisms of formation and function. Impaired enzymatic crosslinking and/or an increase of AGEs have been proposed as a major cause of bone fragility associated with aging and numerous disease states. This review focuses on the effects of collagen crosslinking on bone material properties in health and disease. Springer Science+Business Media New York, 2015 Collagen crosslinking nationallicence Advanced glycation end products (AGEs) nationallicence Osteoporosis nationallicence Diabetes nationallicence Glucocorticoids nationallicence Saito Mitsuru Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan aut Marumo Keishi Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan aut Calcified Tissue International Springer US; http://www.springer-ny.com 97/3(2015-09-01), 242-261 0171-967X 97:3<242 2015 97 223 https://doi.org/10.1007/s00223-015-9985-5 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00223-015-9985-5 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Saito Mitsuru Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan aut NATIONALLICENCE 700 1- Marumo Keishi Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan aut NATIONALLICENCE 773 0- Calcified Tissue International Springer US; http://www.springer-ny.com 97/3(2015-09-01), 242-261 0171-967X 97:3<242 2015 97 223