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Iodothyronamines are Oxidatively Deaminated to Iodothyroacetic Acids in vivo
Author(s) -
Wood Warren J. L.,
Geraci Travis,
Nilsen Aaron,
DeBarber Andrea E.,
Scanlan Thomas S.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800607
Subject(s) - triac , amine oxidase , chemistry , semicarbazide , iproniazid , monoamine oxidase , endogeny , metabolism , in vivo , biochemistry , oxidase test , amine gas treating , nordihydroguaiaretic acid , enzyme , lipoxygenase , organic chemistry , biology , physics , microbiology and biotechnology , quantum mechanics , voltage
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 .