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Tissue inhibitor of metalloproteinase

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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.

Regulation of TIMP expression

In adrenocortical cells the trophic hormone ACTH induces expression of TIMP-1 and the increase in TIMP expression is also associated with decreased collagenase activity.[2]

References

  1. ^ 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)
  2. ^ Reichenstein, M.; Reich, R.; LeHoux, JG.; Hanukoglu, I. (2004). "ACTH induces TIMP-1 expression and inhibits collagenase in adrenal cortex cells". Mol Cell Endocrinol. 215 (1–2): 109–14. doi:10.1016/j.mce.2003.11.011. PMID 15026182. {{cite journal}}: Unknown parameter |month= ignored (help)