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Degradation of Rod Outer Segment Proteins by Cathepsin D
Abstract
The degradation of proteins of the rod outer segment (ROS) fraction by partially purified cathepsin D [EC 3.4.23.5] from the retinal pigment epithelium was studied. The ROS fraction, prepared from bovine eyes by sucrose density gradient centrifugation, had little cathepsin D activity. Partially purified cathepsin D, obtained from crude extract of bovine retinal pigment epithelium using bovine serum albumin as a substrate, hydrolyzed the porteine of the ROS fraction. The rate of degradation of ROS proteins was proportional to both the enzyme concentration and the incubation time. With ROS proteins as substrate, the optimal pH of cathepsin D was about 3.5. The degradation of ROS proteins was inhibited by pepstatin.
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In the citing paper
“It was reported to degrade OS proteins in vitro (Hayasaka et al., 1975; Rakoczy et al., 1997), including rhodopsin (Regan et al., 1980).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Hayasaka et al., 1975
In the citing paper
“RPE melanosomes contain proteases (Azarian et al., 2006), including cathepsin D, a major enzyme in the degradation of OS proteins (Hayasaka et al., 1975), and have been observed to fuse with phagosomes (e.g. Schraermeyer et al., 1999).”
From The cell biology of the retinal pigment epithelium (2020) · cites this paper as Hayasaka et al., 1975
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The cell biology of the retinal pigment epithelium
Lakkaraju, A., Umapathy, A., Tan, L. X., Daniele, L., Philp, N. J., Boesze-Battaglia, K., & Williams, D. S. (2020) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100846 · Cited by 422
“, 2006), including cathepsin D, a major enzyme in the degradation of OS proteins (Hayasaka et al., 1975), and have been observed to fuse with phagosomes (e.”
BackgroundLipofuscin of the retinal pigment epithelium: A review
Kennedy, C. J., Rakoczy, P. E., & Constable, I. J. (1995) · Eye · doi:10.1038/eye.1995.192 · Cited by 366
Liu, J., Lu, W., Reigada, D., Nguyen, J., Laties, A. M., & Mitchell, C. H. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.07-0675 · Cited by 141
Baltazar, G. C., Guha, S., Lu, W., Lim, J. C.-S., Boesze‐Battaglia, K., Laties, A. M., Tyagi, P., Kompella, U. B., & Mitchell, C. H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049635 · Cited by 141
“Cathepsin D is a major protease in the lysosomes of RPE cells and contributes to the degradation of phagocytosed photoreceptor outer segments [34].”
BackgroundPADGETT, L. C., LUI, G.-M., Werb, Z., & LaVail, M. M. (1997) · Experimental Eye Research · doi:10.1006/exer.1997.0287 · Cited by 84
Metadata
- Authors
- HAYASAKA, S., HARA, S., & MIZUNO, K.
- Affiliations
- Tohoku University (JP)
- ORCID
- HARA, Satoshi
- Venue
- The Journal of Biochemistry
- Publisher
- Oxford University Press (OUP)
- Published
- 1975-12
- Volume
- 78
- Issue
- 6
- Pages
- 1365-1367
- ISSN
- 0021-924X (ISSN-L)
- 1756-2651
- OpenAlex
- W1846923783
- Cited by
- 34
- References
- 0
- Citations by year
- 2024: 3 · 2021: 1 · 2020: 3 · 2019: 1 · 2015: 1 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.96
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The Journal of Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Ophthalmology › Retinal Development and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- cathepsin D, retinal pigment epithelium, protein degradation, proteolysis, pepstatin inhibition, pH optimum, bovine retina
- MeSH terms
- Animals, Cathepsins, Cattle, Epithelial Cells, Epithelium, Eye Proteins, Pepstatins, Photoreceptor Cells, Protein Denaturation, Serum Albumin, Bovine
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