Initial activation of proMMP2 by MMP1, 7

Stable Identifier
R-HSA-1604359
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

MMP2 can be activated by MMP1 (Crabbe et al. 1994a, Sang et al. 1996) and MMP7 (Crabbe et al. 1994b, Sang et al. 1996). MMP1 initially cleaves either Pro33-Ile34 or Asn66-Leu67. This is followed by autolytic cleavage at Asn109-Tyr110 (Crabbe et al. 1994a, Okada et al. 1990, Sang et al. 1996). MMP1 and MMP7 are not efficient activators of MMP2; significant physiological activation of proMMP2 is performed by the MT-MMPs MMP14 (Sato et al. 1994), MMP15 (Butler et al. 1997, Morrison et al. 2001) and MMP16 (Takino et al. 1995). Residue numbering here refers to the UniProt canonical sequence.

Literature References
PubMed ID Title Journal Year
8015608 A matrix metalloproteinase expressed on the surface of invasive tumour cells

Sato, H, Takino, T, Okada, Y, Cao, J, Shinagawa, A, Yamamoto, E, Seiki, M

Nature 1994
8194591 Human progelatinase A can be activated by matrilysin

Crabbe, T, Smith, B, O'Connell, J, Docherty, A

FEBS Lett 1994
7981201 Reciprocated matrix metalloproteinase activation: a process performed by interstitial collagenase and progelatinase A

Crabbe, T, O'Connell, JP, Smith, BJ, Docherty, AJ

Biochemistry 1994
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
serine-type endopeptidase activity of MMP1,7 [extracellular region]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed