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J Biol Chem, Vol. 275, Issue 16, 11765-11770, April 21, 2000

Disulfide Bond Formation Is Not Required for Human Chorionic Gonadotropin Subunit Association
STUDIES WITH DITHIOTHREITOL IN JEG-3 CELLS*

Vinod SinghDagger and Wolfgang E. Merz§

From the Biochemie-Zentrum Heidelberg, University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany

To study the influence of disulfide bridge formation on the assembly of the subunits of human chorionic gonadotropin in JEG-3 choriocarcinoma cells, dithiothreitol (DTT) was used to create a reducing milieu in the endoplasmic reticulum (ER) in vivo. In the presence of 5 mM DTT during pulse-chase experiments all of the beta -subunit precursors observed in unperturbed cells (pbeta 0, pbeta 1, pbeta 2, and beta *) collapsed into the pbeta 0 form. The reducing milieu of the ER was reoxidized in less than 5 min after removal of DTT from the medium. DTT markedly increased the half-life of the pbeta 0 precursor from 8.8 to 65.2 min. Under reoxidation conditions, the beta -subunit precursors folded back from pbeta 0 in less than 5 min. In unperturbed JEG-3 cells, the alpha -subunit was present in both fully glycosylated and monoglycosylated precursor (pre-alpha ) forms. The attachment of the second N-linked glycan residue of the alpha -subunit was accelerated in the presence of DTT, and consequently pre-alpha -subunit was missing from the DTT-treated cultures. The formation of alpha beta -dimers appeared to be at least partially independent of the oxidation state in the ER. The alpha beta -dimer was present under conditions in which disulfide bridge formation was prevented by exposure to 5 mM DTT before and during the pulse period. This clearly suggests that the human chorionic gonadotropin subunits may acquire association-competent conformations even when no disulfide bridge formation has taken place.

* This work was supported by Grant Me 545/10-1 from the Deutsche Forschungsgemeinschaft, Bonn-Bad Godesberg (to W. E. M.) and a fellowship of the Alexander von Humboldt Foundation, Bonn-Bad Godesberg (to V. S.).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.

Dagger Present address: Hormone Biochemistry Laboratory, Inst. of Self Organizing Systems and Biophysics, North-Eastern Hill University, Permanent Campus, Shillong-793022, Meghalaya, India.

§ To whom correspondence should be addressed: Biochemie-Zentrum Heidelberg, University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. Tel.: 49-6221-544181; Fax: 49-6221-545586; E-mail: wolfgang.merz@urz.uni-heidelberg.de.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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