Affiliation: | 1. Department of Clinical Laboratory Science, Graduate School of Medical Science, Kanazawa University, Kanazawa, Japan These authors contributed equally to this study.;2. Department of Clinical Engineering, Faculty of Health Sciences, Komatsu University, Komatsu, Japan These authors contributed equally to this study.;3. Life Science Research Center, University of Toyama, Toyama, Japan;4. Department of Clinical Laboratory Science, Graduate School of Medical Science, Kanazawa University, Kanazawa, Japan;5. Noto Center for Fisheries Science and Technology, Kanazawa University, Kanazawa, Japan;6. Department of Biology, College of Liberal Arts and Sciences, Tokyo Medical and Dental University, Ichikawa, Japan;7. Noto Marine Laboratory, Institute of Nature and Environmental Technology, Kanazawa University, Kanazawa, Japan |
Abstract: | The high plasma glucose induced in glucose metabolism disorders leads to the non-enzymatic glucose-dependent modification (glycation) of type 1 collagen, which is an essential component of bone tissue. The glycation of proteins induces the formation of advanced glycation end-products, such as carboxymethyl arginine, which is preferentially generated in glycated collagen. However, the effect of advanced glycation end-product formation on the characteristics of type 1 collagen remains unclear due to the lack of suitable in vitro experimental systems analyzing type 1 collagen. Here, we show that the glycation of type 1 collagen can be analyzed in vitro using a goldfish-scale bone model. Our study using these scales provides evidence that the advanced glycation end-product formation in type 1 collagen induced by glyoxal, the carboxymethyl arginine inducer, facilitates the crosslinking of type 1 collagen, decreasing both its strength and flexibility. |