Glycation Contributes to Interaction Between Human Bone Alkaline Phosphatase and Collagen Type I

摘要: Bone is a biological composite material comprised primarily of collagen type I and mineral crystals calcium phosphate in the form hydroxyapatite (HA), which together provide its mechanical properties. alkaline phosphatase (ALP), produced by osteoblasts, plays pivotal role mineralization process. Affinity contacts between collagen, mainly II, crown domain various ALP isozymes were reported few vitro studies 1980s 1990s, but have not attracted much attention since, although such interactions may important implications for bone The objective this study was to investigate binding properties human ALP, including two isoforms B1 B2. from liver, placenta E. coli also studied. A surface plasmon resonance-based analysis, supported electrophoresis blotting, showed that binds stronger comparison with ALPs expressed non-mineralizing tissues. Further, B2 isoform significantly isoform. Human liver (with identical amino acid composition) displayed pronounced differences binding, revealing post-translational glycosylation govern these large extent. In conclusion, presents first evidence are crucial importance protein-protein I, presence be necessary. Different affinities among influence mineral-collagen interface, kinetics, degree matrix mineralization, factors determining bone.