The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The in vitro activity of ADAM‐10 is inhibited by TIMP‐1 and TIMP‐3
Abstract
A recombinant soluble form of the catalytic domain of human ADAM‐10 was expressed as an Fc fusion protein from myeloma cells. The ADAM‐10 was catalytically active, cleaving myelin basic protein and peptides based on the previously described ‘metallosheddase’ cleavage sites of tumour necrosis factor α, CD40 ligand and amyloid precursor protein. The myelin basic protein degradation assay was used to demonstrate that hydroxamate inhibitors of matrix metalloproteinases (MMPs) were also inhibitors of ADAM‐10. The natural MMP inhibitors, TIMP‐2 and TIMP‐4 were unable to inhibit ADAM‐10, but TIMP‐1 and TIMP‐3 were inhibitory. Using a quenched fluorescent substrate assay and ADAM‐10 we obtained approximate apparent inhibition constants of 0.1 nM (TIMP‐1) and 0.9 nM (TIMP‐3). The TIMP‐1 inhibition of ADAM‐10 could therefore prove useful in distinguishing its activity from that of TACE, which is only inhibited by TIMP‐3, in cell based assays.
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Cites
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
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Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349
Metalloproteinases and their inhibitors: Regulators of wound healing
Gill, S. E., & Parks, W. C. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.024 · Cited by 742
Metalloproteinases and their natural inhibitors in inflammation and immunity
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Lichtenthaler, S. F., Haass, C., & Steiner, H. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07248.x · Cited by 205
The Metalloprotease Disintegrin ADAM8
Schlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C. G., Docherty, A. J. P., Lambert, M., Skelton, L., Jockusch, H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203355200 · Cited by 171
Self-citationRivera, S., García-González, L., Khrestchatisky, M., & Baranger, K. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03178-2 · Cited by 111
Zhou, X., Chen, Y., Mok, K. Y., Zhao, Q., Chen, K., Chen, Y., Hardy, J., Li, Y., Fu, A. K. Y., Guo, Q., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715554115 · Cited by 96
Hoe, H.-S., Cooper, M. J., Burns, M. P., Lewis, P. A., van der Brug, M., Chakraborty, G., Cartagena, C. M., Pak, D. T. S., Cookson, M. R., & Rebeck, G. W. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.3135-07.2007 · Cited by 90
The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.
Rapti, M., Atkinson, S. J., Lee, M.-H., Trim, A., Moss, M., & Murphy, G. (2008) · Biochemical Journal · doi:10.1042/bj20071430 · Cited by 43
Self-citationA microarray study to characterize the molecular mechanism of TIMP-3-mediated tumor rejection
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Metadata
- Authors
- Amour, A., Knight, C. G., Webster, A., Slocombe, P. M., Stephens, P. E., Knäuper, V., Docherty, A. J. P., & Murphy, G.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2000-05-12
- Volume
- 473
- Issue
- 3
- Pages
- 275-279
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2092863938
- Cited by
- 404
- References
- 1
- FWCI
- 8.28
- Type
- journal article
- Language
- en
- Open access
- closed
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