July 1990
Volume 31, Issue 7
Free
Articles  |   July 1990
Immunohistochemical localization of cathepsin D in ocular tissues.
Author Affiliations
  • T Yamada
    Department of Ophthalmology, Tohoku University School of Medicine, Sendai, Japan.
  • S Hara
    Department of Ophthalmology, Tohoku University School of Medicine, Sendai, Japan.
  • M Tamai
    Department of Ophthalmology, Tohoku University School of Medicine, Sendai, Japan.
Investigative Ophthalmology & Visual Science July 1990, Vol.31, 1217-1223. doi:
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      T Yamada, S Hara, M Tamai; Immunohistochemical localization of cathepsin D in ocular tissues.. Invest. Ophthalmol. Vis. Sci. 1990;31(7):1217-1223.

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Abstract

Cathepsin D has been believed to play an important role in the catabolism of protein in various tissues. In retinal pigment epithelium, cathepsin D degrades rod outer segments and rhodopsin into glycopeptides. To our knowledge, no reports have described the immunohistochemical localization of cathepsin D in whole ocular tissues. We investigated the reaction of bovine, rat, and human eyes with a polyclonal antibody to cathepsin D from bovine spleen. Cathepsin D immunoreactivity was observed in the cytoplasm of the following cells: epithelium and endothelium of the cornea; keratocytes; pigmented and nonpigmented epithelium of the ciliary body; epithelium and cortex of the lens; epithelium and sphincter and dilator muscles of the iris; MĂĽller cells; ganglion cells and pigment epithelium of the retina; and endothelium of various vessels. Positively stained ocular tissues were believed to have a high activity of protein catabolism. Since cathepsin D was closely associated with phagosomes in retinal pigment epithelium, we concluded that cathepsin D probably contributes to the physiologic degradation of rod outer segments.

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