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TIMP2  -  TIMP metallopeptidase inhibitor 2

Sus scrofa

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High impact information on TIMP-2


Biological context of TIMP-2


Anatomical context of TIMP-2


Associations of TIMP-2 with chemical compounds

  • Other serine and cysteine protease inhibitors as well as TIMP-2 and BB-2116 (natural tissue inhibitor-2 and synthetic inhibitor of matrix metalloproteinases [MMPs], respectively) were ineffective [7].
  • Immunoblotting for tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) showed no decreased production in the doxycycline-treated groups [8].
  • Hematoxylin and eosin staining, safranin O staining, and immunostaining [matrix metalloprotease-1 (MMP-1) and tissue inhibitor of metalloprotease-2 (TIMP-2)] were used for the histological evaluations of transplanted cartilage [9].

Other interactions of TIMP-2

  • The concentrations were influenced by the type of tissue (TIMP-1, P < 0.005; TIMP-2, P < 0.005, TIMP-3, P > 0.05), and the highest concentrations occurred in the theca tissue [10].

Analytical, diagnostic and therapeutic context of TIMP-2


  1. Expression of tissue inhibitor of metalloproteinase-1, -2, and -3 during neointima formation in organ cultures of human saphenous vein. Kranzhöfer, A., Baker, A.H., George, S.J., Newby, A.C. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  2. 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]
  3. Pressure distention compared with pharmacologic relaxation in vein grafting upregulates matrix metalloproteinase-2 and -9. Chung, A.W., Rauniyar, P., Luo, H., Hsiang, Y.N., van Breemen, C., Okon, E.B. J. Vasc. Surg. (2005) [Pubmed]
  4. Cloning and expression of guinea pig TIMP-2. Expression in normal and hyperoxic lung injury. Meléndez, J., Maldonado, V., Bingle, C.D., Selman, M., Pardo, A. Am. J. Physiol. Lung Cell Mol. Physiol. (2000) [Pubmed]
  5. 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]
  6. Luteinization and proteolysis in ovarian follicles of Meishan and Large White gilts during the preovulatory period. Driancourt, M.A., Quesnel, H., Meduri, G., Prunier, A., Hermier, D. J. Reprod. Fertil. (1998) [Pubmed]
  7. Proteolytic activity degrading insulin-like growth factor-binding protein-2, -3, -4, and -5 in healthy growing and atretic follicles in the pig ovary. Besnard, N., Pisselet, C., Monniaux, D., Monget, P. Biol. Reprod. (1997) [Pubmed]
  8. 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]
  9. Experimental evaluation of the usefulness of osteochondral allograft for articular cartilage defect. Maruyama, S., Hasegawa, Y., Sakano, S., Warashina, H., Kitamura, S., Yamauchi, K., Iwata, H. Journal of orthopaedic science : official journal of the Japanese Orthopaedic Association. (2003) [Pubmed]
  10. 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]
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