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(American Journal of Pathology. 2003;163:81-89.)
© 2003 American Society for Investigative Pathology

Up-Regulation of ALG-2 in Hepatomas and Lung Cancer Tissue

Jonas M. la Cour^*, Jens Mollerup^*, Pernille Winding^*, Svetlana Tarabykina^*, Maxwell Sehested and Martin W. Berchtold^*

From the Department of Molecular Cell Biology,^* Institute of Molecular Biology, University of Copenhagen, Copenhagen, and the Department of Pathology, University Hospital, Copenhagen, Denmark

ALG-2 was isolated in a screen for proteins involved in programmed cell death and is the first Ca²⁺-binding protein found to be directly involved in apoptosis. We have generated polyclonal antibodies that are suitable for detecting ALG-2 using different immunological methods. Three commercial antibodies against ALG-2 did neither detect mouse recombinant ALG-2 nor endogenous ALG-2 in Jurkat cell lysates, whereas our own affinity-purified antibody recognized recombinant as well as endogenous ALG-2. The specificity of the antibody was shown by preabsorbtion experiments and on ALG-2-deficient cells using Western blot analysis and immunohistochemistry. Western blot analysis of 15 different adult mouse tissues demonstrated that ALG-2 is ubiquitously expressed. We found that ALG-2 was more than threefold overexpressed in rat liver hepatoma compared to normal rat liver using Western blot analysis, a result confirmed by immunohistochemical analysis. Staining of four different lung cancer tissue microarrays including specimens of 263 patients showed that ALG-2 is mainly localized to epithelial cells and significantly up-regulated in small-cell lung cancers and in non-small-cell lung cancers. Our results lead to the conclusion that ALG-2 beside its known proapoptotic functions may be a player in survival pathways.

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