V-ATPase a3 Directs Secretory Lysosome Transport in Enamel Formation
By K. Otsu, S. Ikezaki, N. Goto-Matsumoto, A. Ikarashi, H. Sano, H. Ida-Yonemochi, H. Ohshima, G.-H. Sun-Wada, Y. Wada, M. Nakanishi-Matsui, H. Harada
Originally at journals.sagepub.com
Summary & scoring by The Bell Brief (Dr. Jennifer Bell) using the Drill-Down Protocol (Drill-Down Score) — not the original publisher.
Why it matters for dental
Maturation-stage ameloblasts rely on V-ATPase a3 to shuttle secretory lysosomes that deliver enamel-matrix proteins and regulate pH, so mutations or drug interference with this isoform could impair enamel quality and create diagnostic or restorative challenges for clinicians.
Key points
- The study shows V-ATPase a3 isoform specifically directs secretory lysosome transport in maturation ameloblasts, distinct from other a-subunit isoforms.
- Disruption of a3 function blocks protein secretion and pH control at the enamel surface, directly linking genotype to enamel defects seen in patients.
- Findings may inform future targeted therapies or diagnostics for amelogenesis imperfecta and other developmental enamel disorders.
- Practice impact: pediatric dentists and prosthodontists should consider genetic enamel-formation disorders when unexplained hypomineralization appears in multiple teeth.
Who should care
Read the original on Journal of Dental Research (JDR)
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