TY - JOUR
T1 - Immunolocalisation of sodium/proton exchanger-like proteins in the gills of elasmobranchs
AU - Edwards, S. L.
AU - Donald, J. A.
AU - Toop, T.
AU - Donowitz, M.
AU - Tse, C. M.
N1 - Funding Information:
The authors would like to thank Mr Rod Watson (Queenscliff Marine Station) and Dr Terry Walker (Marine and Freshwater Resources Institute) for supplying and caring for the animals used in these experiments. Financial support for the study was provided by the School of Biological and Chemical Sciences, Deakin University, and a Deakin University Postgraduate Scholarship to S.L.E.
PY - 2002
Y1 - 2002
N2 - Na+/H+ exchangers are integral membrane proteins that exchange Na+ and H+ across cell membranes. The Na+/H+ exchangers 2 and 3 are epithelial isoforms in mammals and contribute to acid-base homeostasis. The gills of fishes, including elasmobranchs, are also associated with acid/base balance, and are probably the primary acid/base regulatory organ. This study examines the presence of Na+/H+ exchangers 2 and 3 using immunohistochemistry and immunoblotting in the gills of four species of elasmobranchs, the banjo ray (Trygonorrhina fasciata), southern eagle ray (Myliobatis australis), the gummy shark (Mustelus antarcticus) and the Australian angel shark (Squatina australis) using heterologous antibodies. Na+/H+ exchanger 2-like immunoreactivity was observed in the gills of the banjo ray, eagle ray and angel shark. In the banjo and eagle rays, this Na+/H+ exchanger-like immunoreactivity co-localised with immunoreactivity to Na+/K+-ATPase, a marker for the mitochondrial-rich cells of fishes. Na+/H+ exchanger 3-like immunoreactivity was only observed in the gills of the angel and gummy sharks, some Na+/H+ exchanger 3-like cells also showed Na+/K+-ATPase immunoreactivity. However, immunoblotting of banjo and eagle ray gill membranes demonstrated Na+/H+ exchanger 3-like immunoreactivity, which was not consistent with the immunohistochemical results. These data demonstrate the presence of epithelial Na+/H+ exchangers 2 and 3 in the gills of elasmobranchs and a link with acid/base regulation is suggested.
AB - Na+/H+ exchangers are integral membrane proteins that exchange Na+ and H+ across cell membranes. The Na+/H+ exchangers 2 and 3 are epithelial isoforms in mammals and contribute to acid-base homeostasis. The gills of fishes, including elasmobranchs, are also associated with acid/base balance, and are probably the primary acid/base regulatory organ. This study examines the presence of Na+/H+ exchangers 2 and 3 using immunohistochemistry and immunoblotting in the gills of four species of elasmobranchs, the banjo ray (Trygonorrhina fasciata), southern eagle ray (Myliobatis australis), the gummy shark (Mustelus antarcticus) and the Australian angel shark (Squatina australis) using heterologous antibodies. Na+/H+ exchanger 2-like immunoreactivity was observed in the gills of the banjo ray, eagle ray and angel shark. In the banjo and eagle rays, this Na+/H+ exchanger-like immunoreactivity co-localised with immunoreactivity to Na+/K+-ATPase, a marker for the mitochondrial-rich cells of fishes. Na+/H+ exchanger 3-like immunoreactivity was only observed in the gills of the angel and gummy sharks, some Na+/H+ exchanger 3-like cells also showed Na+/K+-ATPase immunoreactivity. However, immunoblotting of banjo and eagle ray gill membranes demonstrated Na+/H+ exchanger 3-like immunoreactivity, which was not consistent with the immunohistochemical results. These data demonstrate the presence of epithelial Na+/H+ exchangers 2 and 3 in the gills of elasmobranchs and a link with acid/base regulation is suggested.
KW - Acid/base regulation
KW - Elasmobranch
KW - Gills
KW - Mitochondria-rich cells
KW - Na/H exchanger (NHE)
KW - Sodium/proton exchanger
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U2 - 10.1016/S1095-6433(01)00449-4
DO - 10.1016/S1095-6433(01)00449-4
M3 - Article
C2 - 11818215
AN - SCOPUS:0036163833
VL - 131
SP - 257
EP - 265
JO - Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology
JF - Comparative Biochemistry and Physiology - A Molecular and Integrative Physiology
SN - 1095-6433
IS - 2
ER -