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International Immunology, Vol. 12, No. 11, 1593-1604, November 2000
© 2000 Japanese Society for Immunology

Transendothelial migration of 27E10+ human monocytes

Ines Eue, Barbara Pietz, Josef Storck1, Martin Klempt2 and Clemens Sorg

Institute of Experimental Dermatology and
1 Institute of Physiology, University of Münster, von-Esmarch-Strasse 56, 48149 Münster, Germany
2 Institute of Physiology and Biochemistry of Nutrition, Federal Dairy Research Center, 24103 Kiel, Germany

Correspondence to: I. Eue

The myeloid-related proteins MRP8 (S100A8) and MRP14 (S100A9), two members of the S100 family of calcium-binding proteins, are co-expressed and form a cell-surface and cytoskeleton-associated heterodimer upon calcium mobilization which is recognized by the mAb 27E10. The heterodimer is abundantly expressed in the cytoplasm of granulocytes and a subpopulation of blood monocytes. Previously, we and others demonstrated endothelium-associated MRP8/14 in inflamed tissues in the vicinity of transmigrating leukocytes, suggesting a function of the proteins in this process. Here, we demonstrate that 27E10+ cells represent a fast-migrating monocyte subpopulation which preferentially utilizes an ICAM-1-dependent mechanism. The following observations imply a function of MRP8/14 in the transmigration process: (i) higher secretion of MRP8/14 from 27E10+ monocytes compared to 27E10 monocytes after interaction with activated endothelium, (ii) higher expression of CD11b on 27E10+ compared to 27E10 monocytes, (iii) up-regulation of CD11b on 27E10 monocytes in the presence of MRP14 or MRP8/14 heterodimers but not MRP8 and (iv) active participation of MRP14 but not of MRP8 in transmigration as shown by blocking with respective antibodies. We show that the interaction of 27E10+ monocytes with activated endothelium leads to MRP8/14 release which may account for the high MRP8/14 concentrations in body fluids of patients with acute or chronic inflammatory diseases. Released MRP8/14 may serve a function by enhancing CD11b expression and/or affinity in human monocytes and by participating in the transendothelial migration mechanism. Thus, MRP8/14 substantially contributes to the recruitment of monocytes to an inflammatory site.

Keywords: 27E10, adhesion, inflammation, MRP8, MRP14, myeloid-related proteins, S100A8, S100A9

Transmitting editor: A. Radbruch


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