The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-β 1 release
Open accessAbstract
Decorin (DCN) is a ubiquitous proteoglycan comprised of a core protein attached to a single dermatan/chondroitin sulphate glycosaminoglycan chain. It may play a role in regulation of collagen fibrillogenesis and function as a reservoir of transforming growth factor β(TGF-β) in the extracellular milieu. We have examined the susceptibility of DCN to five different matrix metalloproteinases (MMPs): MMP-1 (tissue collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin 1), MMP-7 (matrilysin) and MMP-9 (gelatinase B). MMP-2 and MMP-3 digest DCN into seven major fragments in a similar pattern. The N-terminal sequence of the two fragments generated by MMP-2 and MMP-3 is Leu211-Lys-Gly-Leu-Asn, but that of the others is Asp1-Glu-Ala-Ser-Gly. MMP-7 cleaves DCN into three major fragments which have the N-termini Asp1-Glu-Ala-Ser-Gly, Glu2-Ala-Ser-Gly-Ile and Leu244-His-Leu-Asp-Asn. Activities of MMP-1 and MMP-9 against DCN are negligible. The values of Km for the MMPs capable of degrading DCN are very similar (10–12 μM), but the kcat/Km value for MMP-7 (30.5 μM-1·h-1) is 4.5-fold higher than those for MMP-2 and MMP-3. Incubation of a DCN–TGF-β1 complex with MMP-2, -3 or -7 results in release of TGF-β1 from the complex. These data indicate proteolytic degradation of DCN by MMP-2, MMP-3 and MMP-7, and suggest the possibility that, under pathophysiological conditions, the digestion by the MMPs may induce tissue reactions mediated by TGF-β1 released from DCN in the connective tissues.
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Cites
Negative regulation of transforming growth factor-β by the proteoglycan decorin
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Self-citationOkuda, S., Languino, L. R., Ruoslahti, E., & Border, W. A. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114731 · Cited by 546
Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA.
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Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
How Matrix Metalloproteinases Regulate Cell Behavior
Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959
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
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
Role of Extracellular Matrix in Development and Cancer Progression
Walker, C., Mojares, E., & Del Río Hernández, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103028 · Cited by 1,084
Metadata
- Authors
- IMAI, K., HIRAMATSU, A., FUKUSHIMA, D., PIERSCHBACHER, M. D., & OKADA, Y.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1997-03-15
- Volume
- 322
- Issue
- 3
- Pages
- 809-814
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W2224483385
- Cited by
- 445
- References
- 32
- FWCI
- 4.41
- Type
- journal article
- Language
- en
- Open access
- bronze
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- IMAI, K., HIRAMATSU, A., FUKUSHIMA, D., PIERSCHBACHER, M. D., & OKADA, Y. (1997). Degradation of decorin by matrix metalloproteinases: identification of the cleavage sites, kinetic analyses and transforming growth factor-β 1 release. Biochemical Journal. https://doi.org/10.1042/bj3220809
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