Iodothyronamines are oxidatively deaminated to iodothyroacetic acids in vivo

Warren J.L. Wood; Travis Geraci; Aaron Nilsen; Andrea E. DeBarber; Thomas S. Scanlan

doi:10.1002/cbic.200800607

Iodothyronamines are oxidatively deaminated to iodothyroacetic acids in vivo

Warren J.L. Wood, Travis Geraci, Aaron Nilsen, Andrea E. DeBarber, Thomas S. Scanlan

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

3-Iodothyronamine (T₁AM) and 3,3′,5-triiodothyroacetic acid (Triac) are bioactive metabolites of the hormone thyroxine (T₄). In the present study, the ability of T₁AM and 3,3′,5-triiodothyronamine (T₃AM) to be metabolized to 3-iodothyroacetic acid (TA₁) and Triac, respectively, was investigated. Both T₁AM and T₃AM were converted to their respective iodinated thyroacetic acid analogues in both cell and tissue extracts. This conversion could be significantly inhibited with the monamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) inhibitor iproniazid. TA₁ was found to be present in trace quantities in human serum and in substantial levels in serum from T₁AM-treated rats. These results demonstrate that iodothyronamines are substrates for amine oxidases and that this metabolism may be the source of the corresponding endogenous arylacetic acid products Triac and TA₁.

Original language	English (US)
Pages (from-to)	361-365
Number of pages	5
Journal	ChemBioChem
Volume	10
Issue number	2
DOIs	https://doi.org/10.1002/cbic.200800607
State	Published - Jan 26 2009
Externally published	Yes

Keywords

Biosynthesis
Biotransformations
Iodothyroacetic acids
Iodothyronamines
Metabolism

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

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title = "Iodothyronamines are oxidatively deaminated to iodothyroacetic acids in vivo",

abstract = "3-Iodothyronamine (T1AM) and 3,3′,5-triiodothyroacetic acid (Triac) are bioactive metabolites of the hormone thyroxine (T4). In the present study, the ability of T1AM and 3,3′,5-triiodothyronamine (T3AM) to be metabolized to 3-iodothyroacetic acid (TA1) and Triac, respectively, was investigated. Both T1AM and T3AM were converted to their respective iodinated thyroacetic acid analogues in both cell and tissue extracts. This conversion could be significantly inhibited with the monamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) inhibitor iproniazid. TA1 was found to be present in trace quantities in human serum and in substantial levels in serum from T1AM-treated rats. These results demonstrate that iodothyronamines are substrates for amine oxidases and that this metabolism may be the source of the corresponding endogenous arylacetic acid products Triac and TA1.",

keywords = "Biosynthesis, Biotransformations, Iodothyroacetic acids, Iodothyronamines, Metabolism",

author = "Wood, {Warren J.L.} and Travis Geraci and Aaron Nilsen and DeBarber, {Andrea E.} and Scanlan, {Thomas S.}",

year = "2009",

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doi = "10.1002/cbic.200800607",

language = "English (US)",

volume = "10",

pages = "361--365",

journal = "ChemBioChem",

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T1 - Iodothyronamines are oxidatively deaminated to iodothyroacetic acids in vivo

AU - Wood, Warren J.L.

AU - Geraci, Travis

AU - Nilsen, Aaron

AU - DeBarber, Andrea E.

AU - Scanlan, Thomas S.

PY - 2009/1/26

Y1 - 2009/1/26

N2 - 3-Iodothyronamine (T1AM) and 3,3′,5-triiodothyroacetic acid (Triac) are bioactive metabolites of the hormone thyroxine (T4). In the present study, the ability of T1AM and 3,3′,5-triiodothyronamine (T3AM) to be metabolized to 3-iodothyroacetic acid (TA1) and Triac, respectively, was investigated. Both T1AM and T3AM were converted to their respective iodinated thyroacetic acid analogues in both cell and tissue extracts. This conversion could be significantly inhibited with the monamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) inhibitor iproniazid. TA1 was found to be present in trace quantities in human serum and in substantial levels in serum from T1AM-treated rats. These results demonstrate that iodothyronamines are substrates for amine oxidases and that this metabolism may be the source of the corresponding endogenous arylacetic acid products Triac and TA1.

AB - 3-Iodothyronamine (T1AM) and 3,3′,5-triiodothyroacetic acid (Triac) are bioactive metabolites of the hormone thyroxine (T4). In the present study, the ability of T1AM and 3,3′,5-triiodothyronamine (T3AM) to be metabolized to 3-iodothyroacetic acid (TA1) and Triac, respectively, was investigated. Both T1AM and T3AM were converted to their respective iodinated thyroacetic acid analogues in both cell and tissue extracts. This conversion could be significantly inhibited with the monamine oxidase (MAO) and semicarbazide-sensitive amine oxidase (SSAO) inhibitor iproniazid. TA1 was found to be present in trace quantities in human serum and in substantial levels in serum from T1AM-treated rats. These results demonstrate that iodothyronamines are substrates for amine oxidases and that this metabolism may be the source of the corresponding endogenous arylacetic acid products Triac and TA1.

KW - Biosynthesis

KW - Biotransformations

KW - Iodothyroacetic acids

KW - Iodothyronamines

KW - Metabolism

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JO - ChemBioChem

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IS - 2

ER -

Iodothyronamines are oxidatively deaminated to iodothyroacetic acids in vivo

Abstract

Keywords

ASJC Scopus subject areas

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