Glycation Contributes to Interaction Between Human Bone Alkaline Phosphatase and Collagen Type I
| Autor: | Karin Enander, Per Magnusson, Cecilia Halling Linder |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
musculoskeletal diseases
0301 basic medicine Gene isoform Glycosylation Endocrinology Diabetes and Metabolism Placenta chemistry.chemical_element 030209 endocrinology & metabolism Calcium Isozyme Mineralization (biology) Bone and Bones Collagen Type I 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Endocrinology Calcification Physiologic stomatognathic system Glycation Pregnancy Cell Line Tumor Protein Interaction Mapping Escherichia coli Humans Orthopedics and Sports Medicine Chromatography High Pressure Liquid Osteoblasts Chemistry Surface Plasmon Resonance Alkaline Phosphatase In vitro Isoenzymes 030104 developmental biology Durapatite Biochemistry Liver Immunology Alkaline phosphatase Female Protein Processing Post-Translational |
| Zdroj: | Calcified tissue international. 98(3) |
| ISSN: | 1432-0827 |
| Popis: | Bone is a biological composite material comprised primarily of collagen type I and mineral crystals of calcium and phosphate in the form of hydroxyapatite (HA), which together provide its mechanical properties. Bone alkaline phosphatase (ALP), produced by osteoblasts, plays a pivotal role in the mineralization process. Affinity contacts between collagen, mainly type II, and the crown domain of various ALP isozymes were reported in a few in vitro studies in the 1980s and 1990s, but have not attracted much attention since, although such interactions may have important implications for the bone mineralization process. The objective of this study was to investigate the binding properties of human collagen type I to human bone ALP, including the two bone ALP isoforms B1 and B2. ALP from human liver, human placenta and E. coli were also studied. A surface plasmon resonance-based analysis, supported by electrophoresis and blotting, showed that bone ALP binds stronger to collagen type I in comparison with ALPs expressed in non-mineralizing tissues. Further, the B2 isoform binds significantly stronger to collagen type I in comparison with the B1 isoform. Human bone and liver ALP (with identical amino acid composition) displayed pronounced differences in binding, revealing that post-translational glycosylation properties govern these interactions to a large extent. In conclusion, this study presents the first evidence that glycosylation differences in human ALPs are of crucial importance for protein-protein interactions with collagen type I, although the presence of the ALP crown domain may also be necessary. Different binding affinities among the bone ALP isoforms may influence the mineral-collagen interface, mineralization kinetics, and degree of bone matrix mineralization, which are important factors determining the material properties of bone. |
| Databáze: | OpenAIRE |
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