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Abstract
The monoclonal antibody M-DC8 defines a major subset of human blood dendritic cells
(DCs). Here we identify the M-DC8 structure as 6-sulfo LacNAc, a novel carbohydrate
modification of the P selectin glycoprotein ligand 1 (PSGL-1). In contrast to previously
described blood DCs, M-DC8+ DCs lack the cutaneous lymphocyte antigen (CLA) on PSGL-1
and fail to bind P and E selectin. Yet they express anaphylatoxin receptors (C5aR
and C3aR) and the Fcgamma receptor III (CD16), which recruit cells to inflammatory
sites. While sharing with DC1 the expression of myeloid markers and a potent capacity
to prime T cells in vitro, M-DC8+ DCs produce far more TNF-alpha in response to the
bacterial endotoxin lipopolysaccharide (LPS). Thus, 6-sulfo LacNAc-expressing DCs
appear as a novel proinflammatory DC subset.