Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1.
By V. Noë, B. Fingleton, K. Jacobs, H. Crawford, S. Vermeulen, W. Steelant, E. Bruyneel, L. Matrisian, M. Mareel. Journal of Cell Science, 2001
754 citations recorded by the source corpus.
View Paper: https://www.semanticscholar.org/paper/221fa1c6d5e022d9a205fa6669d2e0d23d8ab449
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Citations in the corpus
- How matrix metalloproteinases regulate cell behavior. (2001, background): “For example, MMP3 and MMP7 both cleave the adherens junction protein E-cadherin, and the soluble extracellular fragment that is released disrupts cell aggregation and promotes cell invasion in a paracrine manner independent of the cleavage event itself (Lochter et al. 1997, Noe et al. 2001).”
- Interplay of cadherin-mediated cell adhesion and canonical Wnt signaling. (2010, unknown): “5) (Lochter et al. 1997; Noe et al. 2001).”
- Role of tissue stroma in cancer cell invasion (2003, background): “Ectodomain shedding of E-cadherin generates a soluble 80 kDa fragment that stimulates invasion [163,164].”
- Involvement of members of the cadherin superfamily in cancer. (2009, unknown): “4) (Lochter et al. 1997; Davies et al. 2001; Noë et al. 2001; Covington et al. 2006; Symowicz et al. 2007).”
- Extracellular matrix remodelling: the role of matrix metalloproteinases (2003, background): “E-cadherin is cleaved by MMP-3 and -7 [56] whereas the extracellular domain of the hyaluronan (HA) receptor CD44 is cleaved by MMP-14 [57].”
- E-cadherin–integrin crosstalk in cancer invasion and metastasis (2013, background): “E-cadherin and thus impact on AJ integrity (Noë et al., 2001; Rios-Doria et al., 2003).”
- EMT and tumor metastasis (2015, background): “Cleavage of the E-cadherin ectodomain has been shown to create a fragment, sE-cad, capable of inducing EMT, invasion, and proliferation in a paracrine manner via EGFR signaling [50,51].”
- Matrix MetalloProteinases (MMPs) andTissue Inhibitors of MetalloProteinases (TIMPs): positive and negative regulators intumor cell adhesion (2010, unknown): “The released soluble E-cadherin was shown to promote cell invasion;although the mechanism was not shown, it was proposed that the soluble fragment my inhibit the membrane bound E-cadherin function and disrupt cell-cell contacts [74].”
- The p120ctn-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides (2002, background): “cleavage by Matrilysin (39) provide additional links between Matrilysin and cadherin-mediated cell adhesion.”