The purpose of this study was to investigate variations in the enzyme activities of the kynurenine pathway in various mammals (rabbit, mouse, rat, guinea-pig). Liver tryptophan 2,3-dioxygenase, small intestine indole 2,3-dioxygenase, liver and kidney kynurenine 3-monooxygenase, kynureninase, kynurenine-oxoglutarate transaminase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase were analysed. Small intestine superoxide dismutase activity and free and total serum tryptophan were also measured. Liver tryptophan 2,3-dioxygenase was present as both holoenzyme and apoenzyme only in rat, while in the other species only holoenzyme activity was observed. Also, small intestine indole 2,3-dioxygenase activity was more abundant in rat than in the other animals studied. The highest activity of small intestine superoxide dismutase was found in rat, and the lowest in rabbit. Liver and kidney kynurenine 3-monooxygenase activity was very elevated and higher in mouse, followed by rat; rabbit showed the lowest activity. Kynureninase activity appeared to be much lower among the enzymes of the kynurenine pathway. However, guinea-pig showed higher activity in both liver and kidney in comparison with other species. With regard to kynurenine-oxoglutarate transaminase, all species examined here presented more abundant enzyme activity in kidney, the value being similar between rat and mouse. Guinea-pig was the animal with the lowest activity. 3-Hydroxyanthranilate 3,4-dioxygenase showed the highest activity of all the enzymes evaluated in the study, but with different levels in liver and kidney, varying among species. The most elevated activity of aminocarboxymuconate-semialdehyde decarboxylase was present in kidney of guinea-pig, and the lowest in rabbit. Serum concentrations of tryptophan were higher in rat, followed by mouse, rabbit and guinea-pig. In conclusion, the present study demonstrates that the enzyme activities of the kynurenine pathway are very active in tissues of the four species of mammals investigated. The proposed method of in vitro enzyme determination represents a valid alternative to study of the tryptophan metabolic route.
Enzyme activities of tryptophan metabolism along the kynurenine pathway in various species of animals
ALLEGRI, GRAZIELLA;COSTA, CARLO VIRGILIO LUIGI;BERTAZZO, ANTONELLA;RAGAZZI, EUGENIO
2003
Abstract
The purpose of this study was to investigate variations in the enzyme activities of the kynurenine pathway in various mammals (rabbit, mouse, rat, guinea-pig). Liver tryptophan 2,3-dioxygenase, small intestine indole 2,3-dioxygenase, liver and kidney kynurenine 3-monooxygenase, kynureninase, kynurenine-oxoglutarate transaminase, 3-hydroxyanthranilate 3,4-dioxygenase and aminocarboxymuconate-semialdehyde decarboxylase were analysed. Small intestine superoxide dismutase activity and free and total serum tryptophan were also measured. Liver tryptophan 2,3-dioxygenase was present as both holoenzyme and apoenzyme only in rat, while in the other species only holoenzyme activity was observed. Also, small intestine indole 2,3-dioxygenase activity was more abundant in rat than in the other animals studied. The highest activity of small intestine superoxide dismutase was found in rat, and the lowest in rabbit. Liver and kidney kynurenine 3-monooxygenase activity was very elevated and higher in mouse, followed by rat; rabbit showed the lowest activity. Kynureninase activity appeared to be much lower among the enzymes of the kynurenine pathway. However, guinea-pig showed higher activity in both liver and kidney in comparison with other species. With regard to kynurenine-oxoglutarate transaminase, all species examined here presented more abundant enzyme activity in kidney, the value being similar between rat and mouse. Guinea-pig was the animal with the lowest activity. 3-Hydroxyanthranilate 3,4-dioxygenase showed the highest activity of all the enzymes evaluated in the study, but with different levels in liver and kidney, varying among species. The most elevated activity of aminocarboxymuconate-semialdehyde decarboxylase was present in kidney of guinea-pig, and the lowest in rabbit. Serum concentrations of tryptophan were higher in rat, followed by mouse, rabbit and guinea-pig. In conclusion, the present study demonstrates that the enzyme activities of the kynurenine pathway are very active in tissues of the four species of mammals investigated. The proposed method of in vitro enzyme determination represents a valid alternative to study of the tryptophan metabolic route.
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