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A New Mode of Action for This Drug

Karin U. Schallreuter, MD; Mark R. Pittelkow, MD

Arch Dermatol. 1987;123(11):1494-1498.

Abstract
• Membrane-associated thioredoxin reductase (TR) activity has been measured in 3-mm punch biopsy specimens from psoriatic and uninvolved skin in eight patients with chronic plaque-type psoriasis vulgaris. The mean specific activity for this free radical reducing enzyme in psoriatic vs uninvolved skin was 28.5 ± 8.0 U vs 16.8 ± 4.25 U. Because TR contains two reactive thiolate groups at its active site, this enzyme reacts with anthralin to form a covalent anthralin-TR complex causing irreversible enzyme deactivation. This mode of action for anthralin was confirmed by using pure TR from Escherichia coli. Keratinocyte cell cultures, grown from normal and psoriatic skin of one donor, revealed 24% and 42% inhibition of cell surface TR activity, respectively, in the presence of 2x10^-5M anthralin. Time-dependent topical application of anthralin on guinea pig skin gave 70% inhibition of TR with concentrations of 0.25% to 1.0% after 24 hours in open and occlusive applications of the drug. Short contact with 1% anthralin showed 70% inhibition after 120 minutes.

(Arch Dermatol 1987;123:1494-1498)

Author Affiliations
From the Departments of Dermatology and Biochemistry, University of Minnesota, Minneapolis (Dr Schallreuter); and the Department of Dermatology, Mayo Clinic, Rochester, Minn (Dr Pittelkow).

Footnotes
Accepted for publication May 12, 1987.

Reprint requests to the Department of Dermatology, University of Hamburg, Martinstraße 52, 2000 Hamburg 20, West Germany (Dr Schallreuter).

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