The a subunit isoforms of vacuolar-type proton ATPase exhibit differential distribution in mouse perigastrulation embryos

• Published in: Scientific reports Vol. 12; no. 1; p. 13590
• Main Authors: Sun-Wada, Ge-Hong, Wada, Yoh
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 10-08-2022; Nature Publishing Group; Nature Portfolio
• Subjects: 631/136; 631/80; Acidification; Developmental stages; Differential distribution; Embryogenesis; Embryonic growth stage; Embryos; Endoderm; Gastrulation; H+-transporting ATPase; Humanities and Social Sciences; Isoforms; Mammalian cells; multidisciplinary; Science; Science (multidisciplinary); Signal transduction; Vacuoles
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-022-18002-4

Vacuolar-type H
+
-ATPases (V-ATPases) are large multi-subunit complexes that play critical roles in the acidification of a variety of intracellular or extracellular compartments. Mammalian cells contain four isoforms of the membrane integral subunit a (a1–a4); these isoforms contain the information necessary to target the enzyme to different cellular destinations. They are also involved in regulating the efficiency of ATP hydrolysis and proton transport. Previously, we showed that early embryogenesis requires V-ATPase function, and the luminal acidic endocytic and lysosomal compartments in the visceral endoderm of mouse embryos at the pre-gastrulation stage (E6.5) are essential for both nutrition and signal transduction during early embryogenesis. In this study, we examined the expression and distribution of a subunit isoforms in mouse embryos at E6.5. We found that all four isoforms expressed and exhibited differential distribution in the E6.5 embryo. At this developmental stage, the embryos establish highly elaborate endocytic compartments called apical vacuoles, on which the a3 isoform specifically accumulated.