Localization of cathepsin L in the synovial lining cells of the normal rat temporomandibular joint was investigated by the avidin-biotin-peroxidase complex method for semithin (1 microns) cryosections and the colloidal gold-labelled IgG method for ultrathin sections of LR gold resin. At the light-microscopic level, type A (macrophage-like) and B (fibroblast-like) cells formed the synovial lining layer. Extensive immunoreactivity for cathepsin L was observed in many granules and vacuoles of type A cells, while in the type B cells, immunoreactivity was found in very few granules. In the sublining layer, macrophages and a few fibroblasts were positive for cathepsin L. By electron microscopy, at the peripheral cytoplasm of the type A cells close to the lateral intercellular spaces and joint cavity, numerous coated vesicles and vacuoles (probably early endosomes) indicating endocytotic function were found. Gold particles indicating cathepsin L were localized in the vesicles (primary lysosomes) in the perinuclear cytoplasm and in the larger amorphous vacuoles (1 microns dia) as phagolysosomes. In type B cells, gold particles were limited to the vesicles only (primary lysosomes). The cathepsin L-positive primary lysosomes were numerous in a few fibroblasts in the sublining layer. These results indicate that type A cells contain a large amount of cathepsin L, and suggest that these cells endocytose surplus substances such as collagen and proteoglycan fragments in normal rat TMJ, effecting their digestion and degradation by the action of this proteolytic cathepsin.