Functional complementation of V-ATPase a subunit isoforms in osteoclasts
| Autor: | Naomi Matsumoto, Yasuyuki Fujimoto, Mizuki Sekiya, Mayumi Nakanishi-Matsui, Ge-Hong Sun-Wada, Satoshi Haga, Yoh Wada |
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| Rok vydání: | 2020 |
| Předmět: |
Gene isoform
Vacuolar Proton-Translocating ATPases Protein subunit Osteoclasts Biochemistry Bone resorption Mice 03 medical and health sciences 0302 clinical medicine Osteoclast Lysosome medicine Animals V-ATPase Molecular Biology 030304 developmental biology Mice Knockout 0303 health sciences Chemistry rab7 GTP-Binding Proteins General Medicine Cell biology Resorption Isoenzymes Complementation Protein Subunits medicine.anatomical_structure rab GTP-Binding Proteins 030220 oncology & carcinogenesis Lysosomes |
| Zdroj: | The Journal of Biochemistry. 169:459-466 |
| ISSN: | 1756-2651 0021-924X |
| DOI: | 10.1093/jb/mvaa118 |
| Popis: | In osteoclasts, the a3 isoform of the proton-pumping V-ATPase plays essential roles in anterograde trafficking of secretory lysosomes and extracellular acidification required for bone resorption. This study examined functional complementation of the a isoforms by exogenously expressing the a1, a2 and a3 isoforms in a3-knockout (KO) osteoclasts. The expression levels of a1 and a2 in a3KO osteoclasts were similar, but lower than that of a3. a1 significantly localized to lysosomes, whereas a2 slightly did. On the other hand, a2 interacted with Rab7, a regulator of secretory lysosome trafficking in osteoclasts, more efficiently than a1. a1 partly complemented the functions of a3 in secretory lysosome trafficking and calcium phosphate resorption, while a2 partly complemented the former but not the latter function. |
| Databáze: | OpenAIRE |
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