Cathepsins are specific proteases in lysosomes that parucipate in the degradation of proteins, some of which are derived from endocytosis. In this study we examined the immunocytochemical localization of cathepsin B and D antibodies in cells of rat testis and epididymis, using light and electron "pi c immunocytochemistry. In testis, cathepsin D was immunolocalized over lysosomes of Sertoli cells and Leydig cells and on the acrosome of spermatids. Cathepsin B was found over lysosomes of macrophages. Non-ciliated The epididymis is an organ consisting of an epithelium lined by several cell types with specific structural features and functions. Principal cells, the major cell type throughout the epididymis, are involved in regional secretion and endocytosis of specific proteins along the length of the epididymis (reviewed in Hermo et al., 1994;Robaire and Hermo, 1988;Cooper, 1986;Hamilton, 1975). Epithelial clear cells are also involved in regional differences with respect to the endocytosis of various substances along the epididymal length, including the uptake of the contents of cytoplasmic droplets that detach from spermatozoa in the distal part of the duct (Hermo et al., ,1992bMoore and Bedford, 1979). In both these cell types, endocytosed substances eventually end up in lysosomes, where they are presumably degraded.Lysosomes