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Originally published In Press as doi:10.1074/jbc.M010741200 on January 30, 2001

J. Biol. Chem., Vol. 276, Issue 18, 14665-14674, May 4, 2001
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Biochemical and Pharmacological Criteria Define Two Shedding Activities for TRANCE/OPGL That Are Distinct from the Tumor Necrosis Factor alpha  Convertase*

Johannes SchlöndorffDagger §, Lawrence LumDagger ||, and Carl P. BlobelDagger **

From the Dagger  Cellular Biochemistry and Biophysics Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 and § Tri-Institutional (Cornell University/Rockefeller University/Sloan-Kettering Cancer Center) MD-PhD Training Program, New York, New York 10021

A number of structurally and functionally diverse membrane proteins are released from the plasma membrane in a process termed protein ectodomain shedding. Ectodomain shedding may activate or inactivate a substrate or change its properties, such as converting a juxtacrine into a paracrine signaling molecule. Here we have characterized the activities involved in protein ectodomain shedding of the tumor necrosis factor family member TRANCE/OPGL in different cell types. The criteria used to evaluate these activities include (a) cleavage site usage, (b) response to activators and inhibitors of intracellular signaling pathways, and (c) sensitivity to tissue inhibitors of metalloproteases (TIMPs). At least two TRANCE shedding activities emerged, both of which are distinct from the tumor necrosis factor alpha  convertase. One of the TRANCE sheddases is induced by the tyrosine phosphatase inhibitor pervanadate but not by phorbol esters, whereas the other is refractory to both of these stimuli. Furthermore, the pervanadate-regulated sheddase activity is sensitive to TIMP-2 but not TIMP-1, which is consistent with the properties of a membrane type matrix metalloprotease. This study provides insights into the properties of different activities involved in protein ectodomain shedding and has implications for the functional regulation of TRANCE by potentially more than one protease.

* This work was supported in part by a grant from Glaxo Wellcome (to C. P. B.), by National Institutes of Health Grant RO1 GM58668 (to C. P. B.), by Memorial Sloan-Kettering Cancer Center Support Grant NCI-P30-CA-08748, by the Samuel and May Rudin Foundation, and by the DeWitt Wallace Fund.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported in part by a National Institutes of Health Medical Scientist Training Program Training Grant 5T32GM07739-17 and the Louis and Rachel Rudin Family Foundation.

|| Present address: Johns Hopkins University School of Medicine, 725 North Wolfe St., PCTB Rm. 714, Baltimore, MD 21205.

** To whom correspondence should be addressed: Cellular Biochemistry and Biophysics Program, Sloan-Kettering Inst., Memorial Sloan-Kettering Cancer Center, Box 368, 1275 York Ave., New York, NY 10021. Tel.: 212-639-2915; Fax: 212-717-3047; E-mail: c-blobel@ski.mskcc.org.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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