IMR Press / FBL / Volume 27 / Issue 3 / DOI: 10.31083/j.fbl2703083
Open Access Original Research
Arginine Promotes the Expression of Aquaporin-3 and Water Transport in Porcine Trophectoderm Cells Through NO- and cAMP-Dependent Mechanisms
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1 School of Life Science and Engineering, Foshan University, 528225 Foshan, Guangdong, China
2 Institute of Animal Science, Guangdong Academy of Agricultural Sciences, 510640 Guangzhou, Guangdong, China
3 Department of Animal Science, Texas A&M University, College Station, TX 77843, USA
4 Department of Integrative Biosciences, Texas A&M University, College Station, TX 77843, USA
*Correspondence: jiangzy@gdaas.cn (Zongyong Jiang); g-wu@tamu.edu (Guoyao Wu)
These authors contributed equally.
Academic Editor: Graham Pawelec
Front. Biosci. (Landmark Ed) 2022, 27(3), 83; https://doi.org/10.31083/j.fbl2703083
Submitted: 16 December 2021 | Revised: 1 February 2022 | Accepted: 11 February 2022 | Published: 5 March 2022
Copyright: © 2022 The Author(s). Published by IMR Press.
This is an open access article under the CC BY 4.0 license.
Abstract

Background: Dietary supplementation with L-arginine (Arg) has been shown to increase the volume of fetal fluids in gestating swine. Aquaporins (AQPs), known as water channel proteins, are essential for embryonic growth and development. It was not known if Arg mediates water transport through AQPs in porcine conceptus trophectoderm (pTr2) cells. Methods: pTr2 cells derived from pregnant gilts on day 12 of gestation were cultured in customized Arg-free Dulbecco’s modified Eagle’s Ham medium (DMEM) supplemented with either 0.00, 0.25, or 0.50 mM Arg. Results: Arg treatment increased water transport and the expression of AQP3, which was abundantly expressed in pTr2 cells at both the mRNA and protein levels. Arg also increased the expression of iNOS and the synthesis of nitric oxide (NO) in pTr2 cells. The presence of Nω-nitro-L-arginine methyl ester hydrochloride (L-NAME; an inhibitor of NO synthase) significantly attenuated the Arg-induced expression of AQP3. Furthermore, 0.50 mM Arg increased the concentrations of cAMP and the abundances of phosphorylated cAMP-dependent protein kinase A (PKA), phosphorylated PKA α/β/γ, and phosphorylated CREB. These effects of Arg were mimicked by Forskolin (a cell-permeable activator of adenylyl cyclase), but inhibited by H-89 (an inhibitor of cAMP-dependent protein kinase). Conclusions: The results of this study demonstrate that Arg regulates AQP3 expression and promotes water transport in pTr2 cells through NO- and cAMP-dependent signaling pathways.

Keywords
arginine
aquaporin-3
pig
placenta
pregnancy
cAMP pathway
Figures
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