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Graefes Arch Clin Exp Ophthalmol. 1996 Jul;234(7):457-62.

Indoleamine 2,3-dioxygenase: antioxidant enzyme in the human eye.

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1
Laboratoire d'Ophthalmologie Expérimentale, Institut Suisse de Recherche Expérimentale sur le Cancer, Epalinges s/Lausanne, Switzerland.

Abstract

BACKGROUND:

Indoleamine 2,3-dioxygenase (IDO) is the first enzyme of the tryptophan degradation pathway. IDO is an antioxidant enzyme because it is a direct scavenger of superoxide radicals. In this study, we measured the activity of IDO in the human eye.

METHODS:

IDO was detected in the protein extract of human retina, iris/ciliary body, and lens. The products formed were measured using HPLC with electrochemical detection. Enzyme activity was expressed as the quantity of kynurenine and 3-hydroxykynurenine formed.

RESULTS:

IDO activity in the retina extract was 51.5 (+/-10) nmol/g tissue/h, and kynurenine formation was detected. In the iris/ ciliary body, IDO activity was 191.8 (+/49) nmol/g tissue/h, and both kynurenine and 3-hydroxy-kynurenine were formed from tryptophan. In the extract of lens cortex only 3-hydroxykynurenine was formed from tryptophan. IDO activity was 351 (+/-67.3) nmol/g tissue/h.

CONCLUSION:

Free tryptophan is degradated in the human eye by IDO, an antioxidative enzyme. IDO may be an antioxidant mechanism in the eye.

PMID:
8817290
[Indexed for MEDLINE]
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