E-cadherin strand dimer degradation by MMP3, MMP7 and Plasmin

Stable Identifier
R-NUL-2534162
Type
Reaction [transition]
Species
Homo sapiens
Compartment
General
SVG |   | PPTX  | SBGN
E-cadherin strand dimer degradation by MMP3, MMP7 and Plasmin

Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001) and plasmin (Ryniers et al. 2002), all cleave dog CDH1 extracellularly, close to the transmembrane region.

Literature References
PubMed ID Title Journal Year
11928810 Plasmin produces an E-cadherin fragment that stimulates cancer cell invasion

Ryniers, F, Stove, C, Goethals, M, Brackenier, L, Noë, V, Bracke, M, Vandekerckhove, J, Mareel, M, Bruyneel, E

Biol. Chem. 2002
11112695 Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1

Noë, V, Fingleton, B, Jacobs, K, Crawford, HC, Vermeulen, S, Steelant, W, Bruyneel, E, Matrisian, LM, Mareel, M

J Cell Sci 2001
Participants
Catalyst Activity
Catalyst Activity
Title
serine-type endopeptidase activity of MMP3, MMP7, Plasmin [extracellular region]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
Cite Us!