Lewis x Antigen Mediates Adhesion of Human Breast Carcinoma Cells to Activated Endothelium. Possible Involvement of the Endothelial Scavenger Receptor C-type Lectin

• DOI: 10.1007/s10549-006-9286-9
• Publication Date: 2006-07-18T08:08:25Z
• Authors: María Teresa Elola; Mariana Isabel Ca...; María Marcela Barrio; Peter J. Coombs; Maureen E. Taylor; Kurt Drickamer; José Mordoh
• Keywords: 0301 basic medicine; LEWIS X; SSEA-1; Neutrophils; Blotting, Western; Antibodies, Monoclonal; Endothelial Cells; Fluorescent Antibody Technique; Lewis X Antigen; Breast Neoplasms; Flow Cytometry; 3. Good health; 03 medical and health sciences; Galβ(1–4)Fucα(1–3)GlcNAc; Cell Line, Tumor; https://purl.org/becyt/ford/3.2; Cell Adhesion; Humans; Female; Lectins, C-Type; https://purl.org/becyt/ford/3; Endothelium, Vascular

Lewis x (Le(x), CD15), also known as SSEA-1 (stage specific embryonic antigen-1), is a trisaccharide with the structure Galbeta(1-4)Fucalpha(1-3)GlcNAc, which is expressed on glycoconjugates in human polymorphonuclear granulocytes and various tumors such as colon and breast carcinoma. We have investigated the role of Le(x) in the adhesion of MCF-7 human breast cancer cells and PMN to human umbilical endothelial cells (HUVEC) and the effects of two different anti-Le(x) mAbs (FC-2.15 and MCS-1) on this adhesion. We also analyzed the cytolysis of Le(x+)-cells induced by anti-Le(x) mAbs and complement when cells were adhered to the endothelium, and the effect of these antibodies on HUVEC. The results indicate that MCF-7 cells can bind to HUVEC, and that MCS-1 but not FC-2.15 mAb inhibit this interaction. Both mAbs can efficiently lyse MCF-7 cells bound to HUVEC in the presence of complement without damaging endothelial cells. We also found a Le(x)-dependent PMN interaction with HUVEC. Although both anti-Le(x) mAbs lysed PMN in suspension and adhered to HUVEC, PMN aggregation was only induced by mAb FC-2.15. Blotting studies revealed that the endothelial scavenger receptor C-type lectin (SRCL), which binds Le(x)-trisaccharide, interacts with specific glycoproteins of M (r ) approximately 28 kD and 10 kD from MCF-7 cells. The interaction between Le(x+)-cancer cells and vascular endothelium is a potential target for cancer treatment.