The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.
The role of TIMPs in regulation of extracellular matrix proteolysis
Open accessAbstract
Tissue inhibitors of metalloproteinases (TIMPs), which inhibit matrix metalloproteinases (MMPs) as well as the closely related, a disintegrin and metalloproteinases (ADAMs) and ADAMs with thrombospondin motifs (ADAMTSs), were traditionally thought to control extracellular matrix (ECM) proteolysis through direct inhibition of MMP-dependent ECM proteolysis. This classical role for TIMPs suggests that increased TIMP levels results in ECM accumulation (or fibrosis), whereas loss of TIMPs leads to enhanced matrix proteolysis. Mice lacking TIMP family members have provided support for such a role; however, studies with these TIMP deficient mice have also demonstrated that loss of TIMPs can often be associated with an accumulation of ECM. Collectively, these studies suggest that the divergent roles of TIMPs in matrix accumulation and proteolysis, which together can be referred to as ECM turnover, are dependent on the TIMP, specific tissue, and local tissue environment (i.e. health vs. injury/disease). Ultimately, these combined factors dictate the specific metalloproteinases being regulated by a given TIMP, and it is likely the diversity of metalloproteinases and their physiological substrates that determines whether TIMPs inhibit matrix proteolysis or accumulation. In this review, we discuss the evidence for the dichotomous roles of TIMPs in ECM turnover highlighting some of the common findings between different TIMP family members. Importantly, while we now have a better understanding of the role of TIMPs in regulating ECM turnover, much remains to be determined. Data on the specific metalloproteinases inhibited by different TIMPs in vivo remains limited and must be the focus of future studies.
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
1 retracted
Pang, H., Han, B., Yu, T., & Peng, Z. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092216 · Cited by 45
RetractedMatrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929
Tissue inhibitors of metalloproteinases: evolution, structure and function
Brew, K., Dinakarpandian, D., & Nagase, H. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00279-4 · Cited by 1,908
Matrix metalloproteinases: they're not just for matrix anymore!
McCawley, L. J., & Matrisian, L. M. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00248-9 · Cited by 1,274
Metalloproteinase inhibitors: biological actions and therapeutic opportunities
Baker, A. H., Edwards, D. R., & Murphy, G. (2002) · Journal of Cell Science · doi:10.1242/jcs.00063 · Cited by 1,179
Qi, J. H., Ebrahem, Q., Moore, N., Murphy, G., Claesson-Welsh, L., Bond, M., Baker, A., & Anand-Apte, B. (2003) · Nature Medicine · doi:10.1038/nm846 · Cited by 658
TNF‐α converting enzyme (TACE) is inhibited by TIMP‐3
Amour, A., Slocombe, P. M., Webster, A., Butler, M., Knight, C. G., Smith, B. J., Stephens, P. E., Shelley, C., Hutton, M., Knäuper, V., et al. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01031-x · Cited by 609
Metalloproteinases and their natural inhibitors in inflammation and immunity
Khokha, R., Murthy, A., & Weiss, A. (2013) · Nature reviews. Immunology · doi:10.1038/nri3499 · Cited by 552
TIMP-3 Is a Potent Inhibitor of Aggrecanase 1 (ADAM-TS4) and Aggrecanase 2 (ADAM-TS5)
Kashiwagi, M., Tortorella, M., Nagase, H., & Brew, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000848200 · Cited by 509
Leco, K. J., Khokha, R., Pavloff, N., Hawkes, S. P., & Edwards, D. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37115-6 · Cited by 480
Cited by
The Roles of Matrix Metalloproteinases and Their Inhibitors in Human Diseases
Cabral-Pacheco, G. A., Garza-Veloz, I., Castruita-De la Rosa, C., Ramirez-Acuña, J. M., Perez-Romero, B. A., Guerrero-Rodriguez, J. F., Martinez-Avila, N., & Martinez-Fierro, M. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249739 · Cited by 1,820
Proteoglycan Chemical Diversity Drives Multifunctional Cell Regulation and Therapeutics
Karamanos, N. K., Piperigkou, Z., Theocharis, A. D., Watanabe, H., Franchi, M., Baud, S., Brézillon, S., Götte, M., Passi, A., Vigetti, D., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00354 · Cited by 367
Perineuronal Nets in the Adult Sensory Cortex Are Necessary for Fear Learning
Banerjee, S. B., Gutzeit, V. A., Baman, J., Aoued, H. S., Doshi, N. K., Liu, R. C., & Ressler, K. J. (2017) · Neuron · doi:10.1016/j.neuron.2017.06.007 · Cited by 163
Shaping Synapses by the Neural Extracellular Matrix
Ferrer-Ferrer, M., & Dityatev, A. (2018) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2018.00040 · Cited by 169
PI4KIIIβ is a therapeutic target in chromosome 1q–amplified lung adenocarcinoma
Tan, X., Banerjee, P., Pham, E. A., Rutaganira, F. U. N., Basu, K., Bota-Rabassedas, N., Guo, H.-F., Grzeskowiak, C. L., Liu, X., Yu, J., et al. (2020) · Science Translational Medicine · doi:10.1126/scitranslmed.aax3772 · Cited by 70
Metadata
- Authors
- Arpino, V., Brock, M., & Gill, S. E.
- Venue
- Matrix Biology
- Publisher
- Elsevier BV
- Published
- 2015-05
- Volume
- 44-46
- Pages
- 247-254
- ISSN
- 0945-053X (ISSN-L)
- OpenAlex
- W2036322339
- Cited by
- 734
- References
- 66
- FWCI
- 15.01
- Type
- journal article
- Language
- en
- Open access
- hybrid
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: The role of TIMPs in regulation of extracellular matrix proteolysis. https://app.cochat.ai/papers/10.1016/j.matbio.2015.03.005
- The paper
- Arpino, V., Brock, M., & Gill, S. E. (2015). The role of TIMPs in regulation of extracellular matrix proteolysis. Matrix Biology. https://doi.org/10.1016/j.matbio.2015.03.005
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.
