Tissue inhibitor of metalloproteinase: Difference between revisions
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The complex of latent MMP-2 (pro-MMP-2)with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP ([[MMP14|MMP-14]]), a membrane-anchored MMP. |
The complex of latent MMP-2 (pro-MMP-2)with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP ([[MMP14|MMP-14]]), a membrane-anchored MMP. |
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The |
The role of the pro-MMP-9/TIMP-1 complex is still unknown. |
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==References== |
==References== |
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Revision as of 23:56, 5 November 2013
The matrix metalloproteinases are inhibited by specific endogenous tissue inhibitors of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP1, TIMP2, TIMP3 and TIMP4.[1]
Overall, all MMPs are inhibited by TIMPs once they are activated but the gelatinases (MMP-2 and MMP-9) can form complexes with TIMPs when the enzymes are in the latent form.
The complex of latent MMP-2 (pro-MMP-2)with TIMP-2 serves to facilitate the activation of pro-MMP-2 at the cell surface by MT1-MMP (MMP-14), a membrane-anchored MMP.
The role of the pro-MMP-9/TIMP-1 complex is still unknown.
References
- ^ Brew K, Dinakarpandian D, Nagase H (2000). "Tissue inhibitors of metalloproteinases: evolution, structure and function". Biochim Biophys Acta. 1477 (1–2): 267–83. doi:10.1016/S0167-4838(99)00279-4. PMID 10708863.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
- Tissue+Inhibitor+of+Metalloproteinases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)