Identification and localization of retinal cystatin C
(2001) In Investigative Ophthalmology & Visual Science 42(8). p.1901-1906- Abstract
- 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... (More)
- 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 human retinas. 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1120822
- author
- Wasselius, Johan LU ; Håkansson, Katarina LU ; Johansson, Kjell LU ; Abrahamson, Magnus LU and Ehinger, Berndt LU
- organization
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Investigative Ophthalmology & Visual Science
- volume
- 42
- issue
- 8
- pages
- 1901 - 1906
- publisher
- Association for Research in Vision and Ophthalmology Inc.
- external identifiers
-
- pmid:11431459
- scopus:0034934606
- ISSN
- 1552-5783
- language
- English
- LU publication?
- yes
- id
- fe11792a-c9f1-46d4-9663-0dbd3f6afa9f (old id 1120822)
- alternative location
- http://www.iovs.org/cgi/content/full/42/8/1901
- date added to LUP
- 2016-04-01 15:39:16
- date last changed
- 2022-02-12 08:59:54
@article{fe11792a-c9f1-46d4-9663-0dbd3f6afa9f, abstract = {{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 human retinas. 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.}}, author = {{Wasselius, Johan and Håkansson, Katarina and Johansson, Kjell and Abrahamson, Magnus and Ehinger, Berndt}}, issn = {{1552-5783}}, language = {{eng}}, number = {{8}}, pages = {{1901--1906}}, publisher = {{Association for Research in Vision and Ophthalmology Inc.}}, series = {{Investigative Ophthalmology & Visual Science}}, title = {{Identification and localization of retinal cystatin C}}, url = {{http://www.iovs.org/cgi/content/full/42/8/1901}}, volume = {{42}}, year = {{2001}}, }