The DOI matches its Crossref record.
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
Guha, S., Liu, J., Baltazar, G., Laties, A. M., & Mitchell, C. H. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-3209-8_14 · Cited by 64
Lysosomal enzymes in ocular tissues and diseases
Hayasaka, S. (1983) · Survey of Ophthalmology · doi:10.1016/0039-6257(83)90125-x · Cited by 54
Self-citationMelanoregulin (MREG) modulates lysosome function in pigment epithelial cells
Damek-Poprawa, M., Diemer, T., Lopes, V. S., Lillo, C., Harper, D. C., Marks, M. S., Wu, Y., Sparrow, J. R., Rachel, R. A., Williams, D. S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808857200 · Cited by 50
Comparative Pathology of Murine Mucolipidosis Types II and IIIC
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Autofluorescent inclusions in long-term postconfluent cultures of retinal pigment epithelium.
Burke, J. M., & Skumatz, C. M. B. (1998) · PubMed · Cited by 41
Proteomic analysis of mature melanosomes from the retinal pigmented epithelium
Azarian, S. M., McLeod, I., Lillo, C., Gibbs, D., Yates, J. R., & Williams, D. S. (2006) · Journal of Proteome Research · doi:10.1021/pr0502323 · Cited by 35
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Bird, A. C. (2020) · British Journal of Ophthalmology · doi:10.1136/bjophthalmol-2020-317447 · Cited by 33
Retinal light-damage in albino rats: Lysosomal enzymes, rhodopsin, and age
Penn, J. S., Baker, B. N., Howard, A. G., & Williams, T. P. (1985) · Experimental Eye Research · doi:10.1016/s0014-4835(85)80017-8 · Cited by 32
Dalvi, S., Galloway, C. A., Winschel, L., Hashim, A., Soto, C. A., Tang, C., MacDonald, L. A., & Singh, R. (2019) · Cell Death Discovery · doi:10.1038/s41420-019-0171-9 · Cited by 28
Jiang, M., Paniagua, A. E., Volland, S., Wang, H., Balaji, A., Li, D. G., Lopes, V. S., Burgess, B. L., & Williams, D. S. (2020) · Journal of Cell Science · doi:10.1242/jcs.242214 · Cited by 28
Lysosomal enzymes in subretinal fluid
Hayasaka, S., Hara, S., & Mizuno, K. (1976) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/bf00411429 · Cited by 22
Self-citationRegional comparisons of cathepsin D activity in bovine retinal pigment epithelium.
Burke, J. M., & Twining, S. S. (1988) · PubMed · Cited by 20
Regional distribution of lysosomal enzymes in the retina and choroid of human eyes
Hayasaka, S., Shiono, T., Hara, S., et al. (1981) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/bf00455034 · Cited by 18
Self-citationDistribution and some properties of cathepsin B in the bovine eyes
Hayasaka, S., Hara, S., Takaku, Y., et al. (1978) · Experimental Eye Research · doi:10.1016/0014-4835(78)90151-3 · Cited by 18
Self-citationExtracellular Acidification Induces Lysosomal Dysregulation
Ordway, B., Gillies, R. J., & Damaghi, M. (2021) · Cells · doi:10.3390/cells10051188 · Cited by 17
Hara, S., Ishiguro, S.-I., Hayasaka, S., et al. (1987) · Archives of Ophthalmology · doi:10.1001/archopht.1987.01060020114041 · Cited by 13
Self-citationLysosomal behavior in the retina and choroid of spontaneously dystrophic rats
Hayasaka, S., Takahashi, J., & Mizuno, K. (1977) · Experimental Eye Research · doi:10.1016/0014-4835(77)90153-1 · Cited by 13
Self-citationHara, S., Plantner, J. J., & Kean, E. L. (1983) · Experimental Eye Research · doi:10.1016/0014-4835(83)90034-9 · Cited by 12
Self-citationModulation of V-ATPase by βA3/A1-Crystallin in Retinal Pigment Epithelial Cells
Valapala, M., Sergeev, Y. V., Wawrousek, E. F., Hose, S., Zigler, J. S., & Sinha, D. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-17121-0_104 · Cited by 10
Changes of lysosomal enzymes in the ciliary epithelium by foreign bodies
Mizuno, K., & Hayasaka, S. (1980) · Experimental Eye Research · doi:10.1016/s0014-4835(80)80053-4 · Cited by 10
Self-citationLoss of melanoregulin (MREG) enhances cathepsin-D secretion by the retinal pigment epithelium
FROST, L. S., LOPES, V. S., STEFANO, F. P., BRAGIN, A., WILLIAMS, D. S., MITCHELL, C. H., & BOESZE-BATTAGLIA, K. (2013) · Visual Neuroscience · doi:10.1017/s0952523813000096 · Cited by 9
Impaired cathepsin D in retinal pigment epithelium cells mediates Stargardt disease pathogenesis
Ng, E. S. Y., Hu, J. G., Jiang, Z., & Radu, R. A. (2024) · The FASEB Journal · doi:10.1096/fj.202400210rr · Cited by 9
“16 Like other deg-radative lysosomal enzymes, CatD functions optimally within a narrow range of acidic pH. 17,18 Importantly, the acidic environment of endo-lysosomes is crucial for CatD maturation, converting it from an inactive precursor into a functional mature protein.”
BackgroundEffect of continuous low-intensity light on the lysosomal enzymes in the retina of albino rats
Hayasaka, S., & Lai, Y. (1979) · Experimental Eye Research · doi:10.1016/0014-4835(79)90077-0 · Cited by 9
Self-citationEnzymatic heterogeneity of bovine retinal pigment epithelial cells in vivo and in vitro
Fröhlich, E., & Klessen, C. (2001) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s004170000218 · Cited by 9
“The lysosomal proteases (dipeptidylpeptidases I and II and cathepsin B) were tested because they may be involved in the phagocytosis of ROS, as has been demonstrated for cathepsin D [19].”
Fröhlich, E., & Klessen, C. (2003) · Graefe s Archive for Clinical and Experimental Ophthalmology · doi:10.1007/s00417-003-0640-x · Cited by 8
Peroxidation of lipids and degeneration of photoreceptors in the retina of rats with avitaminosis E
Kagan, V. E., Gv, B., & Novikov, K. N. (1977) · Bulletin of Experimental Biology and Medicine · doi:10.1007/bf00807480 · Cited by 6
Cai, J., Liao, F., Mao, Y., Liu, S., Wu, X., Wang, S., Wang, S., Shan, G., & Wu, S. (2024) · Experimental Eye Research · doi:10.1016/j.exer.2024.110129 · Cited by 5
Shiono, T., Hayasaka, S., & Mizuno, K. (1983) · Experimental Eye Research · doi:10.1016/0014-4835(83)90040-4 · Cited by 2
Self-citationCellular Organization of the Retinal Pigment Epithelium
Burgoyne, T., & Futter, C. E. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-13820-1.00067-0
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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