The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Cell–matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca2+ influx and PKC activation
Open accessAbstract
CD44 is an adhesion molecule that interacts with hyaluronic acid (HA) and undergoes sequential proteolytic cleavages in its ectodomain and intramembranous domain. The ectodomain cleavage is triggered by extracellular Ca2+ influx or the activation of protein kinase C. Here we show that CD44-mediated cell–matrix adhesion is terminated by two independent ADAM family metalloproteinases, ADAM10 and ADAM17, differentially regulated in response to those stimuli. Ca2+ influx activates ADAM10 by regulating the association between calmodulin and ADAM10, leading to CD44 ectodomain cleavage. Depletion of ADAM10 strongly inhibits the Ca2+ influx-induced cell detachment from matrix. On the other hand, phorbol ester stimulation activates ADAM17 through the activation of PKC and small GTPase Rac, inducing proteolysis of CD44. Furthermore, depletion of ADAM10 or ADAM17 markedly suppressed CD44-dependent cancer cell migration on HA, but not on fibronectin. The spatio-temporal regulation of two independent signaling pathways for CD44 cleavage plays a crucial role in cell–matrix interaction and cell migration.
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Cites
CD44 is the principal cell surface receptor for hyaluronate
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A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cells
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Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
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Membrane-Type 1 Matrix Metalloproteinase Cleaves Cd44 and Promotes Cell Migration
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Self-citationTNF‐α converting enzyme (TACE) is inhibited by TIMP‐3
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Cited by
Ishimoto, T., Nagano, O., Yae, T., Tamada, M., Motohara, T., Oshima, H., Oshima, M., Ikeda, T., Asaba, R., Yagi, H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.01.038 · Cited by 1,192
Self-citationEDWARDS, D., HANDSLEY, M., & PENNINGTON, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,161
CD44: can a cancer-initiating cell profit from an abundantly expressed molecule?
Zöller, M. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3023 · Cited by 1,112
Martinez-Pomares, L. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0512231 · Cited by 531
Matrix Metalloproteinases Shape the Tumor Microenvironment in Cancer Progression
Niland, S., Riscanevo, A. X., & Eble, J. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010146 · Cited by 503
Metadata
- Authors
- Nagano, O., Murakami, D., Hartmann, D., de Strooper, B., Saftig, P., Iwatsubo, T., Nakajima, M., Shinohara, M., & Saya, H.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2004-06-14
- Volume
- 165
- Issue
- 6
- Pages
- 893-902
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2153266189
- Cited by
- 294
- References
- 43
- FWCI
- 7.72
- Type
- journal article
- Language
- en
- Open access
- green
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- Nagano, O., Murakami, D., Hartmann, D., de Strooper, B., Saftig, P., Iwatsubo, T., Nakajima, M., Shinohara, M., & Saya, H. (2004). Cell–matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca2+ influx and PKC activation. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200310024
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