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(American Journal of Pathology. 2001;159:537-546.)
© 2001 American Society for Investigative Pathology

Regular Articles

cis Interaction of the Cell Adhesion Molecule CEACAM1 with Integrin ß₃

Jens Brümmer^*, Alireza Ebrahimnejad^*, Raid Flayeh^*, Udo Schumacher, Thomas Löning, Ana-Maria Bamberger and Christoph Wagener^*

From the Department of Clinical Chemistry,^*
Clinic of Internal Medicine, the Department of Neuroanatomy,
Institute of Anatomy, and the Institute of Pathology,
University Hospital Eppendorf, Hamburg, Germany

CEACAM1 is a cell adhesion molecule that has been implicated in a number of physiological processes (eg, tumor suppressor in epithelial tissues, potent angiogenic factor in microvessel formation, microbial receptor in human granulocytes and epithelial cells). The mechanism of CEACAM1 action is still largely unresolved but recent findings demonstrated that the cytoplasmic CEACAM1 domain is linked indirectly to the actin-based cytoskeleton. We have isolated integrin ß₃ as an associated protein using CEACAM1 tail affinity purification. This association depends on phosphorylation of Tyr-488 in the CEACAM1 cytoplasmic domain. Confocal laser scanning microscopy confirmed in vivo colocalization of both molecules in human granulocytes and epithelial cells. Furthermore, the concentrated colocalization at the tumor-stroma interface of invading melanoma masses suggests a functional role of CEACAM1-integrin ß₃ interaction in melanoma invasion. Moreover, colocalization of the two adhesion molecules is also found at the apical surface of glandular cells of pregnancy endometrium. Colocalization of CEACAM1 and integrin ß₃ at the transitional zone from proliferative to invasive extravillous trophoblast of the maternal-fetal interface supports a role for CEACAM1/integrin ß₃ complexes in cell invasion.

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