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* {{Cite journal|author=Brew K, Dinakarpandian D, Nagase H |title=Tissue inhibitors of metalloproteinases: evolution, structure and function |journal=Biochim Biophys Acta |volume=1477 |issue=1–2 |pages=267–83 |year=2000 |pmid=10708863|doi=10.1016/S0167-4838(99)00279-4}}
* {{Cite journal|author=Brew K, Dinakarpandian D, Nagase H |title=Tissue inhibitors of metalloproteinases: evolution, structure and function |journal=Biochim Biophys Acta |volume=1477 |issue=1–2 |pages=267–83 |year=2000 |pmid=10708863|doi=10.1016/S0167-4838(99)00279-4}}


[[Category:Human proteins]]





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[[ru:Эндогенные ингибиторы металлопротеиназ]]
[[ru:Эндогенные ингибиторы металлопротеиназ]]
[[Category:Human proteins]]

Revision as of 03:42, 2 January 2012

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.

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.

Activated by TGF-Beta

  • 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. doi:10.1016/S0167-4838(99)00279-4. PMID 10708863.{{cite journal}}: CS1 maint: multiple names: authors list (link)