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FXYD-11 associates with Na+-K+-ATPase in the gill of Atlantic salmon: regulation and localization in relation to changed ion-regulatory status.
Am J Physiol Regul Integr Comp Physiol. 2010 Nov; 299(5):R1212-23.AJ

Abstract

The Na(+)-K(+)-ATPase is the primary electrogenic component driving transepithelial ion transport in the teleost gill; thus regulation of its level of activity is of critical importance for osmotic homeostasis. In the present study, we examined the dynamics of the gill-specific FXYD-11 protein, a putative regulatory subunit of the pump, in Atlantic salmon during seawater (SW) acclimation, smoltification, and treatment with cortisol, growth hormone, and prolactin. Dual-labeling immunohistochemistry showed that branchial FXYD-11 is localized in Na(+)-K(+)-ATPase immunoreactive cells, and coimmunoprecipitation experiments confirmed a direct association between FXYD-11 and the Na(+)-K(+)-ATPase α-subunit. Transfer of freshwater (FW)-acclimated salmon to SW induced a parallel increase in total α-subunit and FXYD-11 protein expression. A similar concurrent increase was seen during smoltification in FW. In FW fish, cortisol induced an increase in both α-subunit and FXYD-11 abundance, and growth hormone further stimulated FXYD-11 levels. In SW fish, prolactin induced a decrease in FXYD-11 and α-subunit protein levels. In vitro cortisol (18 h, 10 μg/ml) stimulated FXYD-11, but not FXYD-9, mRNA levels in gills from FW and SW salmon. The data show that Na(+)-K(+)-ATPase expressed in branchial mitochondrion-rich cells is accompanied by FXYD-11, and that regulation of the two proteins is highly coordinated. The demonstrated association of FXYD-11 and α-subunit strengthens our hypothesis that FXYD-11 has a role in modulating the pump's kinetic properties. The presence of putative phosphorylation sites on the intracellular domain of FXYD-11 suggests the possibility that this protein also may transmit external signals that regulate Na(+)-K(+)-ATPase activity.

Authors+Show Affiliations

Institute of Biology, University of Southern Denmark, Odense, Denmark. tipsmark@uark.eduNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20702795

Citation

Tipsmark, Christian K., et al. "FXYD-11 Associates With Na+-K+-ATPase in the Gill of Atlantic Salmon: Regulation and Localization in Relation to Changed Ion-regulatory Status." American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, vol. 299, no. 5, 2010, pp. R1212-23.
Tipsmark CK, Mahmmoud YA, Borski RJ, et al. FXYD-11 associates with Na+-K+-ATPase in the gill of Atlantic salmon: regulation and localization in relation to changed ion-regulatory status. Am J Physiol Regul Integr Comp Physiol. 2010;299(5):R1212-23.
Tipsmark, C. K., Mahmmoud, Y. A., Borski, R. J., & Madsen, S. S. (2010). FXYD-11 associates with Na+-K+-ATPase in the gill of Atlantic salmon: regulation and localization in relation to changed ion-regulatory status. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, 299(5), R1212-23. https://doi.org/10.1152/ajpregu.00015.2010
Tipsmark CK, et al. FXYD-11 Associates With Na+-K+-ATPase in the Gill of Atlantic Salmon: Regulation and Localization in Relation to Changed Ion-regulatory Status. Am J Physiol Regul Integr Comp Physiol. 2010;299(5):R1212-23. PubMed PMID: 20702795.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - FXYD-11 associates with Na+-K+-ATPase in the gill of Atlantic salmon: regulation and localization in relation to changed ion-regulatory status. AU - Tipsmark,Christian K, AU - Mahmmoud,Yasser A, AU - Borski,Russell J, AU - Madsen,Steffen S, Y1 - 2010/08/11/ PY - 2010/8/13/entrez PY - 2010/8/13/pubmed PY - 2010/12/14/medline SP - R1212 EP - 23 JF - American journal of physiology. Regulatory, integrative and comparative physiology JO - Am. J. Physiol. Regul. Integr. Comp. Physiol. VL - 299 IS - 5 N2 - The Na(+)-K(+)-ATPase is the primary electrogenic component driving transepithelial ion transport in the teleost gill; thus regulation of its level of activity is of critical importance for osmotic homeostasis. In the present study, we examined the dynamics of the gill-specific FXYD-11 protein, a putative regulatory subunit of the pump, in Atlantic salmon during seawater (SW) acclimation, smoltification, and treatment with cortisol, growth hormone, and prolactin. Dual-labeling immunohistochemistry showed that branchial FXYD-11 is localized in Na(+)-K(+)-ATPase immunoreactive cells, and coimmunoprecipitation experiments confirmed a direct association between FXYD-11 and the Na(+)-K(+)-ATPase α-subunit. Transfer of freshwater (FW)-acclimated salmon to SW induced a parallel increase in total α-subunit and FXYD-11 protein expression. A similar concurrent increase was seen during smoltification in FW. In FW fish, cortisol induced an increase in both α-subunit and FXYD-11 abundance, and growth hormone further stimulated FXYD-11 levels. In SW fish, prolactin induced a decrease in FXYD-11 and α-subunit protein levels. In vitro cortisol (18 h, 10 μg/ml) stimulated FXYD-11, but not FXYD-9, mRNA levels in gills from FW and SW salmon. The data show that Na(+)-K(+)-ATPase expressed in branchial mitochondrion-rich cells is accompanied by FXYD-11, and that regulation of the two proteins is highly coordinated. The demonstrated association of FXYD-11 and α-subunit strengthens our hypothesis that FXYD-11 has a role in modulating the pump's kinetic properties. The presence of putative phosphorylation sites on the intracellular domain of FXYD-11 suggests the possibility that this protein also may transmit external signals that regulate Na(+)-K(+)-ATPase activity. SN - 1522-1490 UR - https://www.unboundmedicine.com/medline/citation/20702795/FXYD_11_associates_with_Na+_K+_ATPase_in_the_gill_of_Atlantic_salmon:_regulation_and_localization_in_relation_to_changed_ion_regulatory_status_ L2 - http://www.physiology.org/doi/full/10.1152/ajpregu.00015.2010?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -