Matrix metalloproteinases (MMPs) are a family of extracellular zinc-dependent endopeptidases that can break down all types of extracellular matrix proteins . They play a role in tissue remodeling, angiogenesis , cell proliferation, migration and differentiation of cells, apoptosis , and tumor growth inhibition. Involved in the cleavage of membrane receptors, the release of apoptotic ligands, such as FAS, as well as in the activation and deactivation of chemokines and cytokines . [one]
MMPs were first described in vertebrates in 1962, and later found in invertebrates and plants. The main differences between MMP and other endopeptidases are their dependence on metal ions , the ability to destroy the structures of the extracellular matrix.
Content
Genes
| Gene | Title | Localization | Description |
| MMP1 | Interstitial collagenase | secreted | |
| MMP2 | Gelatinase-A, 72 kDa- Gelatinase | secreted | |
| MMP3 | Stromelysin 1 | secreted | |
| MMP7 | Matrelysin, PUMP 1 | secreted | |
| MMP8 | Neutrophilic Collagenase | secreted | |
| MMP9 | Gelatinase-B, 92 kDa-Gelatinase | secreted | may play a significant role in the local proteolysis of the extracellular matrix and in the migration of leukocytes. May participate in bone osteoclastic resorption. Splits collagen type IV and V into large C-terminal and smaller N-terminal fragments. Cleaves fibronectin, but not laminin. |
| MMP10 | Stromelysin 2 | secreted | |
| MMP11 | Stromelysin 3 | secreted | MMP-11 is closer to MT-MMP, activated by convertases, and is usually secreted in association with convertase-activated MMPs. |
| MMP12 | Macrophage metalloelastase | secreted | |
| MMP13 | Collagenase 3 | secreted | |
| MMP14 | MT1-MMP | membrane-associated | type-I transmembrane MMP |
| MMP15 | MT2-MMP | membrane-associated | type-I transmembrane MMP |
| MMP16 | MT3-MMP | membrane-associated | type-I transmembrane MMP |
| MMP17 | MT4-MMP | membrane-associated | glycosyl phosphatidylinositol -attached |
| MMP18 | Collagenase 4, xcol4, xenopus -collagenase | - | No human orthologs found |
| MMP19 | RASI-1, sometimes also stromelysin-4 | - | |
| MMP20 | Enamelizin | secreted | |
| MMP21 | X-MMP | secreted | |
| MMP23A | CA-MMP | membrane-associated | type-II transmembrane cysteine array |
| MMP23B | - | membrane-associated | type-II transmembrane cysteine array |
| MMP24 | MT5-MMP | membrane-associated | type-I transmembrane MMP |
| MMP25 | MT6-MMP | membrane-associated | glycosyl phosphatidylinositol -attached |
| MMP26 | Matrilizin-2, endometase | - | |
| MMP27 | MMP-22, C-MMP | - | |
| MMP28 | Epilizine | secreted | Opened in 2001, the name was due to its discovery in human keratinocytes. Unlike other MMPs, this enzyme is constitutively expressed in many tissues. Threonine replaces proline in its cysteine switch (PRCGVTD). [2] |
See also
- Endogenous metalloproteinase inhibitors
Notes
- ↑ Van Lint P., Libert C. Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation (Eng.) // J. Leukoc. Biol. : journal. - 2007 .-- December ( vol. 82 , no. 6 ). - P. 1375-1381 . - DOI : 10.1189 / jlb.0607338 . - PMID 17709402 . (inaccessible link)
- ↑ Lohi J., Wilson CL, Roby JD, Parks WC. Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury. (Eng.) // J Biol Chem : journal. - 2001. - Vol. 276 , no. 13 . - P. 10134-10144 . - DOI : 10.1074 / jbc.M001599200 . - PMID 11121398 .
Links
- MMP (MATRIX METALLOPROTEINASES) - medbiol.ru