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. 2021 Apr 25;22(9):4483. doi: 10.3390/ijms22094483

Table 6.

Characteristics of MMPs associated with BC development.

Gene Gene Localised Name (Aliases) Location Substrates Activation Pathway References
MMP-1 11q22.2 interstitial collagenase (CLG, CLGN) secreted collagens: I, II, III, VII, VIII, X, gelatin The plasmin has been described and other serine proteases, i.e., kallikrein, trypsin, neutrophil elastase, cathepsin G, tryptase and chymase may be involved in the activation of proMMP-1. [293,294]
MMP-2 16q12.2 gelatinase-A, 72 kDa gelatinase secreted gelatin, collagens: I, II, III, IV, Vii, X A complex of membrane-type 1 MMP (MT1-MMP/MMP14) and tissue inhibitor of MMP-2 recruits pro-MMP 2 from the extracellular milieu to the cell surface. Activation then requires an active molecule of MT1-MMP and autocatalytic cleavage. Clustering of integrin chains promotes MMP-2 activation. Another factor that will support the activation of MMP-2 is cell-cell clustering. A wild-type activated leukocyte cell adhesion molecule (ALCAM) is also required to activate the MMP-2. [146,147,293,295,296,297,298,299,300,301,302,303,304,305,306]
MMP-7 11q22.2 matrilysin, PUMP 1 (MMP-7, MPSL-1, PUMP-1) secreted fibronectin, laminin, collagen IV, gelatin Pro-MMP7 is converted from the latent form to the active form by endoproteinases and plasmin. Plasmin cleaves at the site recognisable to trypsin is considered as the possible physiological activator. [299,307]
MMP-9 20q13.12 gelatinase-B, 92 kDa gelatinase (CLG4B, GELB, MANDP2, MMP-9) secreted gelatin, collagen IV, V The proMMP-9 includes a cysteine residue in the N-terminal pro-domain that binds to the zinc atom in the active site thus maintaining latency. Activation of MMP-9 requires a disruption of the cysteine interaction with the zinc atom. MMP-9 activators include MMP-2, MMP-3, MMP-7, MMP-10, MMP-13, cathepsin G and urokinase/plasmin. [296,297,298,299,304]
MMP12 11q22.2 macrophage metalloelastase (HME, ME, MME, MMP-12) secreted elastin, fibronectin, collagen IV Neutrophil elastase may be required for the proteolytic activation of pro-MMP-12 [304]