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Originally published In Press as doi:10.1074/jbc.M203832200 on May 22, 2002

J. Biol. Chem., Vol. 277, Issue 29, 26540-26546, July 19, 2002
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Detection of Circulating and Endothelial Cell Polymers of Z and Wild Type alpha 1-Antitrypsin by a Monoclonal Antibody*

Sabina JanciauskieneDagger §, Ruta DominaitieneDagger , Nils H. Sternby, Eva Piitulainen||, and Sten ErikssonDagger

From the Departments of Dagger  Internal Medicine,  Pathology, and || Respiratory Medicine, University Hospital, Malmö, 20502 Malmö, Sweden

Globular inclusions of abnormal alpha 1-antitrypsin (AAT) in the endoplasmic reticulum of hepatocytes are a characteristic feature of AAT deficiency of the PiZZ phenotype. Monoclonal antibodies, which contain constant specificity and affinity, are often used for the identification of Z-mutation carriers. A mouse monoclonal antibody (ATZ11) raised against PiZZ hepatocytic AAT was successfully used in enzyme-linked immunosorbent assays (ELISA) and in identification of Z-related AAT globular inclusions by immunohistochemical techniques. Using electrophoresis, Western blotting, and ELISA procedures, we have shown in the present study that this monoclonal antibody specifically detects a conformation-dependent neoepitope on both polymerized and elastase-complexed molecular forms of AAT. The antibody has no apparent affinity for native, latent, or cleaved forms of AAT. The antibody ATZ11 illustrates the structural resemblance between the polymerized form of AAT and its complex with elastase and provides evidence that Z-homozygotes beyond the native form may have at least one more circulating molecular form of AAT, i.e. its polymerized form. In addition, staining of endothelial cells with ATZ11 antibody in both M- and Z-AAT individuals shows that AAT attached to endothelial cells is in a polymerized form. The antibody can be a powerful tool for the study of the molecular profile of AAT, not only in Z-deficiency cases but also in other (patho)physiological conditions.

* This work was funded in part by the Swedish Medical Research Council (K01-72X), the Medical Faculty of Lund University, and the Tore Nilsson and Alfred Österlund Foundations.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.

§ To whom correspondence should be addressed: Dept. of Medicine, Wallenberg Laboratory, Ing. 46, UMAS, S-20502, Malmö, Sweden. Tel.: 46-40-33-14-14; Fax: 46-40-33-40-71; E-mail: sabina.janciauskiene@medforsk.mas.lu.se.

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