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Gene Review

Timp3  -  TIMP metallopeptidase inhibitor 3

Rattus norvegicus

Synonyms: Metalloproteinase inhibitor 3, TIMP-3, Timp-3, Tissue inhibitor of metalloproteinases 3
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Disease relevance of Timp3


Psychiatry related information on Timp3

  • Furthermore, the shedding process appears to be regulated under physiologic conditions, because a putative inhibitor of the shedding process, tissue inhibitor of metalloprotease-3 (TIMP-3), is increased by food deprivation [6].

High impact information on Timp3


Biological context of Timp3


Anatomical context of Timp3


Associations of Timp3 with chemical compounds

  • Alendronate did not alter the expression of TIMP 1 and 2, but modestly stimulated the expression of TIMP 3 [18].
  • It also inhibited genes involved in estradiol (P-450(AROM)) and cholesterol biosynthesis (HMG-CoA synthase), as well as genes involved in tissue remodeling: VEGF and TIMP3 [19].
  • LH alone or with genistein did not alter the expression of mRNA encoding TIMP-2 and TIMP-3, or mRNA encoding gelatinases A and B. These data indicate that tyrosine kinases play a role in the LH-induced tissue remodelling required for ovulation by mediating the LH-stimulated expression of collagenase 3 [20].
  • In this study we show that overexpression of TIMP-3 by adenovirus-mediated gene transfer partially protects neurons against excitotoxic death induced by glutamate in culture [21].

Other interactions of Timp3

  • TIMP-2 and TIMP-3 transcripts become detectable on day 10 and remained stable afterwards [22].
  • Amelioration of hepatic ischemia/reperfusion injury after inhibition of TACE activity by TIMP-3 suggests that TACE inhibition may play an important role in preventing liver ischemia/reperfusion injury warranting further experimental and clinical study [1].
  • In contrast, TIMP-1 and TIMP-3 expression in E19 scarring wounds increased six-fold and four-fold, respectively [23].
  • Both MMP-9 and TIMP-3 were regulated by various cytokines [16].
  • Taken together, our results suggest that MMP-2 and TIMP-3 may have functional roles in rat luteal formation, while TIMP-2 may be implicated in both formation and regression of the pregnant CL [24].

Analytical, diagnostic and therapeutic context of Timp3


  1. TIMP-3 Ameliorates Hepatic Ischemia/Reperfusion Injury Through Inhibition of Tumor Necrosis Factor-Alpha-Converting Enzyme Activity in Rats. Tang, Z.Y., Loss, G., Carmody, I., Cohen, A.J. Transplantation (2006) [Pubmed]
  2. Differential mRNA expression of renal cortical tissue inhibitor of metalloproteinase-1, -2, and -3 in experimental hydronephrosis. Engelmyer, E., van Goor, H., Edwards, D.R., Diamond, J.R. J. Am. Soc. Nephrol. (1995) [Pubmed]
  3. ADAM-17 and TIMP3 protein and mRNA expression in spinal cord white matter of rats with acute experimental autoimmune encephalomyelitis. Plumb, J., Cross, A.K., Surr, J., Haddock, G., Smith, T., Bunning, R.A., Woodroofe, M.N. J. Neuroimmunol. (2005) [Pubmed]
  4. Fibrosis and matrix metalloproteinases in rat renal allografts. Inkinen, K.A., Soots, A.P., Krogerus, L.A., Lautenschlager, I.T., Ahonen, J.P. Transpl. Int. (2005) [Pubmed]
  5. ADAMTS-1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes. Cross, A.K., Haddock, G., Stock, C.J., Allan, S., Surr, J., Bunning, R.A., Buttle, D.J., Woodroofe, M.N. Brain Res. (2006) [Pubmed]
  6. Syndecan-3 modulates food intake by interacting with the melanocortin/AgRP pathway. Reizes, O., Benoit, S.C., Strader, A.D., Clegg, D.J., Akunuru, S., Seeley, R.J. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  7. Divergent effects of tissue inhibitor of metalloproteinase-1, -2, or -3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis. Baker, A.H., Zaltsman, A.B., George, S.J., Newby, A.C. J. Clin. Invest. (1998) [Pubmed]
  8. Tissue inhibitor of metalloproteinase-3 induces a Fas-associated death domain-dependent type II apoptotic pathway. Bond, M., Murphy, G., Bennett, M.R., Newby, A.C., Baker, A.H. J. Biol. Chem. (2002) [Pubmed]
  9. TIMP-3 binds to sulfated glycosaminoglycans of the extracellular matrix. Yu, W.H., Yu, S., Meng, Q., Brew, K., Woessner, J.F. J. Biol. Chem. (2000) [Pubmed]
  10. Cellular localization of tissue inhibitors of metalloproteinases in the rat ovary throughout pseudopregnancy. Curry, T.E., Wheeler, S.E. Biol. Reprod. (2002) [Pubmed]
  11. Distribution and expression of tissue inhibitors of metalloproteinase in dorsal root entry zone and dorsal column after dorsal root injury. Zhang, X., Bo, X., Anderson, P.N., Lieberman, A.R., Zhang, Y. J. Neurosci. Res. (2006) [Pubmed]
  12. Spatiotemporal messenger ribonucleic acid expression of ovarian tissue inhibitors of metalloproteinases throughout the rat estrous cycle. Simpson, K.S., Byers, M.J., Curry, T.E. Endocrinology (2001) [Pubmed]
  13. Cloning and expression of the cDNA encoding rat tissue inhibitor of metalloproteinase 3 (TIMP-3). Wu, I., Moses, M.A. Gene (1996) [Pubmed]
  14. Expression patterns of matrix metalloproteinases and their inhibitors in parenchymal and non-parenchymal cells of rat liver: regulation by TNF-alpha and TGF-beta1. Knittel, T., Mehde, M., Kobold, D., Saile, B., Dinter, C., Ramadori, G. J. Hepatol. (1999) [Pubmed]
  15. Cellular localization of gelatinases and tissue inhibitors of metalloproteinases during follicular growth, ovulation, and early luteal formation in the rat. Curry, T.E., Song, L., Wheeler, S.E. Biol. Reprod. (2001) [Pubmed]
  16. Matrix metalloproteases and their inhibitors are produced by overlapping populations of activated astrocytes. Muir, E.M., Adcock, K.H., Morgenstern, D.A., Clayton, R., von Stillfried, N., Rhodes, K., Ellis, C., Fawcett, J.W., Rogers, J.H. Brain Res. Mol. Brain Res. (2002) [Pubmed]
  17. Regulation of collagenase-3 by bone morphogenetic protein-2 in bone cell cultures. Varghese, S., Canalis, E. Endocrinology (1997) [Pubmed]
  18. Alendronate stimulates collagenase 3 expression in osteoblasts by posttranscriptional mechanisms. Varghese, S., Canalis, E. J. Bone Miner. Res. (2000) [Pubmed]
  19. Opposite effect of prolactin and prostaglandin F(2 alpha) on the expression of luteal genes as revealed by rat cDNA expression array. Stocco, C., Callegari, E., Gibori, G. Endocrinology (2001) [Pubmed]
  20. Effects of genistein on the periovulatory expression of messenger ribonucleic acid for matrix metalloproteinases and tissue inhibitors of metalloproteinases in the rat ovary. Komar, C.M., Matousek, M., Mitsube, K., Mikuni, M., Brännström, M., Curry, T.E. Reproduction (2001) [Pubmed]
  21. Adenoviral mediated transfer of TIMP-3 partially prevents glutamate-induced cell death in primary cultured cortical neurons of the rat. Pi, R., Yin, W., Zheng, S., Qiu, P., Zhou, J., Guo, W., Su, T., Yan, G. Brain Res. Mol. Brain Res. (2004) [Pubmed]
  22. Altered balance between matrix metalloproteinases and their inhibitors in experimental biliary fibrosis. Kossakowska, A.E., Edwards, D.R., Lee, S.S., Urbanski, L.S., Stabbler, A.L., Zhang, C.L., Phillips, B.W., Zhang, Y., Urbanski, S.J. Am. J. Pathol. (1998) [Pubmed]
  23. Scarless fetal wounds are associated with an increased matrix metalloproteinase-to-tissue-derived inhibitor of metalloproteinase ratio. Dang, C.M., Beanes, S.R., Lee, H., Zhang, X., Soo, C., Ting, K. Plast. Reconstr. Surg. (2003) [Pubmed]
  24. Expression of gelatinases and their tissue inhibitors in rat corpus luteum during pregnancy and postpartum. Li, Q.L., Wang, H.M., Lin, H.Y., Liu, D.L., Zhang, X., Liu, G.Y., Qian, D., Zhu, C. Mol. Reprod. Dev. (2002) [Pubmed]
  25. Tissue inhibitor of metalloproteinase-3 is associated with neuronal death in reperfusion injury. Wallace, J.A., Alexander, S., Estrada, E.Y., Hines, C., Cunningham, L.A., Rosenberg, G.A. J. Cereb. Blood Flow Metab. (2002) [Pubmed]
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