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Papers In Press, published online ahead of print May 14, 2003
J. Biol. Chem, 10.1074/jbc.M300456200
Submitted on January 15, 2003
Revised on May 14, 2003
Accepted on May 14, 2003

An aminopeptidase, ARTS-1, is required for interleukin-6 receptor shedding

Xinle Cui, Farshid N. Rouhani, Feras Hawari, and Stewart J. Levine

Pulmonary-Critical Care Medicine Branch,, National Heart, Lung, and Blood Institute, NIH, Bethesda, Maryland 20892-1590

Corresponding Author: levines{at}nih.gov

ARTS-1 (aminopeptidase regulator of TNFR1 shedding) binds to the type I tumor necrosis factor receptor (TNFR1) and promotes receptor shedding. Since hydroxamic acid-based metalloprotease inhibitors prevent shedding of both TNFR1 and the interleukin-6 receptor (IL-6Ra), we hypothesized that ARTS-1 might also regulate shedding of IL-6Ra, a member of the type I cytokine receptor superfamily that is structurally different from TNFR1. Reciprocal co-immunoprecipitation experiments identified that membrane-associated ARTS-1 directly binds to a 55-kDa IL-6Ra, a size consistent with soluble IL-6Ra generated by ectodomain cleavage of the membrane-bound receptor. Further, ARTS-1 promoted IL-6Ra shedding, as demonstrated by a direct correlation between increased membrane-associated ARTS-1 protein, increased IL-6Ra shedding, and decreased membrane-associated IL-6Ra in cell lines over-expressing ARTS-1. The absence of basal IL-6Ra shedding from arts-1 knock-out cells identified that ARTS-1 was required for constitutive IL-6Ra shedding. Further, the mechanism of constitutive IL-6Ra shedding requires ARTS-1 catalytic activity. Thus, ARTS-1 promotes the shedding of two cytokine receptor superfamilies, the type I cytokine receptor superfamily (IL-6R) and the TNF receptor superfamily (TNFR1). We propose that ARTS-1 is a multi-functional aminopeptidase that may modulate inflammatory events by promoting IL-6Ra and TNFR1 shedding.


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