The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Osteopontin, a Novel Substrate for Matrix Metalloproteinase-3 (Stromelysin-1) and Matrix Metalloproteinase-7 (Matrilysin)
Open accessAbstract
Osteopontin (OPN) is a secreted phosphoprotein shown to function in wound healing, inflammation, and tumor progression. Expression of OPN is often co-localized with members of the matrix metalloproteinase (MMP) family. We report that OPN is a novel substrate for two MMPs, MMP-3 (stromelysin-1) and MMP-7 (matrilysin). Three cleavage sites were identified for MMP-3 in human OPN, and two of those sites were also cleaved by MMP-7. These include hydrolysis of the human Gly166-Leu167, Ala201-Tyr202 (MMP-3 only), and Asp210-Leu211 peptide bonds. Only the N-terminal Gly-Leu cleavage site is conserved in rat OPN (Gly151-Leu152). These sites are distinct from previously reported cleavage sites in OPN for the proteases thrombin or enterokinase. We found evidence for the predicted MMP cleavage fragments of OPN in vitro in tumor cell lines, and in vivo in remodeling tissues such as the postpartum uterus, where OPN and MMPs are co-expressed. Furthermore, cleavage of OPN by MMP-3 or MMP-7 potentiated the function of OPN as an adhesive and migratory stimulus in vitro through cell surface integrins. We predict that interaction of MMPs with OPN at tumor and wound healing sites in vivo may be a mechanism of regulation of OPN bioactivity.
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Cites
Matrix Metalloproteinases: Biologic Activity and Clinical Implications
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Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5
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Eta-1 (Osteopontin): An Early Component of Type-1 (Cell-Mediated) Immunity
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Self-citationMatrix metalloproteinases: multifunctional contributors to tumor progression
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Cited by
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Matricellular proteins: extracellular modulators of cell function
Bornstein, P., & Sage, E. H. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00361-7 · Cited by 965
Matrix Metalloproteinases as Modulators of Inflammation
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The extracellular matrix in tumor progression and metastasis
Eble, J. A., & Niland, S. (2019) · Clinical & Experimental Metastasis · doi:10.1007/s10585-019-09966-1 · Cited by 613
Rodríguez, D., Morrison, C. J., & Overall, C. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.09.015 · Cited by 560
Metadata
- Authors
- Agnihotri, R., Crawford, H. C., Haro, H., Matrisian, L. M., Havrda, M. C., & Liaw, L.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-07
- Volume
- 276
- Issue
- 30
- Pages
- 28261-28267
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2167677178
- Cited by
- 414
- References
- 42
- FWCI
- 10.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Agnihotri, R., Crawford, H. C., Haro, H., Matrisian, L. M., Havrda, M. C., & Liaw, L. (2001). Osteopontin, a Novel Substrate for Matrix Metalloproteinase-3 (Stromelysin-1) and Matrix Metalloproteinase-7 (Matrilysin). Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m103608200
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