Natural anti-proteases in rainbow trout, Oncorhynchus mykiss and brook charr, Salvelinus fontinalis and the in vitro neutralization of fish α2-macroglobulin by the metalloprotease from the pathogenic haemoflagellate, Cryptobia salmositica

Parasitology ◽  
1997 ◽  
Vol 114 (4) ◽  
pp. 375-382 ◽  
Author(s):  
X. ZUO ◽  
P. T. K. WOO

Natural anti-proteases (α1-protease inhibitor (α1-PI; α1-antitrypsin) and α2-macroglobulin (α2-M)) were found in the blood of rainbow trout, Oncorhynchus mykiss and brook charr, Salvelinus fontinalis. The α2-M inhibited Cryptobia salmositica proteases and was significantly higher in brook charr than in rainbow trout. Under in vitro conditions it took longer for the same number of parasites to neutralize the α2-M in charr than in trout blood. The haemolysis which occurred when C. salmositica was incubated in the blood of rainbow trout was due to neutralization of α2-M. This in vitro study also showed that it was the metalloprotease of C. salmositica that lysed red blood cells and the plasma of the two species of fishes initially prevented haemolysis by inhibiting the proteolytic activity. We suggest that the natural plasma α2-M plays an important role in defence against cryptobiosis in fishes.

1998 ◽  
Vol 76 (7) ◽  
pp. 1325-1328 ◽  
Author(s):  
J M McLeese ◽  
J G Eales

We exposed rainbow trout, Oncorhynchus mykiss, to various environmental conditions known to alter thyroid function in order to determine their effects on the in vitro carrier-mediated transport rate (J) of 3,5,3prime-triiodo-L-thyronine (T3) into red blood cells (RBC). Values for J (fmol T3 transported/(106 cells · min)) were (i) increased by assay temperature from 0 to 12°C but not from 12 to 21°C, (ii) unaltered by acclimation for 14 d at 5 or 12°C, (iii) depressed by a restricted food ration (0.5% of mean body mass/d) but unaltered by 14 d of fasting, (iv) depressed by a T3 challenge created by feeding T3-supplemented food (12 ppm T3) for 14 d, and (v) depressed 10 d after transport to our laboratory. We conclude that certain conditions that alter thyroid function also alter the rate of T3 transport into trout RBC, with possible consequences for exchange of T3 between plasma and RBC.


2019 ◽  
Vol 207 ◽  
pp. 43-51 ◽  
Author(s):  
Richard C. Kolanczyk ◽  
Jeffrey S. Denny ◽  
Barbara R. Sheedy ◽  
Patricia K. Schmieder ◽  
Mark A. Tapper

1993 ◽  
Vol 50 (1) ◽  
pp. 156-162 ◽  
Author(s):  
V. P. Palace ◽  
H. S. Majewski ◽  
J. F. Klaverkamp

Rainbow trout (Oncorhynchus mykiss) (mean weight 180 ± 10 g) fed diets deficient in ascorbic acid, tocopherol, both, or neither were exposed to one of three cadmium concentrations (0, 2, or 4 μg Cd/L). After 181 d of exposure, liver and whole blood were sampled. Cadmium exposure was found to significantly increase the Cd content in liver, especially in fish fed a diet deficient in ascorbic acid. Hepatic stores of ascorbic acid decreased in fish exposed to Cd and in fish fed diets deficient in tocopherol and ascorbic acid. Depletion of tocopherol in liver occurred only in those fish fed a diet deficient in tocopherol and exposed to Cd. Superoxide dismutase activity in liver increased with Cd exposure and with dietary deficiencies of tocopherol and ascorbic acid, while catalase was inhibited by exposure to Cd alone. Glutathione peroxidase activity was unaffected by Cd but was lower in fish fed a diet deficient in both tocopherol and ascorbic acid. Erythrocyte fragility, measured by spontaneous hemolysis of red blood cells in physiological saline, was increased by Cd exposure and the deficiencies of dietary tocopherol and ascorbic acid.


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