Tissue inhibitor of metalloproteinase: Difference between revisions
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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> |
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{{Redirect|TIMP|the drug metabolite|Thioinosine monophosphate}} |
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The [[matrix metalloproteinase]]s are inhibited by specific endogenous '''tissue inhibitors of metalloproteinases''' (TIMPs), which comprise a family of four protease inhibitors: ''[[TIMP1]]'', ''[[TIMP2]]'', ''[[TIMP3]]'' and ''[[TIMP4]]''.<ref>{{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}}</ref> |
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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 |
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. |
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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 ([[MMP14|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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* {{MeshName|Tissue+Inhibitor+of+Metalloproteinases}} |
* {{MeshName|Tissue+Inhibitor+of+Metalloproteinases}} |
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==External links== |
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*{{Commonscat-inline|Tissue inhibitor of metalloproteinases, TIMP}} |
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[[Category:Human proteins]] |
[[Category:Human proteins]] |
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[[ru:Эндогенные ингибиторы металлопротеиназ]] |
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Latest revision as of 15:26, 20 April 2024
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
[edit]- ^ 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
[edit]
Media related to Tissue inhibitor of metalloproteinases, TIMP at Wikimedia Commons
