The DOI matches its Crossref record; 89 of the 89 references it cites were found in a registry or an index.
Cathepsin cysteine proteases in cardiovascular disease
Abstract
Extracellular matrix (ECM) remodeling is one of the underlying mechanisms in cardiovascular diseases. Cathepsin cysteine proteases have a central role in ECM remodeling and have been implicated in the development and progression of cardiovascular diseases. Cathepsins also show differential expression in various stages of atherosclerosis, and in vivo knockout studies revealed that deficiency of cathepsin K or S reduces atherosclerosis. Furthermore, cathepsins are involved in lipid metabolism. Cathepsins have the capability to degrade low‐density lipoprotein and reduce cholesterol efflux from macrophages, aggravating foam cell formation. Although expression studies also demonstrated differential expression of cathepsins in cardiovascular diseases like aneurysm formation, neoin‐tima formation, and neovascularization, in vivo studies to define the exact role of cathepsins in these processes are lacking. Evaluation of the feasibility of cathepsins as a diagnostic tool revealed that serum levels of cathepsins L and S seem to be promising as biomarkers in the diagnosis of atherosclerosis, whereas cathepsin B shows potential as an imaging tool. Furthermore, ca‐thepsin K and S inhibitors showed effectiveness in (pre) clinical evaluation for the treatment of osteoporosis and osteoarthritis, suggesting that cathepsin inhibitors may also have therapeutic effects for the treatment of atherosclerosis.—Lutgens, S. P. M., Cleutjens, K. B. J. M., Daemen, M. J. A. P., Heeneman, S. Cathepsin cysteine proteases in cardiovascular disease. FASEB J. 21, 3029–3041 (2007)
Overview
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
Cites
Statistics
Verification
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.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Isolation of Putative Progenitor Endothelial Cells for Angiogenesis
Asahara, T., Murohara, T., Sullivan, A., Silver, M., van der Zee, R., Li, T., Witzenbichler, B., Schatteman, G., & Isner, J. M. (1997) · Science · doi:10.1126/science.275.5302.964 · Cited by 8,725
Zarins, C. K., Giddens, D. P., Bharadvaj, B. K., Sottiurai, V. S., Mabon, R. F., & Glagov, S. (1983) · Circulation Research · doi:10.1161/01.res.53.4.502 · Cited by 1,485
Pycnodysostosis, a Lysosomal Disease Caused by Cathepsin K Deficiency
Gelb, B. D., Shi, G.-P., Chapman, H. A., & Desnick, R. J. (1996) · Science · doi:10.1126/science.273.5279.1236 · Cited by 1,029
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice
Saftig, P., Hunziker, E., Wehmeyer, O., Jones, S., Boyde, A., Rommerskirch, W., Moritz, J. D., Schu, P., & von Figura, K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13453 · Cited by 913
Lysosomal cysteine proteases: more than scavengers
Turk, B., Turk, D., & Turk, V. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00263-0 · Cited by 844
The cystatins: Protein inhibitors of cysteine proteinases
Turk, V., & Bode, W. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80804-c · Cited by 820
Newby, A. C. (2005) · Physiological Reviews · doi:10.1152/physrev.00048.2003 · Cited by 817
EMERGING ROLES FOR CYSTEINE PROTEASES IN HUMAN BIOLOGY
Chapman, H. A., Riese, R. J., & Shi, G.-P. (1997) · Annual Review of Physiology · doi:10.1146/annurev.physiol.59.1.63 · Cited by 786
NEW EMBO MEMBERS' REVIEW: Lysosomal cysteine proteases: facts and opportunities
Turk, V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4629 · Cited by 756
Sukhova, G. K., Shi, G. P., Simon, D. I., Chapman, H. A., & Libby, P. (1998) · Journal of Clinical Investigation · doi:10.1172/jci181 · Cited by 665
Cited by
Cysteine cathepsins: From structure, function and regulation to new frontiers
Turk, V., Stoka, V., Vasiljeva, O., Renko, M., Sun, T., Turk, B., & Turk, D. (2012) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.10.002 · Cited by 1,377
The lysosome: from waste bag to potential therapeutic target
Appelqvist, H., Wäster, P., Kågedal, K., & Öllinger, K. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt022 · Cited by 772
Cysteine cathepsin proteases: regulators of cancer progression and therapeutic response
Olson, O. C., & Joyce, J. A. (2015) · Nature Reviews Cancer · doi:10.1038/nrc4027 · Cited by 699
Specialized roles for cysteine cathepsins in health and disease
Reiser, J., Adair, B., & Reinheckel, T. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42918 · Cited by 580
Lysosomes as mediators of drug resistance in cancer
Zhitomirsky, B., & Assaraf, Y. G. (2016) · Drug Resistance Updates · doi:10.1016/j.drup.2015.11.004 · Cited by 482
Metadata
- Authors
- Lutgens, S. P. M., Cleutjens, K. B. J. M., Daemen, M. J. A. P., & Heeneman, S.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2007-05-23
- Volume
- 21
- Issue
- 12
- Pages
- 3029-3041
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2093932892
- Cited by
- 351
- References
- 89
- FWCI
- 6.64
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Cathepsin cysteine proteases in cardiovascular disease. https://app.cochat.ai/papers/10.1096/fj.06-7924com
- The paper
- Lutgens, S. P. M., Cleutjens, K. B. J. M., Daemen, M. J. A. P., & Heeneman, S. (2007). Cathepsin cysteine proteases in cardiovascular disease. The FASEB Journal. https://doi.org/10.1096/fj.06-7924com
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.