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MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1
Open accessAbstract
Matrix metalloproteinase 13 (MMP-13) degrades collagenous extracellular matrix and its aberrant activity associates with diseases such as arthritis, cancer, atherosclerosis and fibrosis. The wide range of MMP-13 proteolytic capacity suggests that it is a powerful, potentially destructive proteinase and thus it has been believed that MMP-13 is not produced in most adult human tissues in the steady state. Present study has revealed that human chondrocytes isolated from healthy adults constitutively express and secrete MMP-13, but that it is rapidly endocytosed and degraded by chondrocytes. Both pro- and activated MMP-13 bind to clusters II and III of low-density lipoprotein (LDL) receptor-related protein 1 (LRP1). Domain deletion studies indicated that the hemopexin domain is responsible for this interaction. Binding competition between MMP-13 and ADAMTS-4, -5 or TIMP-3, which also bind to cluster II, further shown that the MMP-13 binding site within cluster II is different from those of ADAMTS-4, -5 or TIMP-3. MMP-13 is therefore co-endocytosed with ADAMTS-5 and TIMP-3 by human chondrocytes. These findings indicate that MMP-13 may play a role on physiological turnover of cartilage extracellular matrix and that LRP1 is a key modulator of extracellular levels of MMP-13 and its internalization is independent of the levels of ADAMTS-4, -5 and TIMP-3.
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Cites
Little, C. B., Barai, A., Burkhardt, D., Smith, S. M., Fosang, A. J., Werb, Z., Shah, M., & Thompson, E. W. (2009) · Arthritis & Rheumatism · doi:10.1002/art.25002 · Cited by 642
Wells, J. M., Gaggar, A., & Blalock, J. E. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.016 · Cited by 263
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Bassiouni, W., Ali, M. A. M., & Schulz, R. (2021) · The FEBS Journal · doi:10.1111/febs.15701 · Cited by 377
New insights on the MMP-13 regulatory network in the pathogenesis of early osteoarthritis
Li, H., Wang, D., Yuan, Y., & Min, J. (2017) · Arthritis Research & Therapy · doi:10.1186/s13075-017-1454-2 · Cited by 293
Matrix metalloproteinase collagenolysis in health and disease
Amar, S., Smith, L., & Fields, G. B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.04.015 · Cited by 194
Regulation and Function of Matrix Metalloproteinase-13 in Cancer Progression and Metastasis
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Novel insights into the multifaceted and tissue‐specific roles of the endocytic receptor LRP1
Yamamoto, K., Scilabra, S. D., Bonelli, S., Jensen, A., Scavenius, C., Enghild, J. J., & Strickland, D. K. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107521 · Cited by 47
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Metadata
- Authors
- Yamamoto, K., Okano, H., Miyagawa, W., Visse, R., Shitomi, Y., Santamaria, S., Dudhia, J., Troeberg, L., Strickland, D. K., Hirohata, S., & Nagase, H.
- Venue
- Matrix Biology
- Publisher
- Elsevier BV
- Published
- 2016-12
- Volume
- 56
- Pages
- 57-73
- ISSN
- 0945-053X (ISSN-L)
- OpenAlex
- W2340570226
- Cited by
- 180
- References
- 2
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Yamamoto, K., Okano, H., Miyagawa, W., Visse, R., Shitomi, Y., Santamaria, S., Dudhia, J., Troeberg, L., Strickland, D. K., Hirohata, S., & Nagase, H. (2016). MMP-13 is constitutively produced in human chondrocytes and co-endocytosed with ADAMTS-5 and TIMP-3 by the endocytic receptor LRP1. Matrix Biology. https://doi.org/10.1016/j.matbio.2016.03.007
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