scholarly journals The osmotic response of the Asian freshwater stingray (Himantura signifer) to increased salinity: a comparison with marine (Taeniura lymma) and Amazonian freshwater (Potamotrygon motoro) stingrays

2003 ◽  
Vol 206 (17) ◽  
pp. 2931-2940 ◽  
Author(s):  
W. L. Tam
2006 ◽  
Vol 211 (5) ◽  
pp. 507-518 ◽  
Author(s):  
Kannika Chatchavalvanich ◽  
Ricardo Marcos ◽  
Jintana Poonpirom ◽  
Amara Thongpan ◽  
Eduardo Rocha

2005 ◽  
Vol 52 (4) ◽  
pp. 379-385 ◽  
Author(s):  
Kannika Chatchavalvanich ◽  
Amara Thongpan ◽  
Masaaki Nakai

Copeia ◽  
1997 ◽  
Vol 1997 (1) ◽  
pp. 101 ◽  
Author(s):  
William Raschi ◽  
Elaine D. Keithan ◽  
William C. H. Rhee

Heliyon ◽  
2021 ◽  
Vol 7 (4) ◽  
pp. e06763
Author(s):  
Babatunde Adeleke ◽  
Deborah Robertson-Andersson ◽  
Gan Moodley

2004 ◽  
Vol 3 (6) ◽  
pp. 1544-1556 ◽  
Author(s):  
Jade Mei-Yeh Lu ◽  
Robert J. Deschenes ◽  
Jan S. Fassler

ABSTRACT Yeast Sln1p is an osmotic stress sensor with histidine kinase activity. Modulation of Sln1 kinase activity in response to changes in the osmotic environment regulates the activity of the osmotic response mitogen-activated protein kinase pathway and the activity of the Skn7p transcription factor, both important for adaptation to changing osmotic stress conditions. Many aspects of Sln1 function, such as how kinase activity is regulated to allow a rapid response to the continually changing osmotic environment, are not understood. To gain insight into Sln1p function, we conducted a two-hybrid screen to identify interactors. Mog1p, a protein that interacts with the yeast Ran1 homolog, Gsp1p, was identified in this screen. The interaction with Mog1p was characterized in vitro, and its importance was assessed in vivo. mog1 mutants exhibit defects in SLN1-SKN7 signal transduction and mislocalization of the Skn7p transcription factor. The requirement for Mog1p in normal localization of Skn7p to the nucleus does not fully account for the mog1-related defects in SLN1-SKN7 signal transduction, raising the possibility that Mog1p may play a role in Skn7 binding and activation of osmotic response genes.


2002 ◽  
Vol 283 (4) ◽  
pp. R983-R992 ◽  
Author(s):  
Peter M. Piermarini ◽  
Jill W. Verlander ◽  
Ines E. Royaux ◽  
David H. Evans

Pendrin is an anion exchanger in the cortical collecting duct of the mammalian nephron that appears to mediate apical Cl−/HCO[Formula: see text]exchange in bicarbonate-secreting intercalated cells. The goals of this study were to determine 1) if pendrin immunoreactivity was present in the gills of a euryhaline elasmobranch (Atlantic stingray, Dasyatis sabina), and 2) if branchial pendrin immunoreactivity was influenced by environmental salinity. Immunoblots detected pendrin immunoreactivity in Atlantic stingray gills; pendrin immunoreactivity was greatest in freshwater stingrays compared with freshwater stingrays acclimated to seawater (seawater acclimated) and marine stingrays. Using immunohistochemistry, pendrin-positive cells were detected on both gill lamellae and interlamellar regions of freshwater stingrays but were more restricted to interlamellar regions in seawater-acclimated and marine stingray gills. Pendrin immunolabeling in freshwater stingray gills was more apical, discrete, and intense compared with seawater-acclimated and marine stingrays. Regardless of salinity, pendrin immunoreactivity occurred on the apical region of cells rich with basolateral vacuolar-proton-ATPase, and not in Na+-K+-ATPase-rich cells. We suggest that a pendrin-like transporter may contribute to apical Cl−/HCO[Formula: see text] exchange in gills of Atlantic stingrays from both freshwater and marine environments.


1999 ◽  
Vol 274 (29) ◽  
pp. 20185-20190 ◽  
Author(s):  
Varsha Nadkarni ◽  
Kenneth H. Gabbay ◽  
Kurt M. Bohren ◽  
David Sheikh-Hamad

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