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Open AccessArticle

Rainbow Trout (Oncorhynchus mykiss) Na+/H+ Exchangers tNhe3a and tNhe3b Display Unique Inhibitory Profiles Dissimilar from Mammalian NHE Isoforms

1
Department of Biology, Winthrop University, Rock Hill, SC 29733, USA
2
Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E9, Canada
3
Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada
*
Author to whom correspondence should be addressed.
Current Address: Department of Biotechnology, Thapar Institute of Engineering and Technology Patiala, Patiala 147004, India.
Academic Editor: Yoshinori Marunaka
Int. J. Mol. Sci. 2021, 22(4), 2205; https://doi.org/10.3390/ijms22042205 (registering DOI)
Received: 2 February 2021 / Revised: 17 February 2021 / Accepted: 20 February 2021 / Published: 23 February 2021
(This article belongs to the Section Biochemistry)
Freshwater fishes maintain an internal osmolality of ~300 mOsm, while living in dilute environments ranging from 0 to 50 mOsm. This osmotic challenge is met at least partially, by Na+/H+ exchangers (NHE) of fish gill and kidney. In this study, we cloned, expressed, and pharmacologically characterized fish-specific Nhes of the commercially important species Oncorhynchus mykiss. Trout (t) Nhe3a and Nhe3b isoforms from gill and kidney were expressed and characterized in an NHE-deficient cell line. Western blotting and immunocytochemistry confirmed stable expression of the tagged trout tNhe proteins. To measure NHE activity, a transient acid load was induced in trout tNhe expressing cells and intracellular pH was measured. Both isoforms demonstrated significant activity and recovered from an acute acid load. The effect of the NHE transport inhibitors amiloride, EIPA (5-(N-ethyl-N-isopropyl)-amiloride), phenamil, and DAPI was examined. tNhe3a was inhibited in a dose-dependent manner by amiloride and EIPA and tNhe3a was more sensitive to amiloride than EIPA, unlike mammalian NHE1. tNhe3b was inhibited by high concentrations of amiloride, while even in the presence of high concentrations of EIPA (500 µM), some activity of tNhe3b remained. Phenamil and DAPI were ineffective at inhibiting tNhe activity of either isoform. The current study aids in understanding the pharmacology of fish ion transporters. Both isoforms display inhibitory profiles uniquely different from mammalian NHEs and show resistance to inhibition. Our study allows for more direct interpretation of past, present, and future fish-specific sodium transport studies, with less reliance on mammalian NHE data for interpretation. View Full-Text
Keywords: AP-1; fish physiology; ion-regulation; pharmacology; pH regulation AP-1; fish physiology; ion-regulation; pharmacology; pH regulation
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MDPI and ACS Style

Blair, S.; Li, X.; Dutta, D.; Chamot, D.; Fliegel, L.; Goss, G. Rainbow Trout (Oncorhynchus mykiss) Na+/H+ Exchangers tNhe3a and tNhe3b Display Unique Inhibitory Profiles Dissimilar from Mammalian NHE Isoforms. Int. J. Mol. Sci. 2021, 22, 2205. https://doi.org/10.3390/ijms22042205

AMA Style

Blair S, Li X, Dutta D, Chamot D, Fliegel L, Goss G. Rainbow Trout (Oncorhynchus mykiss) Na+/H+ Exchangers tNhe3a and tNhe3b Display Unique Inhibitory Profiles Dissimilar from Mammalian NHE Isoforms. International Journal of Molecular Sciences. 2021; 22(4):2205. https://doi.org/10.3390/ijms22042205

Chicago/Turabian Style

Blair, Salvatore; Li, Xiuju; Dutta, Debajyoti; Chamot, Danuta; Fliegel, Larry; Goss, Greg. 2021. "Rainbow Trout (Oncorhynchus mykiss) Na+/H+ Exchangers tNhe3a and tNhe3b Display Unique Inhibitory Profiles Dissimilar from Mammalian NHE Isoforms" Int. J. Mol. Sci. 22, no. 4: 2205. https://doi.org/10.3390/ijms22042205

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