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J Biol Chem, Vol. 274, Issue 6, 3268-3271, February 5, 1999

COMMUNICATION
Enzyme Activity of Macrophage Migration Inhibitory Factor toward Oxidized Catecholamines

Jun MatsunagaDagger , Debasish Sinha, Lew Pannell**, Chie SantisDagger , Francisco SolanoDagger Dagger , Graeme J. Wistow, and Vincent J. HearingDagger

From the Dagger  Pigment Cell Biology Section, Laboratory of Cell Biology, NCI, the  Section on Molecular Structure and Function, National Eye Institute, the ** Laboratory of Bioorganic Chemistry, NIDDK, National Institutes of Health, Bethesda, Maryland 20892 and the Dagger Dagger  Department of Biochemistry, University of Murcia, E-30100 Murcia, Spain

Macrophage migration inhibitory factor (MIF) is a relatively small, 12.5-kDa protein that is structurally related to some isomerases and for which multiple immune and catalytic roles have been proposed. MIF is widely expressed in tissues with particularly high levels in neural tissues. Here we show that MIF is able to catalyze the conversion of 3,4-dihydroxyphenylaminechrome and norepinephrinechrome, toxic quinone products of the neurotransmitter catecholamines 3,4-dihydroxyphenylamine and norepinephrine, to indoledihydroxy derivatives that may serve as precursors to neuromelanin. This raises the possibility that MIF participates in a detoxification pathway for catecholamine products and could therefore have a protective role in neural tissues, which as in Parkinson's disease, may be subject to catecholamine-related cell death.


Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.



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