The ultrastructure of cells of the renal tubule and its relationship to subepithelial amyloid deposits were studied in experimentally induced amyloidosis in guinea pigs. Amyloid fibrils were demarcated primarily between the epithelial cell and its basement membrane. Basal plasmalemmal infoldings were diminished whenever the cell abutted amyloid. Pocket-like plasmalemmal invaginations, associated with tufts of well-oriented amyloid fibrils, were found occasionally. lntracellular membrane-bound amyloid fibrils, fibrils i n the extracellular space between two epithelial plasma membranes, and fibrils surrounded by basement membrane were also seen on rare occasions. These findings are discussed in relation to clinical features of renal amyloidosis.In a previous communication (1) we surveyed casein-induced renal amyloidosis in guinea pigs by light and electron microscopy. I n brief, the renal amyloid was peritu- bular and classified as subepithelial, pericapillary or interstitial, depending upon the site of the lesion on electron microscopic study. A major site of deposition of amyloid fibrils was between the epithelial cell and the basement membrane, where deposits were oriented or polarized towards the adjacent capillary. Changes in the infoldings of the basal plasma membrane of the renal tubule cell were also observed. This communication describes in greater detail the ultrastructural features of renal tubule cells and their relation to the subepithelial amyloid deposits.