The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L
Open accessAbstract
We have investigated the susceptibility of both the helical and non‐helical regions of isolated rat chondrosarcoma collagens, types II, IX and XI, to degradation by the cysteine proteinases, cathepsins B and L. Both enzymes degrade these collagens at temperatures from 20 to 37°C and pH values from 3.5 to 7.0. Cleavage occurs only within the non‐helical domains unless the helix is destabilized. Cathepsin L is more effective than cathepsin B on a molar basis and they appear to cleave at different sites. Since these cathepsins can degrade cartilage collagens at pH values near neutrality, they may contribute to the destruction of cartilage observed in arthritis.
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“According to earlier research, cathepsins are most active in an acidic environment and are released in an active state when the pH of the environment around the cell is below a certain level.148,149”
From Smart nanoparticles for cancer therapy (2023) · cites this paper as [148]
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Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Cartilage contains mixed fibrils of collagen types II, IX, and XI.
Mendler, M., Eich-Bender, S. G., Vaughan, L., Winterhalter, K. H., & Brückner, P. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.1.191 · Cited by 510
Cartilage collagens. What Is Their Function, and Are They Involved in Articular Disease?
Mayne, R. (1989) · Arthritis & Rheumatism · doi:10.1002/anr.1780320302 · Cited by 193
A comparison of four cathepsins (B, L, N and S) with collagenolytic activity from rabbit spleen
Maciewicz, R. A., & Etherington, D. J. (1988) · Biochemical Journal · doi:10.1042/bj2560433 · Cited by 160
Self-citationOkada, Y., Konomi, H., Yada, T., Kimata, K., & Nagase, H. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80586-1 · Cited by 96
Maciewicz, R. A., Wardale, R. J., Etherington, D. J., & Paraskeva, C. (1989) · International Journal of Cancer · doi:10.1002/ijc.2910430323 · Cited by 96
Self-citationMetalloproteinases and collagenase inhibitors in rheumatoid synovial fluid
Cawston, T. E., Mercer, E., Silva, M. D., & Hazleman, B. L. (1984) · Arthritis & Rheumatism · doi:10.1002/art.1780270306 · Cited by 87
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Self-citationActive center differences between cathepsins L and B: The S1 binding region
Kirschke, H., Wikström, P., & Shaw, E. N. (1988) · FEBS Letters · doi:10.1016/0014-5793(88)80600-8 · Cited by 70
From tadpole collagenase to a family of matrix metalloproteinases
Birkedal‐Hansen, H. (1988) · Journal of Oral Pathology and Medicine · doi:10.1111/j.1600-0714.1988.tb01313.x · Cited by 66
Research works printed but not linked: 3
- Lenarcic B., 1988, Biol. Chem. Hoppe-Seyler, 36, 257
- Maciewicz R.A., 1990, Biol. Chem. Hoppe-Seyler, 371
- Barrett A.J., 1981, Methods in Enzymology, 525
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Smart nanoparticles for cancer therapy
Sun, L., Liu, H., Ye, Y., Lei, Y., Islam, R., Tan, S., Tong, R., Miao, Y.-B., & Cai, L. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01642-x · Cited by 1,073
Müller‐Ladner, U., Kriegsmann, J., Franklin, B. N., Matsumoto, S., Geiler, T., Gay, R. E., & Gay, S. (1996) · Europe PMC (PubMed Central) · Cited by 606
Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumour tissues
Buck, M., Karustis, D. G., Day, N. A., Honn, K. V., & Sloane, B. F. (1992) · Biochemical Journal · doi:10.1042/bj2820273 · Cited by 424
Human cathepsin K cleaves native type I and II collagens at the N-terminal end of the triple helix
Kafienah, W., Brömme, D., Buttle, D. J., Croucher, L. J., & Hollander, A. P. (1998) · Biochemical Journal · doi:10.1042/bj3310727 · Cited by 358
Cathepsin cysteine proteases in cardiovascular disease
Lutgens, S. P. M., Cleutjens, K. B. J. M., Daemen, M. J. A. P., & Heeneman, S. (2007) · The FASEB Journal · doi:10.1096/fj.06-7924com · Cited by 351
Metadata
- Authors
- Maciewicz, R. A., Wotton, S. F., Etherington, D. J., & Duance, V. C.
- Corresponding author
- Maciewicz, Rose A.
- ORCID
- Maciewicz, Rose A.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1990-08-20
- Volume
- 269
- Issue
- 1
- Pages
- 189-193
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2063035603
- Cited by
- 147
- References
- 17
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 4 · 2019: 3 · 2018: 5 · 2017: 3 · 2016: 3 · 2015: 6 · 2014: 1 · 2012: 3
- FWCI
- 3.86
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Rheumatology › Osteoarthritis Treatment and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- cartilage collagen, type II collagen, type IX collagen, type XI collagen, cathepsin B, cathepsin L, cysteine protease, collagen degradation, helix destabilization, arthritis, cartilage destruction
- MeSH terms
- Cathepsin B, Cathepsins, Collagen, Cysteine Endopeptidases, Humans, Hydrogen-Ion Concentration, Liver, Peptide Mapping, Endopeptidases, Temperature, Cathepsin L, In Vitro Techniques
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