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Gene Review

TIMP1  -  TIMP metallopeptidase inhibitor 1

Sus scrofa

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Disease relevance of TIMP1

  • MMPs and the tissue inhibitor of MMPs (TIMP) were investigated in primary cultures of pig fibroblasts from radiation-induced dermal fibrosis and compared to normal dermal fibroblasts [1].
  • Co-transfection of tissue inhibitor of metalloproteinase-1 (TIMP-1) with MMP-9 prevented the intravascular thrombus formation in vivo [2].
  • Staining intensity correlated with TIMP-1 protein levels in oviductal flushings [3].

High impact information on TIMP1

  • CONCLUSION: Cyclical loading of articular cartilage causes bFGF-dependent activation of ERK and synthesis of TIMP-1 [4].
  • These observations were paralleled by the predominant expression of TIMP-1 and -2 in the media (14-fold and 37-fold higher than in adventitia, respectively, P<0.001), whereas higher gelatinolytic activities (MMP-2 and -9) were released from adventitial explants [5].
  • In conclusion, this study demonstrated differential migratory properties and distinct MMP/TIMP synthesis by coronary fibroblasts and smooth muscle cells [5].
  • Smooth muscle cell outgrowth from the media was regulated by endogenous TIMPs, since TIMP inhibition (recombinant MMP-2 or neutralizing anti-TIMP antibodies) facilitated cell outgrowth (P<0.001) [5].
  • PURPOSE: Trabecular meshwork (TM) matrix metalloproteinase (MMP), and tissue inhibitor (TIMP) changes in response to mechanical stretching appear to be central to intraocular pressure (IOP) homeostasis [6].

Chemical compound and disease context of TIMP1


Biological context of TIMP1

  • De novo synthesis of TIMP-1 protein was found throughout the estrous cycle and early pregnancy in all functional segments, but protein expression was greater in the I and greatest on Day 2 [3].
  • An inverse pattern was found for gene expression of TIMP-1 and TIMP-2 [7].
  • There was a phase x tissue type interaction for the presence of both TIMP-1 and -2 (P < 0.03, P < 0.05, respectively), and TIMPs were detected in more granulosa and theca cell samples after hCG than during the follicular phase [8].

Anatomical context of TIMP1

  • The role of TIMP-1 in the oviduct remains to be established [3].
  • Day 15.75 pig embryos and uteri expressed transcripts for uPA, MMP-2 and -9, and TIMP-1, -2, and -3 [9].
  • TIMP-1 transcripts were abundant in extraembryonic endoderm and scattered throughout the trophectoderm [9].
  • TIMP-1 protein was immunolocalized primarily to luminal epithelium of the INF, A, and I on all days of the estrous cycle and early pregnancy and to some cells in the stroma and blood vessel walls [3].
  • In conclusion, TIMP-1, -2 and -3 were present in large and small pig follicles and were produced by both granulosa and theca cells, although concentrations differed with the type of tissue [8].

Associations of TIMP1 with chemical compounds

  • In steroid-treated OVX gilts, TIMP-1 protein synthesis was greatest in the I regardless of treatment, but with increased intensity after EV+P4 treatment [3].
  • In steroid-treated OVX gilts, an effect of treatment with estradiol valerate (EV) + progesterone (P4) was shown with increased (p < 0.003) TIMP-1 mRNA levels [3].
  • Immunoblotting for tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) showed no decreased production in the doxycycline-treated groups [10].

Other interactions of TIMP1


Analytical, diagnostic and therapeutic context of TIMP1

  • Oviductal TIMP-1 mRNA levels and protein expression were examined in gilts during the estrous cycle and early pregnancy and in steroid-treated ovariectomized (OVX) gilts by explant culture, two-dimensional SDS-PAGE and fluorography, dot-blot hybridization, immunoblot analysis, RIA, and immunocytochemical studies [3].
  • By HPLC, collagenase inhibitor activity was localized in a fraction consistent with the size of TIMP [14].


  1. Expression of 72-kDa gelatinase (MMP-2), collagenase (MMP-1), and tissue metalloproteinase inhibitor (TIMP) in primary pig skin fibroblast cultures derived from radiation-induced skin fibrosis. Lafuma, C., El Nabout, R.A., Crechet, F., Hovnanian, A., Martin, M. J. Invest. Dermatol. (1994) [Pubmed]
  2. Overexpression of matrix metalloproteinase-9 promotes intravascular thrombus formation in porcine coronary arteries in vivo. Morishige, K., Shimokawa, H., Matsumoto, Y., Eto, Y., Uwatoku, T., Abe, K., Sueishi, K., Takeshita, A. Cardiovasc. Res. (2003) [Pubmed]
  3. Expression of tissue inhibitor of metalloproteinase-1 protein and messenger ribonucleic acid by the oviduct of cyclic, early-pregnant, and ovariectomized steroid-treated gilts. Buhi, W.C., Alvarez, I.M., Pickard, A.R., McIntush, E.W., Kouba, A.J., Ashworth, C.J., Smith, M.F. Biol. Reprod. (1997) [Pubmed]
  4. Basic fibroblast growth factor mediates transduction of mechanical signals when articular cartilage is loaded. Vincent, T.L., Hermansson, M.A., Hansen, U.N., Amis, A.A., Saklatvala, J. Arthritis Rheum. (2004) [Pubmed]
  5. Role of matrix metalloproteinases and their tissue inhibitors in the regulation of coronary cell migration. Shi, Y., Patel, S., Niculescu, R., Chung, W., Desrochers, P., Zalewski, A. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  6. Signaling pathways used in trabecular matrix metalloproteinase response to mechanical stretch. Bradley, J.M., Kelley, M.J., Rose, A., Acott, T.S. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  7. Secretion and gene expression of metalloproteinases and gene expression of their inhibitors in porcine corpora lutea at different stages of the luteal phase. Pitzel, L., Lüdemann, S., Wuttke, W. Biol. Reprod. (2000) [Pubmed]
  8. Production of tissue inhibitors of metalloproteinases (TIMPs) by pig ovarian cells in vivo and the effect of TIMP-1 on steroidogenesis in vitro. Shores, E.M., Hunter, M.G. J. Reprod. Fertil. (2000) [Pubmed]
  9. Expression of proteinases and proteinase inhibitors during embryo-uterine contact in the pig. Menino, A.R., Hogan, A., Schultz, G.A., Novak, S., Dixon, W., Foxcroft, G.H. Dev. Genet. (1997) [Pubmed]
  10. Doxycycline inhibits elastin degradation and reduces metalloproteinase activity in a model of aneurysmal disease. Boyle, J.R., McDermott, E., Crowther, M., Wills, A.D., Bell, P.R., Thompson, M.M. J. Vasc. Surg. (1998) [Pubmed]
  11. Relaxin increases secretion of tissue inhibitor of matrix metalloproteinase-1 and -2 during uterine and cervical growth and remodeling in the pig. Lenhart, J.A., Ryan, P.L., Ohleth, K.M., Palmer, S.S., Bagnell, C.A. Endocrinology (2002) [Pubmed]
  12. Effect of doxycycline on sulfur mustard-induced respiratory lesions in guinea pigs. Guignabert, C., Taysse, L., Calvet, J.H., Planus, E., Delamanche, S., Galiacy, S., d'Ortho, M.P. Am. J. Physiol. Lung Cell Mol. Physiol. (2005) [Pubmed]
  13. Levels of matrix metalloproteinase-9 and its inhibitor in guinea pig asthma model following ovalbumin challenge. Tang, L.F., Du, L.Z., Zou, C.C., Gu, W.Z. Fetal and pediatric pathology. (2005) [Pubmed]
  14. Collagenase-inhibitory activity in deposit and resorption phases of guinea pig carrageenin granuloma. Pardo, A., Ramirez, R., Ramos, C., Montaãno, M., Selman, M. Connect. Tissue Res. (1992) [Pubmed]
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