Tissue inhibitor of metalloproteinase
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. PMID 10708863. doi:10.1016/S0167-4838(99)00279-4.
- Tissue Inhibitor of Metalloproteinases at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from
Wikipedia.
The text is licensed under Creative Commons - Attribution - Sharealike.
Additional terms may apply for the media files.