Tissue inhibitor of metalloproteinase: Difference between revisions
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The [[matrix metalloproteinase]]s are inhibited by specific endogenous '''tissue inhibitor of metalloproteinases''' (TIMPs), which comprise a family of four protease inhibitors: |
The [[matrix metalloproteinase]]s are inhibited by specific endogenous '''tissue inhibitor of metalloproteinases''' (TIMPs), which comprise a family of four protease inhibitors: ''[[TIMP1]]'', {{Gene|TIMP2}}, {{Gene|TIMP3}} and {{Gene|TIMP4}}. |
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Overall, all |
Overall, all [[Matrix metalloproteinase|MMP]]s are inhibited by TIMPs once they are activated but the [[gelatinase]]s ([[MMP2|MMP-2]] and [[MMP9|MMP-9]]) can form complexes with TIMPs when the enzymes are in the latent form. |
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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 (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 role of the pro-MMP-9/TIMP-1 complex is still unknown. |
The role of the pro-MMP-9/TIMP-1 complex is still unknown. |
Revision as of 20:23, 5 November 2007
The matrix metalloproteinases are inhibited by specific endogenous tissue inhibitor of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP1, TIMP2, TIMP3 and TIMP4.
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.
External links
- Tissue+Inhibitor+of+Metalloproteinases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- Brew K, Dinakarpandian D, Nagase H (2000). "Tissue inhibitors of metalloproteinases: evolution, structure and function". Biochim Biophys Acta. 1477 (1–2): 267–83. PMID 10708863.
{{cite journal}}
: CS1 maint: multiple names: authors list (link)