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Iodothyronamines are oxidatively deaminated to iodothyroacetic acids in vivo

Warren J L Wood1, Travis Geraci, Aaron Nilsen

  • 1Department of Physiology and Pharmacology, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Mail Code L334, Portland, OR 97239, USA.

Chembiochem : a European Journal of Chemical Biology
|December 24, 2008
PubMed

3-Iodothyronamine (T(1)AM) and 3,3',5-triiodothyroacetic acid (Triac) are bioactive metabolites of the hormone thyroxine (T(4)). In the present study, the ability of T(1)AM and 3,3',5-triiodothyronamine (T(3)AM) to be metabolized to 3-iodothyroacetic acid (TA(1)) and Triac, respectively, was investigated. Both T(1)AM and T(3)AM 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. TA(1) was found to be present in trace quantities in human serum and in substantial levels in serum from T(1)AM-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 TA(1).

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