Tissue inhibitor of metalloproteinase: Difference between revisions

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Tissue inhibitors of metalloproteinases (TIMPs) are specific endogenous protease inhibitors to the matrix metalloproteinases. There are four TIMPs; TIMP1, TIMP2, TIMP3 and TIMP4.^[1] TIMP3 has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. ^[2] For this reason, TIMP3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression. ^[2]

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 their 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.
^ ^a ^b Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

Tissue+Inhibitor+of+Metalloproteinases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

External links

Media related to Tissue inhibitor of metalloproteinases, TIMP at Wikimedia Commons

[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.

[Rotondo_2015-2] Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F (April 2015). "Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes". J Cell Physiol. 230 (4): 802–812. doi:10.1002/jcp.24808. hdl:11392/2066612. PMID 25205602. S2CID 24986454.

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 '''Tissue inhibitors of metalloproteinases''' ('''TIMPs''') are specific endogenous protease inhibitors to the [[matrix metalloproteinase]]s. There are four TIMPs;  ''[[TIMP1]]'', ''[[TIMP2]]'', ''[[TIMP3]]'' and ''[[TIMP4]]''.<ref>{{Cite journal|vauthors=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}}</ref> TIMP3 has been observed progressively downregulated in [[Human papillomavirus]]-positive [[Neoplasm|neoplastic keratinocytes]] derived from uterine cervical [[Cervical intraepithelial neoplasia| preneoplastic lesions]] at different levels of malignancy. <ref name = "Rotondo_2015">{{cite journal | vauthors = Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F | title = Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes. | journal = J Cell Physiol | volume = 230| issue = 4 | pages = 802–812 | date = April 2015 | pmid = 25205602 | doi = 10.1002/jcp.24808 | hdl = 11392/2066612 | s2cid = 24986454 | hdl-access = free }}</ref> For this reason, TIMP3 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical [[Cervical intraepithelial neoplasia| preneoplastic lesions]] progression. <ref name = "Rotondo_2015">{{cite journal | vauthors = Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R, Torresani S, Marci R, Garutti P, Negrini M, Tognon M, Martini F | title = Gene expression changes in progression of cervical neoplasia revealed by microarray analysis of cervical neoplastic keratinocytes. | journal = J Cell Physiol | volume = 230| issue = 4 | pages = 802–812 | date = April 2015 | pmid = 25205602 | doi = 10.1002/jcp.24808 | hdl = 11392/2066612 | s2cid = 24986454 | hdl-access = free }}</ref>
-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.
+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 their 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 ([[MMP14|MMP-14]]), a membrane-anchored MMP.