Epidermal lamellar granules (LGs) are specialized organelles that transport and secrete various molecules, including lipids, proteases, protease inhibitors, and structural proteins, thereby providing a protective barrier against the environment. Abnormalities in LG-related molecules result in severe skin diseases, but their transport mechanisms are poorly understood. We studied the distribution of Rab11, a common GTPase in recycling endosomes, in normal human epidermis. Confocal laser scanning microscopy detected Rab11 immunoreactivity in differentiated epidermal keratinocytes. Staining was strong at the apical side of each cell, a pattern commonly seen in LG-associated molecules. Around the nuclei, Rab11 was colocalized with TGN46, a trans-Golgi network marker. Rab11 was also colocalized with known LG-molecules, namely lymphoepithelial Kazal-type-related inhibitor, corneodesmosine, cathepsin D, and glucosylceramides. Immunoelectron microscopy revealed that Rab11 was widely distributed along TGN and tubular-vesicular structures containing different LG molecules. The present results suggest that Rab11 plays a role in the intracellular trafficking of various types of LG-molecule from the TGN to the cell surface.
