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Cation/Ca2+ Exchanger 1 (MdCCX1), a Plasma Membrane-Localized Na+ Transporter, Enhances Plant Salt Tolerance by Inhibiting Excessive Accumulation of Na+ and Reactive Oxygen Species

ABSTRACT: High salinity causes severe damage to plant growth and significantly reduces crop yields. The CCX family proteins can facilitate the transport of multiple ions to prevent toxicity. CCX proteins play an important role in regulating plant salt tolerance, but no detailed studies on CCX proteins in apples have been reported. Here, the CCX family gene MdCCX1 was cloned from apple (Malus domestica). It is constitutively expressed in various apple tissues and is significantly induced by salt stress. As a plasma membrane-localized protein, MdCCX1-overexpression could complement the Na+-sensitive phenotype of yeast mutants and reduce the Na+ content in yeast cells under NaCl treatment, suggesting that MdCCX1 could be a plasma membrane-localized Na+ transporter. To identify the function of MdCCX1 in salt response, we transformed this gene into Arabidopsis, apple calli, and apple plants. Overexpression of MdCCX1 significantly improved the salt tolerance of these transgenic materials. The significantly reduced Na+ content under NaCl treatment indicated that MdCCX1 overexpression could enhance plant salt tolerance by inhibiting the excessive accumulation of Na+. Besides, MdCCX1 overexpression could also enhance plant salt tolerance by promoting ROS scavenging. These findings provide new insight and rich resources for future studies of CCX proteins in plant species.

SUBMITTER: Yang J

PROVIDER: S-EPMC8549818 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Introduction: Safranal, which endows saffron its unique aroma, causes vasodilatation and has a hypotensive effect in animal studies, but the mechanisms of these effects are unknown. In this study, we investigated the mechanisms of safranal vasodilation. Methods: Isolated rat endothelium-intact or -denuded aortic rings were precontracted with phenylephrine and then relaxed with safranal. To further assess the involvement of nitric oxide, prostaglandins, guanylate cyclase, and phospholipase A2 in safranal-induced vasodilation, aortic rings were preincubated with L-NAME, indomethacin, methylene blue, or quinacrine, respectively, then precontracted with phenylephrine, and safranal concentration-response curves were established. To explore the effects of safranal on Ca2+ influx, phenylephrine and CaCl2 concentration-response curves were established in the presence of safranal. Furthermore, the effect of safranal on aortic rings in the presence of ouabain, a Na+-K+ ATPase inhibitor, was studied to explore the contribution of Na+/Ca2+ exchanger to this vasodilation. Results: Safranal caused vasodilation in endothelium-intact and endothelium-denuded aortic rings. The vasodilation was not eliminated by pretreatment with L-NAME, indomethacin, methylene blue, or quinacrine, indicating the lack of a role for NO/cGMP. Safranal significantly inhibited the maximum contractions induced by phenylephrine, or by CaCl2 in Ca2+-free depolarizing buffer. Safranal also relaxed contractions induced by ouabain, but pretreatment with safranal totally abolished the development of ouabain contractions. Discussion/Conclusion: Inhibition of Na+-K+ ATPase by ouabain leads to the accumulation of Na+ intracellularly, forcing the Na+/Ca2+ exchanger to work in reverse mode, thus causing a contraction. Inhibition of the development of this contraction by preincubation with safranal indicates that safranal inhibited the Na+/Ca2+ exchanger. We conclude that safranal vasodilation is mediated by the inhibition of calcium influx from extracellular space through L-type Ca2+ channels and by the inhibition of the Na+/Ca2+ exchanger.

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Cation/Ca2+ Exchanger 1 (MdCCX1), a Plasma Membrane-Localized Na+ Transporter, Enhances Plant Salt Tolerance by Inhibiting Excessive Accumulation of Na+ and Reactive Oxygen Species

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