The effect of pH on plasma electrolytes, carbonic anhydrase and ATPase activities in rainbow trout (Salmo gairdnerii) and largescale suckers (Catostomus macrocheilus)

1985 ◽  
Vol 80 (4) ◽  
pp. 507-514 ◽  
Author(s):  
B.A. McKeown ◽  
G.H. Geen ◽  
T.A. Watson ◽  
J.F. Powell ◽  
D.B. Parker
Keyword(s):  
Rainbow Trout ◽  
Carbonic Anhydrase ◽  
Effect Of Ph ◽  
Plasma Electrolytes ◽  
Catostomus Macrocheilus

Shortening of Branchial Tight Junction Acid-Exposed Rainbow Trout (Oncorhynchus mykiss)

1991 ◽  
Vol 48 (10) ◽  
pp. 2028-2033 ◽  
Author(s):  
J. Freda ◽  
D. A. Sanchez ◽  
H. L. Bergman
Keyword(s):  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
Tight Junctions ◽  
Relative Magnitude ◽  
Chloride Cells ◽  
Pavement Cells ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Plasma Electrolytes ◽  
Gill Structure ◽  
Electrolyte Loss

The objective of this study was to investigate possible sites for Na+ loss in fish exposed to low environmental pH. In rainbow trout (Oncorhynchus mykiss) exposed to pH 4.0 for 1 h, a net loss of Na+ was stimulated, and changes in gill structure occurred. In addition to epithelial lifting and necrosis in the gills of acid-exposed fish, tight junctions between pavement epithelial cells and chloride cells decreased in length by 25% whereas tight junctions between adjacent pavement cells did not significantly change. In a second experiment where fish were moved from pH 4.0 or 3.5 water to pH 6.5 water, we observed that Na+ loss declined immediately and approached control levels. The reversible nature of the stimulation of Na+ loss indicates that the site of Na+ loss in the fish gill can be reversibly opened and closed, which is consistent with the known properties of tight junctions. We hypothesize that the opening of tight junctions contributes to the loss of plasma electrolytes at low environmental pH. However, the relative magnitude of electrolyte loss through the tight junctions remains unknown.

Effect of pH on structure, function, and stability of mitochondrial carbonic anhydrase VA

2016 ◽  
Vol 35 (2) ◽  
pp. 449-461 ◽  
Author(s):  
Danish Idrees ◽  
Mohd. Shahbaaz ◽  
Krishna Bisetty ◽  
Asimul Islam ◽  
Faizan Ahmad ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Structure Function ◽  
Effect Of Ph

Intestinal carbonic anhydrase, bicarbonate, and proton carriers play a role in the acclimation of rainbow trout to seawater

2007 ◽  
Vol 293 (5) ◽  
pp. R2099-R2111 ◽  
Author(s):  
Martin Grosell ◽  
Katie M. Gilmour ◽  
Steven F. Perry
Keyword(s):  
Rainbow Trout ◽  
Carbonic Anhydrase ◽  
Enzymatic Activity ◽  
Intestinal Epithelium ◽  
Ionic Composition ◽  
Extracellular Fluid ◽  
Fold Increase ◽  
Mrna Levels ◽  
Intestinal Fluid ◽  
Fluid Chemistry

Abrupt transfer of rainbow trout from freshwater to 65% seawater caused transient disturbances in extracellular fluid ionic composition, but homeostasis was reestablished 48 h posttransfer. Intestinal fluid chemistry revealed early onset of drinking and slightly delayed intestinal water absorption that coincided with initiation of NaCl absorption and HCO3− secretion. Suggestive of involvement in osmoregulation, relative mRNA levels for vacuolar H+-ATPase (V-ATPase), Na+-K+-ATPase, Na+/H+ exchanger 3 (NHE3), Na+-HCO3− cotransporter 1, and two carbonic anhydrase (CA) isoforms [a general cytosolic isoform trout cytoplasmic CA (tCAc) and an extracellular isoform trout membrane-bound CA type IV (tCAIV)], were increased transiently in the intestine following exposure to 65% seawater. Both tCAc and tCAIV proteins were localized to apical regions of the intestinal epithelium and exhibited elevated enzymatic activity after acclimation to 65% seawater. The V-ATPase was localized to both basolateral and apical regions and exhibited a 10-fold increase in enzymatic activity in fish acclimated to 65% seawater, suggesting a role in marine osmoregulation. The intestinal epithelium of rainbow trout acclimated to 65% seawater appears to be capable of both basolateral and apical H+ extrusion, likely depending on osmoregulatory status and intestinal fluid chemistry.

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