期刊
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-MOLECULAR & INTEGRATIVE PHYSIOLOGY
卷 231, 期 -, 页码 177-187出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpa.2019.02.023
关键词
FXYD proteins; Gill; Milkfish; Na+/K+-ATPase; Salinity
资金
- Ministry of Science and Technology (MOST), Taiwan
- MOST Research Project [MOST-106-2313-B-005-038-MY3]
- iEGG and Animal Biotechnology Center from The Feature Area Research Center Program within the framework of the Higher Education Sprout Project by the Ministry of Education (MOE), Taiwan [MOE-107-S-0023-F]
- MOST
- MOE [MOE-107-S-0023-F, MOST-106-2811-B-005-004]
FXYD proteins are crucial regulators of Na+/K+-ATPase (NKA), which plays an important role in ion exchange by providing the driving force for other ion-transporting systems in the osmoregulatory organs, including the gills. In milkfish (Chanos chanos), gill NKA has been widely investigated and found to alter its expression (both mRNA and protein) and activity in response to environmental salinity changes. However, the expression and roles of the regulatory proteins of NKA, the FXYD proteins, in milkfish gills upon salinity challenge is not yet clear. Hence, this study illustrated the potential roles of milkfish branchial FXYD proteins in modulating NKA expression via identification and tissue distributions of FXYD proteins, as well as the effects of salinity on expression of gill fxyd and nka mRNA. Six milkfish FXYD proteins (CcFXYD) were identified. In milkfish gill, gill-specific Ccfxyd11 was the predominant member, followed by Ccfxyd9 and Ccfxyd8. Upon hypoosmotic challenges, increases in gill Ccfxyd11, Ccfxyd8, Ccnka alpha 1, and Ccnka beta 1 mRNA as well as significantly positive correlations were observed. Moreover, after acute salinity changes, expression of gill Ccfxyd11 and Ccnka was found to change with ambient salinity, and significant positive correlations were also exhibited between Ccfxyd11 and Ccnka alpha 1. Overall, these results revealed close relationships between CcFXYD11 and CcNKA alpha 1 in milkfish gills, highlighting the potential roles of CcFXYD11 in osmoregulation.
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