Knock-Down of Cathepsin D Affects the Retinal Pigment Epithelium, Impairs Swim-Bladder Ontogenesis and Causes Premature Death in Zebrafish (original) (raw)
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Modulation of cathepsin D activity in retinal pigment epithelial cells
Biochemical Journal, 1997
This project used retinal pigment epithelial (RPE) cells to investigate the effects of up- and down-regulation of cathepsin D expression on the processing of cathepsin D and on the normal phagocytic and digestive function of these cells. RPE cells were transfected with a pHβApr-1-neo vector construct carrying the full-length sequence of the translated region of human cathepsin D in sense and antisense directions. Transfected cells were characterized for the presence and expression of the transgene by PCR amplification using transgene-specific primers. Total aspartic proteinase activity present in transformed RPE cells was measured by an enzyme assay using haemoglobin as substrate. Flow cytometry was used to quantify phagocytosis of fluorescein isothiocyanate-labelled rod outer segments (ROS), and lysosomal digestion of ROS was monitored by immunofluorescence. A 435 bp fragment was present in RPE cells carrying the cathepsin D transgene in sense and antisense orientations after PCR a...
Cathepsin D: a cellular roadmap
Biochemical and biophysical research communications, 2008
Cathepsin D is a normal and major component of lysosomes, it is found in almost all cells and tissues of mammals. Present review describes different events in cellular life of cathepsin D mainly its biosynthesis, co-translational and posttranslational modifications, targeting to lysosomes and proteolytic processing and maturation within lysosomes.
Distribution of Cathepsin D in Human Eyes with or without Age-related Maculopathy
Experimental Eye Research, 1999
Cathepsin D is a ubiquitous enzyme which plays an important role in the catabolism of proteins. Enzymatic studies showed that cathepsin D is the most important lysosomal enzyme in the proteolysis of opsin. The importance of cathepsin D in the lysosomal digestion of phagocytosed photoreceptor outer segments by the retinal pigment epithelium suggests that a decrease in cathepsin D activity might contribute to the development of hyalinized drusen and to the development of age-related maculopathy. The aim of this project was to study the immunohistochemical localization of cathepsin D in human eyes and particularly to compare the immunoreactivity of cathepsin D normal retinal pigment epithelial cells and in cells surrounding hyalinized drusen or lesions of age-related maculopathy. Following clinicopathological examinations the eyes were fixed, paraffin embedded and individual sections were subjected to Picro-Mallory staining for histopathological examination. Bleaching was performed then immunohistochemistry was carried out using a monoclonal mouse anti-human cathepsin D antibody. On the basis of the appearance of basal laminar deposit the eyes were divided into five groups corresponding to levels of progression in age-related maculopathy development. Following optimization of bleaching cathepsin D immunostaining was clearly visible in the iris epithelium, ciliary body and the retinal pigment epithelial layer of all eyes with the highest immunoreactivity present in the RPE cells. Within the neural retina the ganglion cells demonstrated a weak signal. Retinal pigment epithelial cathepsin D immunoreactivity was not impaired by age, geographical location or by age-related maculopathy status.
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