Species differences in liver type I iodothyronine deiodinase

Schoenmakers, Christian H.H.; Pigmans, Ingrid G.A.J.; Visser, Theo J.

doi:10.1016/0167-4838(92)90349-i

Cited by 42 publications

(35 citation statements)

References 23 publications

(24 reference statements)

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“…4B). In adult chicken liver microsomes ID-I has been identified as a 26 kDa band [16]. Figure 4 shows the strong correlation between affinity labeling of this 26 kDa band and the varying ID-I activity in chicken liver during embryonic development.…”

Section: Resultsmentioning

confidence: 99%

“…The activity of ID-I was measured by incubation of lOL,rglmI microsorna1 protein for 20 min at 37°C with 1 PM rT, and 75 nCi f3',S-"51]rT3 in 200 ~10.2 M phosphate @H 7.2),4 mM EDTA and 5 mM DTT, followed by isolation of the inI-released on Sephadex IX-Z@ as previously described [16].…”

Section: Deiodinase Mapmentioning

confidence: 99%

“…In chicken liver, the enzyme is mainly present during embryonic development, with the highest activity on day 16 and decreasing rapidly thereafter until very low levels are reached at hatching on day 21 [ 131. In this study we tested if BrAcT, is a useful affinity-label for ID-III in rats and chickens.…”

Section: Introductionmentioning

confidence: 99%

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Reaction of the type III iodothyronine deiodinase with the affinity label N‐bromoacetyl‐triiodothyronine

Schoenmakers¹,

Pigmans²,

Kaptein³

et al. 1993

FEBS Letters

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The type III iodothyronine deiodinase (ID-III) catalyzes the inner ring deiodination and, thus, the inactivation of the thyroid hormones T4 and Tj. ID-III activity in rat brain, rat placenta and embryonic chicken liver is inhibited by the affinity label N-bromoacetyl-T, (BrAcT,) with an affinity similar to that of T,. Reaction of rat brain and placenta microsomes with BrAc['*'I]T, resulted in the extensive labeling of a 32 kDa protein (~32). However, p32 was also prominently labeled in fetal rat liver microsomes which have no ID-III activity. Labeling of p32 was not influenced by 100 PM substrate analogs or inhibitors of ID-III, some of which completely inhibit ID-III activity at 1 PM. BrAc['*'I]T~ labeling of embryonic chicken liver microsomes did not reveal p32 or another protein possibly related to ID-III. In contrast to previous suggestions, it is unlikely that p32 represents ID-III or a subunit thereof.

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Section: Resultsmentioning

confidence: 99%

Section: Deiodinase Mapmentioning

confidence: 99%

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Reaction of the type III iodothyronine deiodinase with the affinity label N‐bromoacetyl‐triiodothyronine

Schoenmakers¹,

Pigmans²,

Kaptein³

et al. 1993

FEBS Letters

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“…The presence of 5'-MD in the mammary gland secures adequate supply of T 3 sup-porting lactogenesis, and makes T 3 available for mammary gland cells independently of temporal variations in TH in the systemic circulation (Ślebodziński et al, 1999). High serum T 3 during the early-lactation phase observed in milking goats may indicate a concomitant rise in type I 5'-MD activity in the liver and the kidneys, the isoenzyme which is responsible for the blood level of T 3 and which among farm animals shows the highest activity in the goat (Schoenmakers et al, 1992). The involvement of blood T 3 , insulin and glucagon in the homeorhetic adaptation to lactation in goats has been suggested in a recent work (Pereka and Riis, 1993).…”

Section: Discussionmentioning

confidence: 99%

“…In spite of the recognised importance of thyroid hormones for mammary gland function in various species, and their benefit to the offspring, such studies in goats are lacking. Amongst farm animals (cows, horses, pigs and sheep) goats have higher TH blood concentration, and the highest activity of liver 5'-MD (type I), the enzyme which is responsible for the main part of peripheral T 3 production and T 3 blood concentrations (Anderson et al, 1988;Schoenmakers et al, 1992).…”

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confidence: 99%

Thyroid hormones (th) and 5'-monodeiodinase (5'-md) activity in goat's milk from the early, mid- and late lactation period

Slebodzinski¹,

Twardoń²

2004

Acta Veterinaria Hungarica

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The physiological significance of thyroid hormones (TH) present in colostrum and milk is still under consideration. The present study was aimed at determining milk thyroxine (T 4 ) and triiodothyronine (T 3 ) levels in three lactation phases (early, mid-and late) of the goat, and to measure activity of the milk 5'-deiodinase (5'-MD) enzyme responsible for the intramammary conversion of prohormone T 4 to its metabolically highly active form T 3 . Thirty-two milk goats (Polish White breed) fed a standard diet were used for milk sampling. The highest TH levels in mammary secretion were recorded during the first 2-3 days post partum. Then the hormone levels decreased, and by about Day 7 fluctuated around the overall mean for the early-lactation phase (Days 1 to 24 of lactation), recording 0.134 ± 0.059 µg T 4 and 150.8 ± 2.80 ng T 3 in 100 ml of the milk. Such T 4 concentrations appeared to be comparable to those in the rabbit and human, whereas the concentration of T 3 was higher than in the cow, pig and mare's milk. Milk 5'-MD activity was higher (P < 0.01) during early and late lactation, compared to the mid-lactation phase. It coincided with low T 4 and high T 3 milk levels during early lactation, and with high milk T 4 and low T 3 concentrations during late lactation. The quantity of T 4 and T 3 available to newborn kids in milk suggests that TH ingested with the colostrum may have a physiological role during the early postnatal life of suckling goats.

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Development of a validated liquid chromatography/tandem mass spectrometry method for the distinction of thyronine and thyronamine constitutional isomers and for the identification of new deiodinase substrates

Piehl

Heberer

Balizs

et al. 2008

Rapid Comm Mass Spectrometry

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Thyronines (THs) and thyronamines (TAMs) are two groups of endogenous iodine-containing signaling molecules whose representatives differ from each other only regarding the number and/or the position of the iodine atoms. Both groups of compounds are substrates of three deiodinase isozymes, which catalyze the sequential reductive removal of iodine from the respective precursor molecule. In this study, a novel analytical method applying liquid chromatography/tandem mass spectrometry (LC-MS/MS) was developed. This method permitted the unequivocal, simultaneous identification and quantification of all THs and TAMs in the same biological sample. Furthermore, a liquid-liquid extraction procedure permitting the concurrent isolation of all THs and TAMs from biological matrices, namely deiodinase (Dio) reaction mixtures, was established. Method validation experiments with extracted TH and TAM analytes demonstrated that the method was selective, devoid of matrix effects, sensitive, linear over a wide range of analyte concentrations and robust in terms of reproducible recoveries, process efficiencies as well as intra-assay and inter-assay stability parameters. The method was applied to study the deiodination reactions of iodinated THs catalyzed by the three deiodinase isozymes. With the HPLC protocol developed herein, sufficient chromatographic separation of all constitutional TH and TAM isomers was achieved. Accordingly, the position of each iodine atom removed from a TH substrate in a Dio-catalyzed reaction was backtracked unequivocally. While several established deiodination reactions were verified, two as yet unknown reactions, namely the phenolic ring deiodination of 3',5'-diiodothyronine (3',5'-T2) by Dio2 and the tyrosyl ring deiodination of 3-monoiodothyronine (3-T1) by Dio3, were newly identified.

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Species differences in liver type I iodothyronine deiodinase

Cited by 42 publications

References 23 publications

Reaction of the type III iodothyronine deiodinase with the affinity label N‐bromoacetyl‐triiodothyronine

Reaction of the type III iodothyronine deiodinase with the affinity label N‐bromoacetyl‐triiodothyronine

Thyroid hormones (th) and 5'-monodeiodinase (5'-md) activity in goat's milk from the early, mid- and late lactation period

Development of a validated liquid chromatography/tandem mass spectrometry method for the distinction of thyronine and thyronamine constitutional isomers and for the identification of new deiodinase substrates

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