Cited by 150Protease and Inhibitor MechanismsOsteoarthritis Treatment and MechanismsProteoglycans and glycosaminoglycans research

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 access

Maciewicz, Rose A., Wotton, Sandra F., Etherington, David J., Duance, Victor C.·1990·FEBS Letters

DOI 10.1016/0014-5793(90)81151-d

Open this paper in CoChat — free account Open PDF

Abstract

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.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/0014-5793(90)81151-d

Cites

17 of 17 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

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-citation
Degradation of type IX collagen by matrix metalloproteinase 3 (stromelysin) from human rheumatoid synovial cells
Okada, Y., Konomi, H., Yada, T., Kimata, K., & Nagase, H. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80586-1 · Cited by 96
Immunodetection of cathepsins b and l present in and secreted from human pre‐malignant and malignant colorectal tumour cell lines
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-citation
Metalloproteinases 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
Susceptibility of cartilage collagens type II, IX, X, and XI to human synovial collagenase and neutrophil elastase
Gadher, S. J., Eyre, D. R., Duance, V. C., Wotton, S. F., Heck, L. W., Schmid, T. M., & Woolley, D. E. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14158.x · Cited by 73
Self-citation
Active 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

Show all 17 references

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

Sorted by citations

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
Synovial fibroblasts of patients with rheumatoid arthritis attach to and invade normal human cartilage when engrafted into SCID mice.
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
The interglobular domain of cartilage aggrecan is cleaved by PUMP, gelatinases, and cathepsin B.
Fosang, A., Neame, P. J., Last, K., Hardingham, T., Murphy, G., & Hamilton, J. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41799-1 · Cited by 297
Molecular and cellular mechanisms of joint destruction in rheumatoid arthritis: two cellular mechanisms explain joint destruction?
Gay, S., Gay, R. E., & Koopman, W. J. (1993) · Annals of the Rheumatic Diseases · doi:10.1136/ard.52.suppl_1.s39 · Cited by 262
Effects of dietary arginine supplementation on growth performance, flesh quality, muscle antioxidant capacity and antioxidant-related signalling molecule expression in young grass carp (Ctenopharyngodon idella)
Wang, B., Liu, Y., Feng, L., Jiang, W., Kuang, S., Jiang, J., Li, S., Tang, L. Y., & Zhou, X. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.06.091 · Cited by 248
Regulation of Collagenase Activities of Human Cathepsins by Glycosaminoglycans
Li, Z., Yasuda, Y., Li, W., Bogyo, M. S., Katz, N., Gordon, R. E., Fields, G. B., & Brömme, D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310349200 · Cited by 235
Metabolic changes associated with tumor metastasis, part 1: tumor pH, glycolysis and the pentose phosphate pathway
Payen, V. L., Porporato, P. E., Baselet, B., & Sonveaux, P. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2098-5 · Cited by 226
Bone formation and resorption biological markers in cosmonauts during and after a 180-day space flight (Euromir 95)
Caillot‐Augusseau, A., Lafage‐Proust, M., Soler, C., Pernod, J., Dubois, F., & Alexandre, C. (1998) · Clinical Chemistry · doi:10.1093/clinchem/44.3.578 · Cited by 218
Different effects of bisphosphonate and estrogen therapy on free and peptide-bound bone cross-links excretion
Garnero, P., Gineyts, É., Arbault, P., Christiansen, C., & Delmas, P. D. (1995) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.5650100418 · Cited by 215
Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival.
Campo, E., Muñoz, J., Miquel, R., Palacı́n, A., Cardesa, A., Sloane, B. F., & Emmert‐Buck, M. R. (1994) · PubMed Central · Cited by 214
Cathepsin L targeting in cancer treatment
Sudhan, D. R., & Siemann, D. W. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.08.007 · Cited by 215
Cathepsin B: A sellsword of cancer progression
Mijanović, O., Branković, A., Panin, A. N., Savchuk, S., Timashev, P., Ulasov, I., & Lesniak, M. S. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.02.035 · Cited by 205
Alterations in extracellular matrix composition during aging and photoaging of the skin
McCabe, M. C., Hill, R. C., Calderone, K., Cui, Y., Yan, Y., Quan, T., Fisher, G. J., & Hansen, K. C. (2020) · Matrix Biology Plus · doi:10.1016/j.mbplus.2020.100041 · Cited by 196
C ysteine P eptidases of M ammals: T heir B iological R oles and P otential E ffects in the O ral C avity and O ther T issues in H ealth and D isease
Dickinson, D. P. (2002) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/154411130201300304 · Cited by 181
Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2
Shi, G., Chapman, H. A., Bhairi, S. M., DeLeeuw, C., Reddy, V. Y., & Weiss, S. J. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01349-6 · Cited by 174
An intracellular form of cathepsin B contributes to invasiveness in cancer.
Szpaderska, A. M., & Frankfater, A. (2001) · PubMed · Cited by 168
Effective activation of the proenzyme form of the urokinase‐type plasminogen activator (pro‐uPA) by the cysteine protease cathepsin L
Goretzki, L., Schmitt, M., Mann, K., Calvete, J. J., Chucholowski, N., Kramer, M. D., Günzler, W. A., Jänicke, F., & Graeff, H. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80339-i · Cited by 161
Cathepsin B in synovial cells at the site of joint destruction in rheumatoid arthritis
Trabandt, A., Gay, R. E., Fassbender, H., & Gay, S. (1991) · Arthritis & Rheumatism · doi:10.1002/art.1780341116 · Cited by 160
The Role of Cysteine Cathepsins in Cancer Progression and Drug Resistance
Rudzińska, M., Parodi, A., Soond, S. M., Винаров, А. З., Korolev, D. O., Morozov, A., Dağlıoğlu, C., Tutar, Y., & Zamyatnin, A. A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20143602 · Cited by 155
Molecular Regulation of Human Cathepsin B: Implication in Pathologies
Yan, S., & Sloane, B. F. (2003) · Biological Chemistry · doi:10.1515/bc.2003.095 · Cited by 153
Expression of Rat Cathepsin S in Phagocytic Cells
Petanceska, S. S., Canoll, P., & Devi, L. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4403 · Cited by 151
Exocytosis of active cathepsin B
Linebaugh, B. E., Sameni, M., Day, N. A., Sloane, B. F., & Keppler, D. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00582.x · Cited by 147
Expression of the Collagenolytic and Ras-Induced Cysteine Proteinase Cathepsin L and Proliferation-Associated Oncogenes in Synovial Cells of MRL/I Mice and Patients with Rheumatoid Arthritis
Trabandt, A., Aicher, W. K., Gay, R. E., Sukhatme, V. P., Nilson-Hamilton, M., Hamilton, R. T., McGhee, J. R., Fassbender, H. G., & Gay, S. (1990) · Matrix · doi:10.1016/s0934-8832(11)80142-3 · Cited by 142
Nutritive values, flavor amino acids, healthcare fatty acids and flesh quality improved by manganese referring to up-regulating the antioxidant capacity and signaling molecules TOR and Nrf2 in the muscle of fish
Jiang, W., Wu, P., Tang, R.-J., Liu, Y., Kuang, S., Jiang, J., Tang, L. Y., Tang, W., Zhang, Y., Zhou, X., et al. (2016) · Food Research International · doi:10.1016/j.foodres.2016.09.020 · Cited by 124
The pathobiology of osteoarthritis and the rationale for the use of pentosan polysulfate for its treatment
Ghosh, P. B. (1999) · Seminars in Arthritis and Rheumatism · doi:10.1016/s0049-0172(99)80021-3 · Cited by 125
Aberrant cancer metabolism in epithelial–mesenchymal transition and cancer metastasis: Mechanisms in cancer progression
Huang, R., & Zong, X. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.04.005 · Cited by 117
Human tumour cathepsin B. Comparison with normal liver cathepsin B
Moin, K., Day, N. A., Sameni, M., Hasnain, S., Hirama, T., & Sloane, B. F. (1992) · Biochemical Journal · doi:10.1042/bj2850427 · Cited by 113
Cathepsin B aggravates coxsackievirus B3-induced myocarditis through activating the inflammasome and promoting pyroptosis
Wang, Y., Jia, L., Shen, J. H., Wang, Y., Fu, Z., Su, S., Cai, Z., Wang, J.-A., & Xiang, M. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1006872 · Cited by 106
Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells.
Lemaire, R., Huet, G., Zerimech, F., Grard, G., Fontaine, C., Duquesnoy, B., & Flipo, R. (1997) · Lara D. Veeken · doi:10.1093/rheumatology/36.7.735 · Cited by 98
Dietary nucleotides supplementation affect the physicochemical properties, amino acid and fatty acid constituents, apoptosis and antioxidant mechanisms in grass carp (Ctenopharyngodon idellus) muscle
Tie, H., Wu, P., Jiang, W., Liu, Y., Kuang, S., Zeng, Y.-Y., Jiang, J., Tang, L. Y., Zhou, X., & Feng, L. (2018) · Aquaculture · doi:10.1016/j.aquaculture.2018.12.045 · Cited by 96
Cathepsin B Gene Knockout Improves Behavioral Deficits and Reduces Pathology in Models of Neurologic Disorders
Hook, G., Reinheckel, T., Ni, J., Wu, Z., Kindy, M. S., Peters, C., & HOOK, V. Y. H. (2022) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000527 · Cited by 98
Epigenetic Silencing of the Tumor Suppressor Cystatin M Occurs during Breast Cancer Progression
Ai, L., Kim, W.-J., Kim, T., Fields, C. R., Massoll, N. A., Robertson, K. D., & Brown, K. D. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0576 · Cited by 90
Comparative Localization of Cathepsin B Protein and Activity in Colorectal Cancer
Hazen, L. G. M., Bleeker, F. E., Lauritzen, B., Bahns, S., Song, J., Jonker, A., Driel, B. E. M. V., Lyon, H., Hansen, U., Köhler, A., et al. (2000) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215540004801012 · Cited by 90
Up regulation of cathepsin K expression in articular chondrocytes in a transgenic mouse model for osteoarthritis
Morko, J. P., Söderström, M., Säämänen, A.-M. K., Salminen, H. J., & Vuorio, E. I. (2004) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2002.004671 · Cited by 89
Sequence analysis, tissue distribution, and expression of rat cathepsin S.
Petanceska, S. S., & Devi, L. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35713-2 · Cited by 89
Detection of Multiple Autoantibodies in Patients with Ankylosing Spondylitis Using Nucleic Acid Programmable Protein Arrays
Wright, C., Sibani, S., Trudgian, D. C., Fischer, R., Kessler, B. M., LaBaer, J., & Bowness, P. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m9.00384 · Cited by 81
Cystatin M suppresses the malignant phenotype of human MDA-MB-435S cells
Shridhar, R., Zhang, J., Jin, S., Booth, B. A., Kevil, C. G., Sotiropoulou, G., Sloane, B. F., & Keppler, D. (2003) · Oncogene · doi:10.1038/sj.onc.1207340 · Cited by 77
Role of Cysteine Cathepsins in Extracellular Proteolysis
Brömme, D., & Wilson, S. C. (2011) · Springer eBooks · doi:10.1007/978-3-642-16861-1_2 · Cited by 75
Cathepsin L‐deficient mice exhibit abnormal skin and bone development and show increased resistance to osteoporosis following ovariectomy
Potts, W., Bowyer, J., Jones, H. B., Tucker, D. L., Freemont, A. J., Millest, A. J., Martin, C., Vernon, W., Neerunjun, D., Slynn, G., et al. (2004) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2004.00373.x · Cited by 75
Self-citation
The type II collagen fragments Helix-II and CTX-II reveal different enzymatic pathways of human cartilage collagen degradation
Tabassi, N. C.-B., Desmarais, S., Bay‐Jensen, A., Delaissé, J., Percival, M. D., & Garnero, P. (2008) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2008.02.008 · Cited by 73
Quantification of protease activities in synovial fluid from rheumatoid and osteoarthritis cases: comparison with antioxidant and free radical damage markers
Mantle, D., Falkous, G., & Walker, D. (1999) · Clinica Chimica Acta · doi:10.1016/s0009-8981(99)00055-8 · Cited by 72
The Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian Cancer
Pranjol, M. Z. I., Gutowski, N. J., Hannemann, M. M., & Whatmore, J. L. (2015) · Biomolecules · doi:10.3390/biom5043260 · Cited by 71
The Role of Phagocyte Proteinases and Proteinase Inhibitors in Multiple Organ Failure
Jochum, M., Gippner‐Steppert, C., Machleidt, W., & Fritz, H. (1994) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/ajrccm/150.6_pt_2.s123 · Cited by 69
Matrix Metalloproteinase Dependent and Independent Collagen Degradation
Song, F. (2006) · Frontiers in bioscience · doi:10.2741/2036 · Cited by 67
Selective Neutral pH Inhibitor of Cathepsin B Designed Based on Cleavage Preferences at Cytosolic and Lysosomal pH Conditions
Yoon, M. C., Solania, A., Jiang, Z., Christy, M. P., Podvin, S., Mosier, C., Lietz, C. B., Ito, G., Gerwick, W. H., Wolan, D. W., et al. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00138 · Cited by 67
Dipeptidyl nitrile inhibitors of Cathepsin L
Asaad, N., Bethel, P. A., Coulson, M., Dawson, J. E., Ford, S. J., Gerhardt, S., Grist, M., Hamlin, G. A., James, M. J., Jones, E. V., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.05.071 · Cited by 66
Identification of Key Genes and Pathways in Cervical Cancer by Bioinformatics Analysis
Wu, X., Peng, L., Zhang, Y., Chen, S., Lei, Q., Li, G., & Zhang, C. (2019) · International Journal of Medical Sciences · doi:10.7150/ijms.34172 · Cited by 66
Detecting cathepsin activity in human osteoarthritis via activity-based probes
Ben-Aderet, L., Merquiol, E., Fahham, D., Kumar, A., Reich, E., Ben‐Nun, Y., Kandel, L., Haze, A., Liebergall, M., Kosinska, M. K., et al. (2015) · Arthritis Research & Therapy · doi:10.1186/s13075-015-0586-5 · Cited by 65
Detection of collagenase-induced damage of collagen by 9A4, a monoclonal C-terminal neoepitope antibody
Otterness, I. G., Downs, J. T., Lane, C. L., Bliven, M. L., Stukenbrok, H., Scampoli, D. N., Milici, A. J., & Mézeš, P. (1999) · Matrix Biology · doi:10.1016/s0945-053x(99)00026-8 · Cited by 65
Cyclic AMP-dependent protein kinase activation of cystic fibrosis transmembrane conductance regulator chloride channels in planar lipid bilayers.
Tilly, B. C., Winter, M. C., Ostedgaard, L. S., O’Riordan, C. R., Smith, A. E., & Welsh, M. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50113-2 · Cited by 61
Bone Disease in Rheumatological Disorders
Goldring, S. R., & Polisson, R. P. (1998) · Elsevier eBooks · doi:10.1016/b978-012068700-8/50022-0 · Cited by 58
Stimulation of the secretion of latent cysteine proteinase activity by tumor necrosis factor α and interleukin‐1
Huet, G., Flipo, R., Colin, C., Janin, A., Hémon, B., Collyn-d'Hooghe, M., Lafyatis, R., Duquesnoy, B., & Degand, P. (1993) · Arthritis & Rheumatism · doi:10.1002/art.1780360606 · Cited by 57
Targeting cathepsin L (CL) by specific ribozymes decreases CL protein synthesis and cartilage destruction in rheumatoid arthritis
Schedel, J., Seemayer, C. A., Pap, T., Neidhart, M., Kuchen, S., Michel, B. A., Gay, R. E., Müller‐Ladner, U., Gay, S., & Zacharias, W. (2004) · Gene Therapy · doi:10.1038/sj.gt.3302265 · Cited by 57
Characterisation of fibroblast-like cells in pannus lesions of patients with rheumatoid arthritis sharing properties of fibroblasts and chondrocytes
Xue, C., Takahashi, M., Hasunuma, T., Aono, H., Yamamoto, K., Yoshino, S., Sumida, T., & Nishioka, K. (1997) · Annals of the Rheumatic Diseases · doi:10.1136/ard.56.4.262 · Cited by 56
Synthesis and optimization of hyaluronic acid–methotrexate conjugates to maximize benefit in the treatment of osteoarthritis
Homma, A., Sato, H., Tamura, T., Okamachi, A., Emura, T., Ishizawa, T., Kato, T., Matsuura, T., Sato, S., Higuchi, Y., et al. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.12.053 · Cited by 53
Characterization of Type XI Collagen-Glycosaminoglycan Interactions
Vaughan‐Thomas, A., Young, R. D., Phillips, A. C., & Duance, V. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008764200 · Cited by 53
Self-citation
Localization of Cathepsins D, K, and L in Degenerated Human Intervertebral Discs
Ariga, K., Yonenobu, K., Nakase, T., Kaneko, M., Okuda, S., Uchiyama, Y., & Yoshikawa, H. (2001) · Spine · doi:10.1097/00007632-200112150-00007 · Cited by 52
Cathepsin B: Basis Sequence: Mouse.
Cavallo‐Medved, D., Moin, K., & Sloane, B. F. (2011) · PubMed · Cited by 51
Peptidyl fluoromethyl ketones as inhibitors of cathepsin B
Ahmed, N. K., Martin, L. A., Watts, L. M., Palmer, J. T., Thornburg, L. P., Prior, J. J., & Esser, R. E. (1992) · Biochemical Pharmacology · doi:10.1016/0006-2952(92)90385-v · Cited by 51
Cathepsin B: The dawn of tumor therapy
Liu, F., Zhou, T., Zhang, S., Li, Y., Chen, Y., Miao, Z., Wang, X., Yang, G., Liu, Y., Zhang, L., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116329 · Cited by 50
Macrophage cathepsin L, a factor in the erosion of subchondral bone in rheumatoid arthritis
Iwata, Y., Mort, J. S., 立石, 博., & Lee, E. R. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400316 · Cited by 50
Extracellular-matrix degradation at acid pH. Avian osteoclast acid collagenase isolation and characterization
Blair, H. C., Teitelbaum, S. L., Grosso, L. E., Lacey, D. L., Tan, H., McCourt, D. W., & Jeffrey, J. J. (1993) · Biochemical Journal · doi:10.1042/bj2900873 · Cited by 50
Cathepsins B and L in synovial fluids from patients with rheumatoid arthritis and the effect of cathepsin B on the activation of pro-urokinase.
Ikeda, Y., Ikata, T., Mishiro, T., Nakano, S., Ikebe, M., & Yasuoka, S. (2000) · PubMed · Cited by 49
Oncogene activation in rheumatoid synovium
Trabandt, A., Gay, R. E., & Gay, S. (1992) · Apmis · doi:10.1111/j.1699-0463.1992.tb04012.x · Cited by 49
Methylation-dependent silencing of CST6 in primary human breast tumors and metastatic lesions
Rivenbark, A. G., Livasy, C., Boyd, C., Keppler, D., & Coleman, W. B. (2007) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2007.03.008 · Cited by 46
Complete degradation of type X collagen requires the combined action of interstitial collagenase and osteoclast-derived cathepsin-B.
Sires, U. I., Schmid, T. M., Fliszar, C. J., Wang, Z. Q., Gluck, S. L., & Welgus, H. G. (1995) · Journal of Clinical Investigation · doi:10.1172/jci117896 · Cited by 46
Identification and characterization of a novel human cathepsin L splice variant
Arora, S., & Chauhan, S. S. (2002) · Gene · doi:10.1016/s0378-1119(02)00700-x · Cited by 44
Evidence for Cross‐Talk Between Sertoli and Germ Cells Using Selected Cathepsins as Markers
Chung, S. S. W., Zhu, L.-J., Mo, M., Silvestrini, B., Lee, W. M., & Cheng, C. Y. (1998) · Journal of Andrology · doi:10.1002/j.1939-4640.1998.tb02078.x · Cited by 43
The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: a 2‐year longitudinal study
Eley, B. M., & Cox, S. W. (1996) · Journal of Periodontal Research · doi:10.1111/j.1600-0765.1996.tb00507.x · Cited by 39
Cathepsin B Dipeptidyl Carboxypeptidase and Endopeptidase Activities Demonstrated across a Broad pH Range
Yoon, M. C., HOOK, V. Y. H., & O’Donoghue, A. J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00358 · Cited by 39
Cysteine and serine proteases of synovial tissue in rheumatoid arthritis and osteoarthritis
Solau‐Gervais, E., Zerimech, F., Lemaire, R., Fontaine, C., Huet, G., & Flipo, R. (2007) · Scandinavian Journal of Rheumatology · doi:10.1080/03009740701340172 · Cited by 36
Enhancement of flavor and healthcare substances, mouthfeel parameters and collagen synthesis in the muscle of on-growing grass carp (Ctenopharyngodon idella) fed with graded levels of glutamine
Ma, X., Feng, L., Wu, P., Liu, Y., Kuang, S., Tang, L. Y., Zhou, X., & Jiang, W. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735486 · Cited by 36
Cathepsin B in Osteoarthritis: Uncontrolled Proteolysis in the Wrong Place
Baici, A., Lang, A., Zwicky, R., & Müntener, K. (2004) · Seminars in Arthritis and Rheumatism · doi:10.1016/j.semarthrit.2004.03.008 · Cited by 36
Guanidinoacetic acid supplementation totally based on vegetable meal diet improved the growth performance, muscle flavor components and sensory characteristics of on-growing grass carp (Ctenopharygodon idella)
Yang, L.-L., Wu, P., Feng, L., Jiang, W., Liu, Y., Kuang, S., Tang, L., & Zhou, X. (2020) · Aquaculture · doi:10.1016/j.aquaculture.2020.735841 · Cited by 34
Synthesis and biochemical evaluation of benzoylbenzophenone thiosemicarbazone analogues as potent and selective inhibitors of cathepsin L
Parker, E. N., Song, J.-L., Kumar, G. D. K., Odutola, S. O., Chavarria, G. E., Charlton-Sevcik, A. K., Strecker, T. E., Barnes, A. L., Sudhan, D. R., Wittenborn, T. R., et al. (2015) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2015.09.036 · Cited by 33
Upregulation of distinct collagen transcripts in post-surgery scar tissue: a study of conjunctival fibrosis
Seet, L., Toh, L. Z., Chu, S. W. L., Finger, S. N., Chua, J., & Wong, T. T. L. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.028555 · Cited by 31
Expression of cathepsins B, D and L in mouse corneas infected withPseudomonas aeruginosa
Dong, Z., Katar, M., Linebaugh, B. E., Sloane, B. F., & Berk, R. S. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02607.x · Cited by 33
Cathepsin L in metastatic bone disease: therapeutic implications
Leto, G., Sepporta, M. V., Crescimanno, M., Flandina, C., & Tumminello, F. M. (2010) · Biological Chemistry · doi:10.1515/bc.2010.069 · Cited by 32
Cathepsin B activity in normal human osteoblast-like cells and human osteoblastic osteosarcoma cells (MG-63) : regulation by interleukin-1 β and parathyroid hormone
Aisa, M. C. (1996) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(95)00182-4 · Cited by 31
Temporal pattern of cysteine endopeptidase (cathepsin B) expression in cartilage and synovium from rabbit knees with experimental osteoarthritis: gene expression in chondrocytes in response to interleukin-1 and matrix depletion
Mehraban, F., Tindal, M. H., Proffitt, M., & Moskowitz, R. W. (1997) · Annals of the Rheumatic Diseases · doi:10.1136/ard.56.2.108 · Cited by 29
Proteolytic Enzymes in Inflammatory Bowel Disease
MacDonald, T. T., & Pender, S. L. F. (1998) · Inflammatory Bowel Diseases · doi:10.1002/ibd.3780040211 · Cited by 29
DO NONIMMUNOLOGICALLY MEDIATED PATHWAYS PLAY A ROLE IN THE PATHOGENESIS OF RHEUMATOID ARTHRITIS?
Koopman, W. J., & Gay, S. (1993) · Rheumatic Disease Clinics of North America · doi:10.1016/s0889-857x(21)00170-8 · Cited by 29
Variation patterns of two degradation enzyme systems in articular cartilage in different stages of osteoarthritis: Regulation by dehydroepiandrosterone
Bao, J., Chen, W., Feng, J., Zhao, J., Shi, Z., Huang, K., & Wu, L. (2009) · Clinica Chimica Acta · doi:10.1016/j.cca.2009.06.040 · Cited by 28
Cysteine proteinases in arthritis and inflammation
Müller‐Ladner, U., Gay, R. E., & Gay, S. (1996) · Perspectives in Drug Discovery and Design · doi:10.1007/bf02174047 · Cited by 28
Expression ofHoxa-1 andHoxb-7 is regulated by extracellular matrix-dependent signals in mammary epithelial cells
Srebrow, A., Friedmann, Y., Ravanpay, A. C., Daniel, C. W., & Bissell, M. J. (1998) · Journal of Cellular Biochemistry · doi:10.1002/(sici)1097-4644(19980615)69:4 · Cited by 54
Monoclonal Antibodies Against Cathepsin L and Procathepsin L of Different Species
Weber, E., Bahn, H., & GÜNTHER, D. (1997) · Hybridoma · doi:10.1089/hyb.1997.16.159 · Cited by 27
Aziridine‐2,3‐dicarboxylic Acid Derivatives as Inhibitors of Papain
Schirmeister, T. (1996) · Archiv der Pharmazie · doi:10.1002/ardp.19963290504 · Cited by 24
Regulation of Collagenolytic Protease Secretion through c-Src in Osteoclasts
Furuyama, N., & Fujisawa, Y. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2698 · Cited by 24
Immunolocalization of cathepsin B in equinedyschondroplastic articular cartilage
Hernández-Vidal, G., Jeffcott, L. B., & Davies, M. (1998) · The Veterinary Journal · doi:10.1016/s1090-0233(98)80122-6 · Cited by 22
The application of scanning confocal microscopy in cartilage research
Wotton, S. F., Jeacocke, R. E., Maciewicz, R. A., Wardale, R. J., & Duance, V. C. (1991) · The Histochemical Journal · doi:10.1007/bf01044964 · Cited by 22
Self-citation
Cathepsin L plays an active role in involution of the mouse mammary gland
Burke, M. A., Hutter, D., Reshamwala, R. P., & Knepper, J. E. (2003) · Developmental Dynamics · doi:10.1002/dvdy.10313 · Cited by 21
Alternative splicing of the 5′ region of cathepsin B pre‐messenger RNA in rheumatoid synovial tissue
Lemaire, R., Flipo, R., Migаud, H., Fontaine, C., Huet, G., Dacquembronne, E., & Lafyatis, R. (1997) · Arthritis & Rheumatism · doi:10.1002/art.1780400824 · Cited by 21
Long-Lasting Tissue Inflammatory Processes Trigger Autoimmune Responses to Extracellular Matrix Molecules
Bei, R., Masuelli, L., Palumbo, C., Tresoldi, I., Scardino, A., & Modesti, A. (2008) · International Reviews of Immunology · doi:10.1080/08830180801939280 · Cited by 20
Cathepsin B in gingival crevicular fluid of adult periodontitis patients: Identification by immunological and enzymological methods
市丸, 英., Tanoue, M., Tani, M., Tani, Y., Kaneko, T., Iwasaki, Y., Kunimatsu, K., & Kato, I. (1996) · Inflammation Research · doi:10.1007/bf02280991 · Cited by 20
Selective increased presentation of type II collagen by leupeptin
Manoury, B. (1997) · International Immunology · doi:10.1093/intimm/9.4.581 · Cited by 20
Modification of the Composition of Articular Cartilage Collagen Fibrils with Increasing Age
Vaughan‐Thomas, A., Dudhia, J., Bayliss, M. T., Kadler, K. E., & Duance, V. C. (2008) · Connective Tissue Research · doi:10.1080/03008200802325417 · Cited by 17
Self-citation
Cathepsin L Induces Proangiogenic Changes in Human Omental Microvascular Endothelial Cells via Activation of the ERK1/2 Pathway
Pranjol, M. Z. I., Gutowski, N. J., Hannemann, M. M., & Whatmore, J. L. (2018) · Current Cancer Drug Targets · doi:10.2174/1568009618666180831123951 · Cited by 16

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
DOI: 10.1016/0014-5793(90)81151-d
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
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 4109 d)
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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks