Celiac disease is a chronic small intestinal inflammation driven by gluten‐reactive T cells of the intestinal mucosa. These T cells are HLA‐DQ2 or ‐DQ8 restricted, and predominantly recognize gluten peptides that are deamidated by the enzyme transglutaminase 2 (TG2). Our recent results strongly suggest that duodenal CD11c⁺ dendritic cells (DC) are directly involved in T cell activation in the celiac lesion. The aim of this study was to investigate whether surface‐associated TG2 could be involved in receptor‐mediated endocytosis of gluten peptides, a process that may contribute to the preferential recognition of deamidated peptides. We found that both monocyte‐derived DC and local CD11c⁺ DC in the duodenal mucosa expressed cell surface‐associated TG2. As phenotypic characterization of CD11c⁺ DC in the celiac lesion suggests that these cells may be derived from circulating monocytes, we used monocyte‐derived DC in functional in vitro studies. Using a functional T cell assay, we obtained evidence that cell surface‐associated TG2 is endocytosed by monocyte‐derived DC. However, we were unable to obtain evidence for a role of surface TG2 in the loading and subsequent generation of deamidated gluten peptides in these cells.