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Originally published In Press as doi:10.1074/jbc.M106996200 on October 31, 2001

J. Biol. Chem., Vol. 277, Issue 1, 303-309, January 4, 2002
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Reelin Is a Serine Protease of the Extracellular Matrix*

Carlo C. Quattrocchiabc, Francesca Wannenesde, Antonio M. Persicoa, Silvia Anna Ciafréd, Gabriella D'Arcangelofghi, Maria G. Faracef, and Flavio Kelleraj

From the a Laboratory of Neuroscience, Department of Physiology and Neuroscience, Università "Campus Bio-Medico," Via Longoni 83, 00155 Roma, Italy, the b Program in Neuroscience, Faculty of Medicine, University of Brescia, Via Valsabbina 19, 25123 Brescia, Italy, the d Department of Experimental Medicine and Biochemical Sciences, Università di Tor Vergata, Via di Tor Vergata 135, 00133 Roma, Italy, the e Department of Internal Medicine, Università di Tor Vergata, Via di Tor Vergata 135, 00133 Roma, Italy, and f The Cain Foundation Laboratories, g Department of Pediatrics, h Program in Developmental Biology and i Division of Neuroscience, Baylor College of Medicine, Houston, Texas 77030

Reelin is an extracellular matrix protein that plays a pivotal role in development of the central nervous system. Reelin is also expressed in the adult brain, notably in the cerebral cortex, where it might play a role in synaptic plasticity. The mechanism of action of reelin at the molecular level has been the subject of several hypotheses. Here we show that reelin is a serine protease and that proteolytic activity is relevant to its function, since (i) Reelin expression in HEK 293T cells impairs their ability to adhere to fibronectin-coated surfaces, and adhesion to fibronectin is restored by micromolar concentrations of diisopropyl phosphorofluoridate, a serine hydrolase inhibitor; (ii) purified Reelin binds FP-Peg-biotin, a trap probe which irreversibly binds to serine residues located in active catalytic sites of serine hydrolases; (iii) purified Reelin rapidly degrades fibronectin and laminin, while collagen IV is degraded at a much slower rate; fibronectin degradation is inhibited by inhibitors of serine proteases, and by monoclonal antibody CR-50, an antibody known to block the function of Reelin both in vitro and in vivo. The proteolytic activity of Reelin on adhesion molecules of the extracellular matrix and/or receptors on neurons may explain how Reelin regulates neuronal migration and synaptic plasticity.

* This work was supported by Consiglio Nazionale delle Ricerche Programma "Biomolecole per la salute umana" Grant 99.00555.PF33.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.

c Present address: Dept. of Pediatrics-Neurology, Baylor College of Medicine, 1102 Bates St., MC 3-6365, Houston, TX 77030.

j To whom correspondence should be addressed: Laboratory of Neuroscience, Università "Campus Bio-Medico," Via Longoni 83, 00155 Roma, Italy. Tel.: 39-06-2254-1335; Fax: 39-06-22-54-14-56; E-mail: f.keller@unicampus.it.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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