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

Stable Identifier
R-NUL-2534162
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, extracellular region
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | 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
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
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
Participants
Input
Output
Catalyst Activity

serine-type endopeptidase activity of MMP3, MMP7, Plasmin [extracellular region]

Physical Entity
MMP3, MMP7, Plasmin [extracellular region] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
Orthologous Events
E-cadherin degradation by MMP3, MMP7 and plasmin (Homo sapiens)
Authored
Jupe, S  (2012-08-08)
Reviewed
Ricard-Blum, S  (2013-08-13)
Created
Jupe, S  (2012-10-24)
Cite Us!