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TIMP2  -  TIMP metallopeptidase inhibitor 2

Gallus gallus

 
 
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Disease relevance of TIMP2

  • The aim of this study was to investigate the distribution of matrix metalloproteinase (MMP)-2, MMP-9, tissue inhibitor of matrix metalloproteinase (TIMP)-1 and TIMP-2 using immunohistochemistry in the ascites syndrome of broiler chickens in a salt-induced experimental model [1].
  • METHODS: Total RNA was extracted from the posterior scleras of form-deprived chick eyes, eyes recovering from deprivation myopia, and paired contralateral control eyes, and subjected to northern blot analysis analyses using cDNA probes to chicken gelatinase A and TIMP-2 [2].
  • In addition, the TIMP-2 concentration in EDTA plasma from colorectal cancer patients revealed a significantly higher level in plasma from patients with Dukes stage A (P = 0.01) compared with patients with more advanced Dukes stages [3].
  • The TIMP-2 concentration in citrate plasma from 15 patients with advanced, stage IV breast cancer had a median value of 160 ng/ml, only slightly higher but statistically distinguishable from the level found in citrate plasma from the healthy donors [3].
 

High impact information on TIMP2

  • Gelatinase A and TIMP-2 expression in the fibrous sclera of myopic and recovering chick eyes [2].
  • In contrast, TIMP-2 expression was significantly decreased (-53%, P = 0.027) in the posterior scleras of form-deprived eyes [2].
  • The presence in transformed cultures of elevated levels of a more readily activated TIMP-free progelatinase, the suppression of its rapid activation by TIMP-2, and the potential effect of the altered balance between TIMP-free and TIMP-complexed 70 kDa progelatinase on the invasive, malignant phenotype, are discussed [4].
  • Tissue inhibitor of metalloproteinase-2 (TIMP-2) expression during cardiac neural crest cell migration and its role in proMMP-2 activation [5].
  • Antisense TIMP-2 oligonucleotides block proMMP-2 activation, decrease NC cell migration from explants, and perturb NC morphogenesis in ovo [5].
 

Biological context of TIMP2

  • The 3.5-kb cDNA presents an open reading frame that predicts a protein of 220 amino acids showing 97.2, 96.8, 97.2, and 77.3% overall identity with human, mouse, rat, and chicken TIMP-2, respectively [6].
  • Its NH2-terminal amino acid sequence determined up to the 11th amino acid residue was identical with that of the tissue inhibitor of metalloproteinases-2 (TIMP-2) [7].
 

Anatomical context of TIMP2

  • TIMP-2 mRNA is expressed at stage 11 in the neural epithelium and only in migrating cardiac NC cells [5].
  • Mechanical stretch also enhanced the expression of MMP-2 and TIMP-2 mRNA in scleral fibroblasts significantly [8].
  • On the other hand, when somites in culture are treated with TIMP-2, some mesenchymal cells are produced, suggesting that they undergo the EMT, but show greatly reduced migration through the collagen gel [9].
  • Induction of angiogenesis in chick yolk-sac membrane by polyamines and its inhibition by tissue inhibitors of metalloproteinases (TIMP and TIMP-2) [10].
 

Associations of TIMP2 with chemical compounds

 

Other interactions of TIMP2

  • Changes in scleral MMP-2, TIMP-2 and TGFbeta-2 mRNA expression after imposed myopic and hyperopic defocus in chickens [12].
 

Analytical, diagnostic and therapeutic context of TIMP2

References

  1. The identification of matrix metalloproteinases and their tissue inhibitors in broiler chickens by immunohistochemistry. Ozyigit, M.O., Kahraman, M.M., Sonmez, G. Avian Pathol. (2005) [Pubmed]
  2. Gelatinase A and TIMP-2 expression in the fibrous sclera of myopic and recovering chick eyes. Rada, J.A., Perry, C.A., Slover, M.L., Achen, V.R. Invest. Ophthalmol. Vis. Sci. (1999) [Pubmed]
  3. Quantification of tissue inhibitor of metalloproteinases 2 in plasma from healthy donors and cancer patients. Larsen, M.B., Stephens, R.W., Brünner, N., Nielsen, H.J., Engelholm, L.H., Christensen, I.J., Stetler-Stevenson, W.G., Høyer-Hansen, G. Scand. J. Immunol. (2005) [Pubmed]
  4. Native TIMP-free 70 kDa progelatinase (MMP-2) secreted at elevated levels by RSV transformed fibroblasts. Stefansson, S., Aimes, R.T., Seward, N.B., Alexander, D.S., Quigley, J.P. J. Cell. Physiol. (1994) [Pubmed]
  5. Tissue inhibitor of metalloproteinase-2 (TIMP-2) expression during cardiac neural crest cell migration and its role in proMMP-2 activation. Cantemir, V., Cai, D.H., Reedy, M.V., Brauer, P.R. Dev. Dyn. (2004) [Pubmed]
  6. 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]
  7. Purification of an angiogenesis inhibitor from culture medium conditioned by a human chondrosarcoma-derived chondrocytic cell line, HCS-2/8. Ohba, Y., Goto, Y., Kimura, Y., Suzuki, F., Hisa, T., Takahashi, K., Takigawa, M. Biochim. Biophys. Acta (1995) [Pubmed]
  8. Involvement of mechanical stretch in the gelatinolytic activity of the fibrous sclera of chicks, in vitro. Fujikura, H., Seko, Y., Tokoro, T., Mochizuki, M., Shimokawa, H. Jpn. J. Ophthalmol. (2002) [Pubmed]
  9. MMP-2 plays an essential role in producing epithelial-mesenchymal transformations in the avian embryo. Duong, T.D., Erickson, C.A. Dev. Dyn. (2004) [Pubmed]
  10. Induction of angiogenesis in chick yolk-sac membrane by polyamines and its inhibition by tissue inhibitors of metalloproteinases (TIMP and TIMP-2). Takigawa, M., Nishida, Y., Suzuki, F., Kishi, J., Yamashita, K., Hayakawa, T. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  11. Isolation and characterisation of a chicken gelatinase (type IV collagenase). Craig, F.M., Archer, C.W., Murphy, G. Biochim. Biophys. Acta (1991) [Pubmed]
  12. Changes in scleral MMP-2, TIMP-2 and TGFbeta-2 mRNA expression after imposed myopic and hyperopic defocus in chickens. Schippert, R., Brand, C., Schaeffel, F., Feldkaemper, M.P. Exp. Eye Res. (2006) [Pubmed]
  13. A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family. Pavloff, N., Staskus, P.W., Kishnani, N.S., Hawkes, S.P. J. Biol. Chem. (1992) [Pubmed]
 
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