Arginine Promotes the Expression of Aquaporin-3 and Water Transport in Porcine Trophectoderm Cells Through NO- and cAMP-Dependent Mechanisms

Bibliographic Details
Title: Arginine Promotes the Expression of Aquaporin-3 and Water Transport in Porcine Trophectoderm Cells Through NO- and cAMP-Dependent Mechanisms
Authors: Cui Zhu, Jinling Ye, Yinshan Bai, Shengdi Hu, Chengquan Tan, Fuller W. Bazer, Gregory A. Johnson, Zongyong Jiang, Guoyao Wu
Source: Frontiers in Bioscience-Landmark, Vol 27, Iss 3, p 083 (2022)
Publisher Information: IMR Press, 2022.
Publication Year: 2022
Collection: LCC:Biochemistry
LCC:Biology (General)
Subject Terms: arginine, aquaporin-3, pig, placenta, pregnancy, camp pathway, Biochemistry, QD415-436, Biology (General), QH301-705.5
More Details: 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2768-6701
Relation: https://www.imrpress.com/journal/FBL/27/3/10.31083/j.fbl2703083; https://doaj.org/toc/2768-6701
DOI: 10.31083/j.fbl2703083
Access URL: https://doaj.org/article/76c5c446d56842cbac5df9d43e0222dc
Accession Number: edsdoj.76c5c446d56842cbac5df9d43e0222dc
Database: Directory of Open Access Journals
More Details
ISSN:27686701
DOI:10.31083/j.fbl2703083
Published in:Frontiers in Bioscience-Landmark
Language:English