Claudin-1 is a critical structural component of tight junctions that have an important role in adhesive properties, barrier function, and paracellular transport of epithelia and other nonhematopoietic tissues. We found claudin-1 in murine CD207+ Langerhans cells (LC) residing in epidermis. Claudin-1 was not detected in other skin dendritic cells (DC). LC expressed claudin-1 in steady state and inflamed skin. Claudin-1 was demonstrated further in lymph node LC under steady state and inflammatory conditions, including after direct tracking with tetramethylrhodamine-isothiocyanate (TRITC). All subsets of skin draining lymph node DC defined by CD205, CD11b, CD11c, and CD8, including a presumably blood-borne lymph node resident CD8+CD207+ LC population, were claudin-1+. TRITC tracking demonstrated claudin-1 in CD207- skin migrant DC in the lymph node, suggesting upregulation of this molecule during migration or once arrived in the lymph node. Claudin-1 expression in CD207+ cells was confirmed at the protein and mRNA levels. Transforming growth factor-beta, a factor critical for the induction of LC in vitro and in vivo, stimulated the accumulation of claudin-1 mRNA and protein when added to bone marrow cells cultured with GM-CSF and IL-4. Claudin-1 may thus have an important function in adhesion and/or migration of LC.