PUBLICATION

Insight into the function of voltage-sensing phosphatase (VSP) in hind-gut derived pseudoplacenta of a viviparous teleost Xenotoca eiseni

Authors
Ratanayotha, A., Iida, A., Nomura, J., Hondo, E., Okamura, Y., Kawai, T.
ID
ZDB-PUB-240402-1
Date
2024
Source
American journal of physiology. Regulatory, integrative and comparative physiology   326(6): R461-R471 (Journal)
Registered Authors
Kawai, Takafumi, Okamura, Yasushi, Ratanayotha, Adisorn
Keywords
Xenotoca eiseni, nutrient absorption, phosphoinositides, trophotaenia, voltage-sensing phosphatase
MeSH Terms
  • Zebrafish
  • Female
  • Phosphoric Monoester Hydrolases*/genetics
  • Phosphoric Monoester Hydrolases*/metabolism
  • Enterocytes/enzymology
  • Enterocytes/metabolism
  • Fish Proteins/genetics
  • Fish Proteins/metabolism
  • Animals
  • Membrane Potentials
  • Electric Fish/metabolism
  • Electric Fish/physiology
  • Viviparity, Nonmammalian*
PubMed
38557151 Full text @ Am. J. Physiol. Regul. Integr. Comp. Physiol.
Abstract
Nutrient absorption is essential for animal survival and development. Our previous study on zebrafish reported that nutrient absorption in lysosome-rich enterocytes (LREs) is promoted by the voltage-sensing phosphatase (VSP), which regulates phosphoinositide (PIP) homeostasis via electrical signaling in biological membranes. However, it remains unknown whether this VSP function is shared by different absorptive tissues in other species. Here we focused on the function of VSP in a viviparous teleost Xenotoca eiseni, whose intra-ovarian embryos absorb nutrients from the maternal ovarian fluid through a specialized hindgut-derived pseudoplacental structure called trophotaenia. X. eiseni VSP (Xe-VSP) is expressed in trophotaenia epithelium, an absorptive tissue functionally similar to zebrafish LREs. Notably, the apical distribution of Xe-VSP in trophotaenia epithelial cells closely resembles Dr-VSP distribution in zebrafish LREs, suggesting a shared role for VSP in absorptive tissues between the two species. Electrophysiological analysis using a heterologous expression system revealed that Xe-VSP preserves functional voltage sensors and phosphatase activity with the leftward shifted voltage-sensitivity compared to zebrafish VSP (Dr-VSP). We also identified a single amino acid variation in the S4 helix of Xe-VSP as one of the factors contributing to the leftward shifted voltage-sensitivity. This study highlights the biological variation and significance of VSP in various animal species, as well as hinting at the potential role of VSP in nutrient absorption in X. eiseni trophotaenia.
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