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The Journal of Immunology, 2001, 167: 6786-6793.
Copyright © 2001 by The American Association of Immunologists

Regulation and Possible Function of {beta}-Catenin in Human Monocytes1

Andrea Thiele2,*, Mark Wasner{dagger}, Claudia Müller*, Kurt Engeland{dagger} and Sunna Hauschildt3,*

* Institute of Zoology, Department of Immunobiology, University of Leipzig, Leipzig, Germany; and {dagger} Medizinische Klinik II, Department of Internal Medicine, University of Leipzig, Max Bürger Research Center, Leipzig, Germany

In this study, we demonstrate that adherence factors, serum constituents, LPS, and zymosan are capable of inducing a cellular accumulation of {beta}-catenin in human monocytes. Whereas adherence-dependent accumulation of {beta}-catenin can be blocked by wortmannin, an inhibitor of phosphatidylinositol 3-kinase, accumulation induced by the remaining stimuli cannot be prevented by inhibition of phosphatidylinositol 3-kinase, implying the involvement of {beta}-catenin in other not yet described signal transduction pathways. A role of {beta}-catenin in adherence-dependent processes by interacting with classical cadherins can be excluded as we could not detect cadherins in monocytes. To test whether it is possible that {beta}-catenin interacts with LEF/TCF (lymphoid enhancer factor/T cell factor) transcription factors, we studied the expression of this protein family. TCF-4 was identified as the LEF/TCF transcription factor present in human monocytes. However, neither cellular induction of {beta}-catenin nor cotransfection experiments with {beta}-catenin conducted in the monocytic cell line THP-1 resulted in the activation of a LEF/TCF-dependent promoter, suggesting the requirement of additional signals. Concurrent with this suggestion, we found that LPS and zymosan, two physiological inducers of {beta}-catenin, caused an increase in the expression of genes that are positively regulated by {beta}-catenin.




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