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Branchial FXYD protein expression in response to salinity change and its interaction with Na+/K+-ATPase of the euryhaline teleost Tetraodon nigroviridis.
J Exp Biol. 2008 Dec; 211(Pt 23):3750-8.JE

Abstract

Na+/K+-ATPase (NKA) is a ubiquitous membrane-bound protein crucial for teleost osmoregulation. The enzyme is composed of two essential subunits, a catalytic alpha subunit and a glycosylated beta subunit which is responsible for membrane targeting of the enzyme. In mammals, seven FXYD members have been found. FXYD proteins have been identified as the regulatory protein of NKA in mammals and elasmobranchs, it is thus interesting to examine the expression and functions of FXYD protein in the euryhaline teleosts with salinity-dependent changes of gill NKA activity. The present study investigated the expression and distribution of the FXYD protein in gills of seawater (SW)- or freshwater (FW)-acclimated euryhaline pufferfish (Tetraodon nigroviridis). The full-length pufferfish FXYD gene (pFXYD) was confirmed by RT-PCR. pFXYD was found to be expressed in many organs including gills of both SW and FW pufferfish. pFXYD mRNA abundance in gills, determined by real-time PCR, was significantly higher in FW fish than in SW fish. An antiserum raised against a partial amino acid sequence of pFXYD was used for the immunoblots of gill homogenates and a major band at 13 kDa was detected. The relative amounts of pFXYD protein and mRNA in gills of SW and FW pufferfish were identical, but opposite to the expression levels of NKA. Immunofluorescent staining of frozen sections demonstrated that pFXYD was colocalized to NKA-immunoreactive cells in the gill filaments. In addition, interaction between pFXYD and NKA was demonstrated by co-immunoprecipitation. Taken together, salinity-dependent expression of pFXYD protein and NKA, as well as the evidence for their colocalization and interaction in pufferfish gills suggested that pFXYD regulates NKA activity in gills of euryhaline teleosts upon salinity challenge.

Authors+Show Affiliations

Department of Life Sciences, National Chung-Hsing University, Taichung 402, Taiwan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19011216

Citation

Wang, Pei-Jen, et al. "Branchial FXYD Protein Expression in Response to Salinity Change and Its Interaction With Na+/K+-ATPase of the Euryhaline Teleost Tetraodon Nigroviridis." The Journal of Experimental Biology, vol. 211, no. Pt 23, 2008, pp. 3750-8.
Wang PJ, Lin CH, Hwang HH, et al. Branchial FXYD protein expression in response to salinity change and its interaction with Na+/K+-ATPase of the euryhaline teleost Tetraodon nigroviridis. J Exp Biol. 2008;211(Pt 23):3750-8.
Wang, P. J., Lin, C. H., Hwang, H. H., & Lee, T. H. (2008). Branchial FXYD protein expression in response to salinity change and its interaction with Na+/K+-ATPase of the euryhaline teleost Tetraodon nigroviridis. The Journal of Experimental Biology, 211(Pt 23), 3750-8. https://doi.org/10.1242/jeb.018440
Wang PJ, et al. Branchial FXYD Protein Expression in Response to Salinity Change and Its Interaction With Na+/K+-ATPase of the Euryhaline Teleost Tetraodon Nigroviridis. J Exp Biol. 2008;211(Pt 23):3750-8. PubMed PMID: 19011216.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Branchial FXYD protein expression in response to salinity change and its interaction with Na+/K+-ATPase of the euryhaline teleost Tetraodon nigroviridis. AU - Wang,Pei-Jen, AU - Lin,Chia-Hao, AU - Hwang,Hau-Hsuan, AU - Lee,Tsung-Han, PY - 2008/11/18/pubmed PY - 2009/2/12/medline PY - 2008/11/18/entrez SP - 3750 EP - 8 JF - The Journal of experimental biology JO - J Exp Biol VL - 211 IS - Pt 23 N2 - Na+/K+-ATPase (NKA) is a ubiquitous membrane-bound protein crucial for teleost osmoregulation. The enzyme is composed of two essential subunits, a catalytic alpha subunit and a glycosylated beta subunit which is responsible for membrane targeting of the enzyme. In mammals, seven FXYD members have been found. FXYD proteins have been identified as the regulatory protein of NKA in mammals and elasmobranchs, it is thus interesting to examine the expression and functions of FXYD protein in the euryhaline teleosts with salinity-dependent changes of gill NKA activity. The present study investigated the expression and distribution of the FXYD protein in gills of seawater (SW)- or freshwater (FW)-acclimated euryhaline pufferfish (Tetraodon nigroviridis). The full-length pufferfish FXYD gene (pFXYD) was confirmed by RT-PCR. pFXYD was found to be expressed in many organs including gills of both SW and FW pufferfish. pFXYD mRNA abundance in gills, determined by real-time PCR, was significantly higher in FW fish than in SW fish. An antiserum raised against a partial amino acid sequence of pFXYD was used for the immunoblots of gill homogenates and a major band at 13 kDa was detected. The relative amounts of pFXYD protein and mRNA in gills of SW and FW pufferfish were identical, but opposite to the expression levels of NKA. Immunofluorescent staining of frozen sections demonstrated that pFXYD was colocalized to NKA-immunoreactive cells in the gill filaments. In addition, interaction between pFXYD and NKA was demonstrated by co-immunoprecipitation. Taken together, salinity-dependent expression of pFXYD protein and NKA, as well as the evidence for their colocalization and interaction in pufferfish gills suggested that pFXYD regulates NKA activity in gills of euryhaline teleosts upon salinity challenge. SN - 0022-0949 UR - https://www.unboundmedicine.com/medline/citation/19011216/Branchial_FXYD_protein_expression_in_response_to_salinity_change_and_its_interaction_with_Na+/K+_ATPase_of_the_euryhaline_teleost_Tetraodon_nigroviridis_ L2 - http://jeb.biologists.org/cgi/pmidlookup?view=long&pmid=19011216 DB - PRIME DP - Unbound Medicine ER -