The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Tissue Inhibitors of Metalloproteinases in Cell Signaling: Metalloproteinase-Independent Biological Activities
Open accessAbstract
Over the past 20 years, the tissue inhibitors of metalloproteinases (TIMPs) have been implicated in direct regulation of cell growth and apoptosis. However, the mechanisms of these effects have been controversial. Recent work by several laboratories has identified specific signaling pathways and cell surface binding partners for members of the TIMP family. TIMP-2 binding to the integrin α 3 β 1 is the first description of a cell surface receptor for a TIMP family member. TIMP-2 has been shown to induce gene expression, to promote G 1 cell cycle arrest, and to inhibit cell migration. TIMP-1 binding to CD63 inhibits cell growth and apoptosis. These new findings suggest that TIMPs are multifunctional and can act either directly through cell surface receptors or indirectly through modulation of protease activity to direct cell fate. The emerging concept is that TIMPs function in a contextual fashion so that the mechanism of action depends on the tissue microenvironment.
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Cites
New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
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
Novel functions of TIMPs in cell signaling
Chirco, R., Liu, X.-W., Jung, K.-K., & Kim, H.-R. C. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-7893-x · Cited by 401 · cited 2×
“In a similar fashion, it has been proposed that TIMP-1 function is also influenced by cellular context, specifically, in that MMPs, in particular MMP-9, may reduce the effective concentration of TIMP-1 and may compete with TIMP-1 for binding to the cell surface receptor CD63 (91).”
BackgroundTIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix
Yu, W.-H., Yu, S.-S. C., Meng, Q., Brew, K., & Woessner, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000907200 · Cited by 328
Baker, A. H., George, S. J., Zaltsman, A. B., Murphy, G., & Newby, A. C. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690217 · Cited by 286
RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity
Muraguchi, T., Takegami, Y., Ohtsuka, T., Kitajima, S., Chandana, E. P. S., Omura, A., Miki, T., Takahashi, R., Matsumoto, N., Ludwig, A., et al. (2007) · Nature Neuroscience · doi:10.1038/nn1922 · Cited by 149
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
Bourboulia, D., & Stetler-Stevenson, W. G. (2010) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2010.05.002 · Cited by 710
Self-citationMetzincin proteases and their inhibitors: foes or friends in nervous system physiology?
Rivera, S., Khrestchatisky, M., Kaczmarek, L., Rosenberg, G. A., & Jaworski, D. M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3467-10.2010 · Cited by 223
Nitric oxide synthase and breast cancer: role of TIMP-1 in NO-mediated Akt activation
Ridnour, L. A., Barasch, K. M., Windhausen, A. N., Dorsey, T. H., Lizardo, M. M., Yfantis, H. G., Lee, D. H., Switzer, C. H., Cheng, R. Y. S., Heinecke, J. L., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0044081 · Cited by 71
Bommarito, A., Richiusa, P., Carissimi, E., Pizzolanti, G., Rodolico, V., Zito, G., Criscimanna, A., Di Blasi, F., Pitrone, M., Zerilli, M., et al. (2011) · Endocrine Related Cancer · doi:10.1530/erc-11-0076 · Cited by 70
Metadata
- Authors
- Stetler-Stevenson, W. G.
- Venue
- Science Signaling
- Published
- 2008-07-08
- Volume
- 1
- Issue
- 27
- Pages
- re6-re6
- ISSN
- 1937-9145 (ISSN-L)
- 1945-0877
- OpenAlex
- W2097579313
- Cited by
- 489
- References
- 6
- FWCI
- 11.52
- Type
- journal article
- Language
- en
- Open access
- green
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