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Johan Wassélius, Katarina Håkansson, Kjell Johansson, Magnus Abrahamson, Berndt Ehinger; Identification and Localization of Retinal Cystatin C. Invest. Ophthalmol. Vis. Sci. 2001;42(8):1901-1906. doi: https://doi.org/.
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© ARVO (1962-2015); The Authors (2016-present)
purpose. Cystatin C is a mammalian cysteine protease inhibitor, synthesized in
various amounts by many kinds of cells and appearing in most body
fluids. There are reports that it may be synthesized in the mammalian
retina and that a cysteine protease inhibitor may influence the
degradation of photoreceptor outer segment proteins. In the current
study cystatin C was identified, quantitated, and localized in mouse,
rat, and human retinas.
methods. Enzyme-linked immunosorbent assay (ELISA), reverse
transcription–polymerase chain reaction (RT-PCR), DNA sequencing,
Western blot analysis, and immunohistochemistry have been used on
mouse, rat, and human retinas (pigment epithelium included).
results. Cystatin C is present in high concentrations in the normal adult rat
retina, as it is throughout its postnatal development. Its
concentration increases to a peak at the time when rat pups open their
eyes and then remains at a high level. It is mainly localized to the
pigment epithelium, but also to some few neurons of varying types in
the inner retina. Cystatin C is similarly expressed in normal mouse and
conclusions. Cystatin C was identified and the localization described in the retinas
of rat, mouse, and human using several techniques. Cystatin C is known
to efficiently inactivate certain cysteine proteases. One of them,
cathepsin S, is present in the retinal pigment epithelium and affects
the proteolytic processing by cathepsin D of diurnally shed
photoreceptor outer segments. Hypothetically, it appears possible that
retinal cystatin C, given its localization to the pigment epithelium
and its ability to inhibit cathepsin S, could be involved in the
regulation of photoreceptor degradation.
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