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Originally published In Press as doi:10.1074/jbc.M200916200 on February 20, 2002

J. Biol. Chem., Vol. 277, Issue 18, 16002-16010, May 3, 2002
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Disulfide Bond Formation Promotes the cis- and trans-Dimerization of the E-cadherin-derived First Repeat*

Irwan T. MakagiansarDagger , Phuong D. NguyenDagger , Atsutoshi IkesueDagger §, Krzysztof Kuczera, William Dentler, Jeffrey L. Urbauer, Nadezhda Galeva||, Michail Alterman||, and Teruna J. SiahaanDagger **

From the Departments of Dagger  Pharmaceutical Chemistry and  Molecular Biosciences and the || Biochemical Research Laboratory, University of Kansas, Lawrence, Kansas 66047

Cadherin is a cell adhesion molecule crucial for epithelial and endothelial cell monolayer integrity. The previously solved x-ray crystallographic structure of the E-CAD12 cis-dimer displayed an unpaired Cys9, which protruded away from the Cys9 on the other protomer. To investigate the possible biological function of Cys9 within the first repeat (the E-cadherin-derived N-terminal repeat), E-CAD1 was overexpressed and secreted into the periplasmic space of Escherichia coli cells. Recombinant E-CAD1 produced a mixed monomer and dimer in an equilibrium fashion. The dimer was linked by a disulfide through Cys9 pairing. Analysis by high pressure liquid chromatography and electron microscopy suggested the existence of oligomeric complexes. Mutation at Trp2 appears to indicate that these oligomeric complexes trans-dimerize. Interestingly, mutation of Cys9 affected not only the cis-dimerization, but also the trans-oligomerization of E-CAD1. Accordingly, it is plausible that, under oxidative stress, the homophilic interactions of E-cadherin through E-CAD1 may be promoted and stabilized by this disulfide bond.

* This work was supported in part by National Institutes of Health Grant EB-00226 and the Pharmaceutical Research and Manufacturers of America Foundation (to P. D. N.). This work was presented in part in abstract form at the Experimental Biology Annual Meeting, March 31 to April 4, 2001, Orlando, FL.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.

§ Present address: Hisamitsu Pharmaceuticals, Inc., Tsukuba Laboratories, Kannondai 1-25-11, Tsukuba 305, Japan.

** To whom correspondence should be addressed: Dept. of Pharmaceutical Chemistry, University of Kansas, Simons Bldg., 2095 Constant Ave., Lawrence, KS 66047. Tel.: 785-864-7327; Fax: 785-864-5736; E-mail: Siahaan@ku.edu.

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