Localization of cathepsin D in rat ocular tissues. An immunohistochemical study

Abstract

Numerous studies have demonstrated that cathepsin D as a major lysosomal acid protease plays an important role in the degradation of protein in several tissues. An important function of the retinal pigment epithelium is to interact with the photoreceptor cells in the renewal process. During the renewal process, the RPE cell phagocytosis discarded photoreceptor discs which are then degraded in the RPE phagolysosomes. It is believed that cathepsin D plays a main role in the degradation of rod outer segments and rhodopsin into glycopeptides. The cellular localization of cathepsin D immunoreactivity was examined at the light microscopic level in the ocular tissues of non-affected RCS-rdy+ rats strain by use of the alkaline phosphatase-antialkaline phosphatase (APAAP) technique. The presence of cathepsin D immunoreactivity was found in the cell cytoplasm of the following ocular tissues: retinal pigment epithelium; Müller cells; ganglion cells; pigmented and non-pigmented ciliary body; iris tissue; epithelium and endothelium of the cornea; endothelium of various vessels, including the tunica vasculosa lentis. High activity of cathepsin D was found in the RPE cells, as well as in the cytoplasm of Müller cells, especially expressed in their foot plates lying close to the inner limiting membrane.