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Increase in Tryptophan Oxygenase Activity in Alcoholic Patients
Author(s) -
BuydensBranchey L.,
Branchey M.,
Worner T. M.,
Zucker D.,
Aramsombatdee E.,
Lieber C. S.
Publication year - 1988
Publication title -
alcoholism: clinical and experimental research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.267
H-Index - 153
eISSN - 1530-0277
pISSN - 0145-6008
DOI - 10.1111/j.1530-0277.1988.tb00153.x
Subject(s) - tryptophan , kynurenine , glucocorticoid , catabolism , medicine , kynurenine pathway , enzyme assay , anabolism , endocrinology , hormone , limiting , enzyme , chemistry , physiology , biochemistry , metabolism , amino acid , mechanical engineering , engineering
This study was conducted in order to assess whether chronic excessive alcohol consumption affects the activity of the liver enzyme tryptophan oxygenase which is rate limiting along the most important pathway of catabolism. Five alcoholics were studied twice, once shortly after admission to an Inpatient unit and the second time 1 month later. On each study day patients were given a trptophan load of 50 mg/kg. Kynurenine in the urines (which reflects tryptophan oxygenase activity) was measured for a period of 8 hr following the load and showed a significantly enhanced activity of the enzyme shortly after cessation of drinking. This increased activity enzyme could explain the lowered tryptophan levels we have previously reported in alcoholics. The increase in enzyme activity may have been mediated by a rise in glucocorticoid hormones. In all instances, plasma cortisol measured hourly for 6 hr after the start of the experiment, was higher shortly after cessation of drinking than 1 month later.