Cloning and Characterization of Type III Iodothyronine Deiodinase from the Fish Oreochromis niloticus

Sanders, J. P.

doi:10.1210/en.140.8.3666

Cited by 34 publications

(16 citation statements)

References 30 publications

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“…Highest similarities were observed with F. heteroclitus , mouse , rat (Gondou et al, 1998), and human (Croteau et al, 1996)D2. Lower simililarities were obtained with tilapia (O. niloticus) D1 (Sanders et al, 1997) and D3 (Sanders et al, 1999). X stands for selenocysteine.…”

Section: Tissue Distribution Of Rtd2 Mrnamentioning

confidence: 95%

Type II iodothyronine deiodinase is preferentially expressed in rainbow trout (oncorhynchus mykiss) liver and gonads*

Sambroni

Gutieres

Cauty

et al. 2001

Molecular Reproduction Devel

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It is well admitted that thyroid hormones (TH) play a role in the development of vertebrates. The major secretory product of the thyroid is a pro-hormone, T(4), which is activated in peripheral tissues by outer ring deiodination to T(3). We have isolated from rainbow trout testis, a full length cDNA encoding type II iodothyronine deiodinase (rtD2). The cDNA was 2410 nucleotides long and coded for a polypeptide of 264 amino acids including a selenocysteine residue. The predicted molecular weight of rtD2 was 29.3 kDa and the isoelectric point 8.71. The deduced amino acids sequence showed 80% identity with Fundulus heteroclitus D2 (fhD2) but only 68-69% identity with rat, mouse, and human D2. The 3' UTR contained a putative selenocysteine insertion sequence (SECIS) similar to that described in human cDNA. The rtD2 gene was isolated and the gene structure was similar to that described in human with two exons separated by a large intron. We studied rtD2 gene expression by Northern blot analysis using total RNA extracted from testis, ovary, and other tissues. We found a high expression of a 3 kb transcript in liver and in gonads. A lower expression was also detected in posterior kidney. In testis, rtD2 mRNA expression was dependent on spermatogenic stages: it increased at the onset of spermatogenesis. Our results show that the structural characteristics of the D2 protein and gene have been highly conserved during evolution. The rtD2 mRNA expression in the gonads suggests that rtD2 may be a key factor regulating local supply of active T(3) during rainbow trout gametogenesis.

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Section: Tissue Distribution Of Rtd2 Mrnamentioning

confidence: 95%

Type II iodothyronine deiodinase is preferentially expressed in rainbow trout (oncorhynchus mykiss) liver and gonads*

Sambroni

Gutieres

Cauty

et al. 2001

Molecular Reproduction Devel

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“…DIO proteins are important for the activation and deactivation of thyroid hormones (Orozco and Valverde-R, 2005). Members of the DIO family have been cloned from fish gills (Sanders et al, 1999), contain osmotic response elements in promoter regions in killifish (Lopez-Bojorquez et al, 2007), and deiodination activity is detectable in killifish gills (Orozco et al, 2000). Intriguingly, thyroid hormone signaling pathways have adaptively diverged between marine and freshwater populations of stickleback (Kitano et al, 2010).…”

Section: Transcription Regulationmentioning

confidence: 99%

Salinity- and population-dependent genome regulatory response during osmotic acclimation in the killifish (Fundulus heteroclitus) gill

Whitehead

Roach

Zhang

et al. 2012

Journal of Experimental Biology

128

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SUMMARYThe killifish Fundulus heteroclitus is abundant in osmotically dynamic estuaries and it can quickly adjust to extremes in environmental salinity. We performed a comparative osmotic challenge experiment to track the transcriptomic and physiological responses to two salinities throughout a time course of acclimation, and to explore the genome regulatory mechanisms that enable extreme osmotic acclimation. One southern and one northern coastal population, known to differ in their tolerance to hypo-osmotic exposure, were used as our comparative model. Both populations could maintain osmotic homeostasis when transferred from 32 to 0.4p.p.t., but diverged in their compensatory abilities when challenged down to 0.1p.p.t., in parallel with divergent transformation of gill morphology. Genes involved in cell volume regulation, nucleosome maintenance, ion transport, energetics, mitochondrion function, transcriptional regulation and apoptosis showed population-and salinity-dependent patterns of expression during acclimation. Network analysis confirmed the role of cytokine and kinase signaling pathways in coordinating the genome regulatory response to osmotic challenge, and also posited the importance of signaling coordinated through the transcription factor HNF-4. These genome responses support hypotheses of which regulatory mechanisms are particularly relevant for enabling extreme physiological flexibility. Supplementary material available online at

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“…However, the type II deiodinase (D2) is a low K m (nM range for T 4 ), low V max enzyme that only has ORD activity and is also not inhibited by PTU (Valverde-R et al 1997, Orozco et al 2002. The type III deiodinase (D3), like D2, is also a selective, low K m (nM range for T 3 ), low V max enzyme that is not inhibited by PTU, but, unlike D2, it is capable only of IRD (Sanders et al 1999).…”

Section: Introductionmentioning

confidence: 99%

Iodothyronine deiodinases and the control of plasma and tissue thyroid hormone levels in hyperthyroid tilapia (Oreochromis niloticus)

Geyten¹,

Byamungu²,

Reyns³

et al. 2005

Journal of Endocrinology

107

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Thyroid status is one of the most potent regulators of peripheral thyroid hormone metabolism in vertebrates. Despite this, the few papers that have been published concerning the role of thyroid hormones in the regulation of thyroid function in fish often offer conflicting data. We therefore set out to investigate the effects of tetraiodothyronine (thyroxine) (T 4 ) or tri-iodothyronine (T 3 ) supplementation (48 p.p.m.) via the food on plasma and tissue thyroid hormone levels as well as iodothyronine deiodinase (D) activities in the Nile tilapia (Oreochromis niloticus). T 4 supplementation did not induce a hyperthyroid state and subsequently had no effects on the thyroid hormone parameters measured, with the liver as the sole notable exception. In T 4 -fed tilapias, the hepatic T 4 levels increased substantially, and this was accompanied by an increase in in vitro type I deiodinase (D1) activity. Although the lack of effect of T 4 supplementation could be partially explained by an inefficient uptake of T 4 from the gut, our current data suggest that also the increased conversion of T 4 into reverse (r)T 3 by the D1 present in the liver plays an important role in this respect. In addition, T 3 supplementation increased plasma T 3 and decreased plasma T 4 concentrations. T 3 levels were also increased in the liver, brain, kidney, gill and white muscle, but without affecting local T 4 concentrations. However, this increase in T 3 availability remained without effect on D1 activity in liver and kidney. This observation, together with the 6-n-propylthiouracyl (PTU) insensitivity of the D1 enzyme in fish, sets the D1 in teleost fish clearly apart from its mammalian and avian counterparts. The changes in hepatic deiodinases confirm the role of the liver as an important T 3 -regulating tissue. However, the very short plasma half-life of exogenously administered T 3 implies the existence of an efficient T 3 clearing/degradation mechanism other than deiodination.

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Cloning and Characterization of Type III Iodothyronine Deiodinase from the Fish Oreochromis niloticus

Cited by 34 publications

References 30 publications

Type II iodothyronine deiodinase is preferentially expressed in rainbow trout (oncorhynchus mykiss) liver and gonads*

Type II iodothyronine deiodinase is preferentially expressed in rainbow trout (oncorhynchus mykiss) liver and gonads*

Salinity- and population-dependent genome regulatory response during osmotic acclimation in the killifish (Fundulus heteroclitus) gill

Iodothyronine deiodinases and the control of plasma and tissue thyroid hormone levels in hyperthyroid tilapia (Oreochromis niloticus)

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