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Abstract
The aberrant expression of myeloid antigens on acute lymphoblastic leukemia (ALL)
cells is a well-documented phenomenon. So far, there have been no reports of a functional
consequence of this aberrant expression. The granulocytic marker carcinoembryonic
antigen-related cell adhesion molecule 6 (CEACAM6, CD66c) is a GPI-anchored molecule
that is reported to be the most frequently aberrantly expressed myeloid marker in
ALL with a strong correlation with genotype.
We mimicked CEACAM6 signaling in ALL cells by cross-linking with anti-CEACAM6 antibody.
Next, we measured a response to CEACAM6 signaling by integrin subunits expression,
integrin ligand binding, phosphorylation of extracellular signal-regulated kinase
1/2 (Erk1/2), Akt, and p38 mitogen-activated protein kinase (MAPK) and apoptosis by
flow cytometry.
Following CEACAM6 cross-linking in ALL cells, we detected Erk1/2, Akt, and p38 MAPK
phosphorylation and integrin upregulation, as well as enhanced binding of integrin
ligands (vascular cell adhesion molecule-1 [VCAM-1] and intercellular cell adhesion
molecule-1 [ICAM-1]). However, CEACAM6 signaling resulted in an increase in apoptosis,
unlike other GPI-anchored molecules, such as CD24.
The present study is the first to demonstrate the functional consequences of CEACAM6
cross-linking in B-cell precursor ALL cells.
2010 ISEH - Society for Hematology and Stem Cells. Published by Elsevier Inc. All
rights reserved.