Effects of Collagen Crosslinking on Bone Material Properties in Health and Disease

Verfasser / Beitragende:
[Mitsuru Saito, Keishi Marumo]
Ort, Verlag, Jahr:
2015
Enthalten in:
Calcified Tissue International, 97/3(2015-09-01), 242-261
Format:
Artikel (online)
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024 7 0 |a 10.1007/s00223-015-9985-5  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00223-015-9985-5 
245 0 0 |a Effects of Collagen Crosslinking on Bone Material Properties in Health and Disease  |h [Elektronische Daten]  |c [Mitsuru Saito, Keishi Marumo] 
520 3 |a 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. 
540 |a Springer Science+Business Media New York, 2015 
690 7 |a Collagen crosslinking  |2 nationallicence 
690 7 |a Advanced glycation end products (AGEs)  |2 nationallicence 
690 7 |a Osteoporosis  |2 nationallicence 
690 7 |a Diabetes  |2 nationallicence 
690 7 |a Glucocorticoids  |2 nationallicence 
700 1 |a Saito  |D Mitsuru  |u Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan  |4 aut 
700 1 |a Marumo  |D Keishi  |u Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan  |4 aut 
773 0 |t Calcified Tissue International  |d Springer US; http://www.springer-ny.com  |g 97/3(2015-09-01), 242-261  |x 0171-967X  |q 97:3<242  |1 2015  |2 97  |o 223 
856 4 0 |u https://doi.org/10.1007/s00223-015-9985-5  |q text/html  |z Onlinezugriff via DOI 
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900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a review-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00223-015-9985-5  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Saito  |D Mitsuru  |u Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Marumo  |D Keishi  |u Department of Orthopaedic Surgery, Jikei University School of Medicine, 3-25-8, Nishi-Shinbashi, Minato-ku, 105-8461, Tokyo, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Calcified Tissue International  |d Springer US; http://www.springer-ny.com  |g 97/3(2015-09-01), 242-261  |x 0171-967X  |q 97:3<242  |1 2015  |2 97  |o 223