scholarly journals Temperature-dependent protection against Ichthyophthirius multifiliis following immunisation of rainbow trout using live theronts

2006 ◽  
Vol 72 ◽  
pp. 269-273 ◽  
Author(s):  
M Alishahi ◽  
K Buchmann
2019 ◽  
Vol 86 ◽  
pp. 486-496 ◽  
Author(s):  
Khairul Syahputra ◽  
Per W. Kania ◽  
Azmi Al-Jubury ◽  
Rzgar M. Jafaar ◽  
Ron P. Dirks ◽  
...  

1987 ◽  
Vol 129 (1) ◽  
pp. 107-123 ◽  
Author(s):  
A. P. Farrell

A preparation was developed to perfuse the coronary circulation in working hearts from rainbow trout (Salmo gairdneri Richardson). The preparation was used to examine pressure-flow relationships for the coronary circulation as the heart generated physiological and subphysiological work loads. Coronary vascular resistance increased exponentially as coronary flow rate decreased. Coronary resistance was also influenced by cardiac metabolism and acclimation temperature. When heart rate was increased, extravascular compression increased in coronary resistance. Direct vasoconstriction of the coronary vessels, produced by injections of adrenaline into the coronary circulation, was temperature-dependent.


Aquaculture ◽  
2020 ◽  
Vol 526 ◽  
pp. 735384
Author(s):  
Khairul Syahputra ◽  
Per W. Kania ◽  
Azmi Al-Jubury ◽  
Huria Marnis ◽  
Heidi Mathiessen ◽  
...  

2009 ◽  
Vol 41 (3) ◽  
pp. 152-157 ◽  
Author(s):  
A.P. Shinn ◽  
S.M. Picon-Camacho ◽  
R. Bawden ◽  
N.G.H. Taylor

2013 ◽  
Vol 45 (18) ◽  
pp. 866-875 ◽  
Author(s):  
Christine E. Genge ◽  
William S. Davidson ◽  
Glen F. Tibbits

The teleost-specific whole genome duplication created multiple copies of genes allowing for subfunctionalization of isoforms. In this study, we show that the teleost cardiac Ca2+-binding troponin C (TnC) is the product of two distinct genes: cardiac TnC (cTnC, TnnC1a) and a fish-specific slow skeletal TnC (ssTnC, TnnC1b). The ssTnC gene is novel to teleosts as mammals have a single gene commonly referred as cTnC but which is also expressed in slow skeletal muscle. In teleosts, the data strongly indicate that these are two TnC genes are different paralogs. Because we determined that ssTnC exists across many teleosts but not in basal ray-finned fish (e.g., bichir), we propose that these paralogs are the result of an ancestral tandem gene duplication persisting only in teleosts. Quantification of mRNA levels was used to demonstrate distinct expression localization patterns of the paralogs within the chambers of the heart. In the adult zebrafish acclimated at 28°C, ssTnC mRNA levels are twofold greater than cTnC mRNA levels in the atrium, whereas cTnC mRNA was almost exclusively expressed in the ventricle. Meanwhile, rainbow trout acclimated at 5°C showed cTnC mRNA levels in both chambers significantly greater than ssTnC. Distinct responses to temperature acclimation were also quantified in both adult zebrafish and rainbow trout, with mRNA in both chambers shifting to express higher levels of cTnC in 18°C acclimated zebrafish and 5°C acclimated trout. Possible subfunctionalization of TnC isoforms may provide insight into how teleosts achieve physiological versatility in chamber-specific contractile properties.


2011 ◽  
Vol 30 (3) ◽  
pp. 859-869 ◽  
Author(s):  
Moonika M. Olsen ◽  
Per W. Kania ◽  
Rasmus D. Heinecke ◽  
Karsten Skjoedt ◽  
Karina J. Rasmussen ◽  
...  

1969 ◽  
Vol 111 (3) ◽  
pp. 287-295 ◽  
Author(s):  
H. W. Behrisch ◽  
P. W. Hochachka

1. The properties of fructose diphosphatase from the liver of rainbow trout (Salmo gairdnerii) were examined over the physiological temperature range of the organism. 2. Saturation curves for substrate (fructose 1,6-diphosphate) and a cofactor (Mg2+) are sigmoidal, and Hill plots of the results suggest a minimum of two interacting fructose 1,6-diphosphate sites and two interacting Mg2+ sites per molecule of enzyme. 3. Mn2+-saturation curves are hyperbolic, and the Ka for Mn2+, which inhibits the enzyme at high concentrations, is 50–100-fold lower than the Ka for Mg2+. 4. Fructose diphosphatase is inhibited by low concentrations of AMP; this inhibition appears to be decreased and reversed by increasing the concentrations of Mg2+ and Mn2+. Higher concentrations of AMP are required to inhibit the trout fructose diphosphatase in the presence of Mn2+. 5. The affinities of fructose diphosphatase for fructose diphosphate and Mn2+ appear to be temperature-independent, whereas the affinities for Mg2+ and AMP are highly temperature-dependent. 6. The pH optimum of the enzyme depends on the concentrations of Mg2+ and Mn2+. In addition, pH determines the Ka for Mg2+; at high pH, Ka for Mg2+ is lowered. 7. The enzyme is inhibited by Ca2+ and Zn2+, and the inhibition is competitive with respect to both cations. 8. The possible roles of these ions and AMP in the modulation of fructose diphosphatase and gluconeogenic activity are discussed in relation to temperature adaptation.


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