ISSN:
1573-5168
Keywords:
thyroid hormone
;
iodothyronines
;
deiodination
;
fish
;
tilapia
;
trout
;
catfish
;
turbot
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Abstract The presence of outer ring deiodinating (ORD) and inner ring deiodinating (IRD) activities was investigated in different tissues of Oreochromis niloticus (Nile tilapia), Clarias gariepinus (African catfish), Oncorhynchus mykiss (rainbow trout) and halmus maximus (turbot). High-Km rT3 ORD is present in the kidney of most of the fishes studied, except in catfish. In turbot, besides the kidney, rT3 ORD is also present in liver, heart and ovary. Low-Km T4 ORD is found in the liver and low-Km T3 IR the brain of all the fishes studied. In addition, low levels of low-Km T3 IRD were demonstrated in gill and skin of Nile tilapia, liver of rainbow trout and gill and kidney of turbot. For the different teleosts, the biochemical properties of the different rT3-deiodinating enzymes mentioned, T4 ORD in liver and T3 IRD in brain and tilapia gill were compared to those of the deiodinases formerly characterized in Oreochromis aureus (blue tilapia). In general, the different deiodinases demonstrate analogous sensitivities to iodothyronines and inhibitors, although minor differences occur. The various deiodinating enzymes all depend on addition of dithiothreitol and demonstrate maximal activity pH between 6.5 and 7. The optimal incubation temperature of rT3 ORD and T4 ORD in tilapia and catfish is 37 °C, in trout and turbot it varies, depending on the tissue, between 25 ° and 37 °C. For the different T3 IRD activities the optimal temperature is 37 °C in warmwater as well as in coldwater species. The apparent Km values for rT3 ORD lay in the μM range, for T4 ORD and T3 IRD they lay in the nM range. Vmax values are usually higher in tilapia as compared to the other teleosts studied. Based on the similarities in susceptibility to inhibition by different iodothyronines and inhibitors and the agreement of the apparent Km values, we conclude that the deiodinating enzymes in teleosts are more similar to mammalian deiodinases than is generally accepted.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1007722812697
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