The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

TIMP1  -  TIMP metallopeptidase inhibitor 1

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of TIMP1


Psychiatry related information on TIMP1


High impact information on TIMP1

  • Tissue inhibitor of metalloproteinases 1 (TIMP-1) message was significantly enhanced by the cytokine in most instances, whereas TIMP-2 message was markedly decreased by IL-1beta in reoxygenated cultures [4].
  • To prove that increased MMP or decreased TIMP expression could be a result of the autocrine action of VEGF on chondrocytes, we repeated the experiments in the presence of a specific inhibitor for the kinase activity of the VEGFR-2 [5].
  • Sensitivity to known matrix metalloproteinase inhibitors as well as to the endogenous tissue inhibitor of metalloproteinases, TIMP-1, further support the notion that aggrecanase is a metalloproteinase potentially related to the ADAM family or MMP family of proteases previously implicated in the catabolism of the extracellular matrix [6].
  • Retinoids modulate endothelial cell production of matrix-degrading proteases and tissue inhibitors of metalloproteinases (TIMP) [3].
  • Hence, regulation of the MMP-9/TIMP balance failed to correlate with the migratory or invasive capacity [7].

Biological context of TIMP1


Anatomical context of TIMP1


Associations of TIMP1 with chemical compounds

  • The IL-1 decreased expression of TIMP-1 was further reduced by dexamethasone, which resulted in a significant loss of TIMP activity [15].
  • RP 59794 blocks complex formation and can partially dissociate established TIMP: collagenase complexes [16].
  • In conclusion, our data indicate that BOEC secrete TIMP-1 and this glycoprotein promotes the prehatched development of "HanWoo" embryos derived from in vitro-fertilization [17].
  • When examined TIMP-1 secretion, fluorescent foci indicating the secretion of TIMP-1 were found after stained BOEC with fluorescein isothiocyanate [17].

Regulatory relationships of TIMP1

  • Treating chondrocytes with IL-1 induced the expression of MMPs and downregulated TIMP-1 but stimulated both the expression of PAs and PAI-1 [18].
  • Cyclic hydrostatic pressure downregulated the expression of MMP-13 and type I collagen and upregulated expression of TIMP-1 compared to the unloaded controls [19].
  • These results suggest that IL-4 is able to specifically block cartilage collagen resorption by down-regulating the production of collagenase (MMP-1) and up-regulating TIMP-1 by chondrocytes within the cartilage [20].

Other interactions of TIMP1

  • The stretched cells produced significantly larger amounts of metalloproteinase-2 (MMP-2) and tissue inhibitor of metalloproteinase-1 (TIMP-1) after 72 hours, compared with cells in nonstretched control [12].
  • We have examined the regulation of the gelatinase/TIMP balance by transforming growth factor-beta1 (TGF-beta1) and phorbol myristate acetate (PMA) in bovine endothelial cells [7].
  • Temporal and spatial expression of tissue inhibitors of metalloproteinases 1 and 2 (TIMP-1 and -2) in the bovine corpus luteum [13].
  • This evidence indicates that fragments originating from TSP-1 switch the pro- or anti-angiogenic phenotype in endothelium by targeting MAPK cascades with opposite functions on MMP/TIMP balance [21].
  • Within the protein coding region of the bovine StAR gene, there is a marked 124 base homology to the 5' non-coding region of another luteal transcript, TIMP-1, suggesting a possible common regulatory function for this sequence [22].

Analytical, diagnostic and therapeutic context of TIMP1


  1. Modulation of bovine articular chondrocyte gene expression in vitro by oxygen tension. Grimshaw, M.J., Mason, R.M. Osteoarthr. Cartil. (2001) [Pubmed]
  2. Decreased expression of tissue inhibitor of metalloproteinase 1 in stunned myocardium. Baghelai, K., Marktanner, R., Dattilo, J.B., Dattilo, M.P., Jakoi, E.R., Yager, D.R., Makhoul, R.G., Wechsler, A.S. J. Surg. Res. (1998) [Pubmed]
  3. Retinoids modulate endothelial cell production of matrix-degrading proteases and tissue inhibitors of metalloproteinases (TIMP). Braunhut, S.J., Moses, M.A. J. Biol. Chem. (1994) [Pubmed]
  4. Effect of hypoxia and reoxygenation on gene expression and response to interleukin-1 in cultured articular chondrocytes. Martin, G., Andriamanalijaona, R., Grässel, S., Dreier, R., Mathy-Hartert, M., Bogdanowicz, P., Boumédiene, K., Henrotin, Y., Bruckner, P., Pujol, J.P. Arthritis Rheum. (2004) [Pubmed]
  5. Mechanical overload induces VEGF in cartilage discs via hypoxia-inducible factor. Pufe, T., Lemke, A., Kurz, B., Petersen, W., Tillmann, B., Grodzinsky, A.J., Mentlein, R. Am. J. Pathol. (2004) [Pubmed]
  6. Generation and characterization of aggrecanase. A soluble, cartilage-derived aggrecan-degrading activity. Arner, E.C., Pratta, M.A., Trzaskos, J.M., Decicco, C.P., Tortorella, M.D. J. Biol. Chem. (1999) [Pubmed]
  7. Examining the relationship between the gelatinolytic balance and the invasive capacity of endothelial cells. Puyraimond, A., Weitzman, J.B., Babiole, E., Menashi, S. J. Cell. Sci. (1999) [Pubmed]
  8. Retinoids and TIMP1 prevent radiation-induced apoptosis of capillary endothelial cells. Vorotnikova, E., Tries, M., Braunhut, S. Radiat. Res. (2004) [Pubmed]
  9. Tissue inhibitor of metalloproteinases (TIMP-1) produced by granulosa and oviduct cells enhances in vitro development of bovine embryo. Satoh, T., Kobayashi, K., Yamashita, S., Kikuchi, M., Sendai, Y., Hoshi, H. Biol. Reprod. (1994) [Pubmed]
  10. mRNA of bovine tissue inhibitor of metalloproteinase: sequence and expression in bovine ovarian tissue. Freudenstein, J., Wagner, S., Luck, R.M., Einspanier, R., Scheit, K.H. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  11. Expression and localization of extracellular matrix-degrading proteinases and their inhibitors in the bovine mammary gland during development, function, and involution. Rabot, A., Sinowatz, F., Berisha, B., Meyer, H.H., Schams, D. J. Dairy Sci. (2007) [Pubmed]
  12. Bovine trabecular cells produce TIMP-1 and MMP-2 in response to mechanical stretching. Okada, Y., Matsuo, T., Ohtsuki, H. Jpn. J. Ophthalmol. (1998) [Pubmed]
  13. Temporal and spatial expression of tissue inhibitors of metalloproteinases 1 and 2 (TIMP-1 and -2) in the bovine corpus luteum. Zhang, B., Moses, M.A., Tsang, P.C. Reprod. Biol. Endocrinol. (2003) [Pubmed]
  14. Replicative senescence of human skin fibroblasts correlates with a loss of regulation and overexpression of collagenase activity. West, M.D., Pereira-Smith, O.M., Smith, J.R. Exp. Cell Res. (1989) [Pubmed]
  15. Effects of non-steroidal antiinflammatory drugs and dexamethasone on the activity and expression of matrix metalloproteinase-1, matrix metalloproteinase-3 and tissue inhibitor of metalloproteinases-1 by bovine articular chondrocytes. Sadowski, T., Steinmeyer, J. Osteoarthr. Cartil. (2001) [Pubmed]
  16. Low molecular weight, sequence based, collagenase inhibitors selectively block the interaction between collagenase and TIMP (tissue inhibitor of metalloproteinases). Lelièvre, Y., Bouboutou, R., Boiziau, J., Faucher, D., Achard, D., Cartwright, T. Matrix (1990) [Pubmed]
  17. Purification and embryotropic roles of tissue inhibitor of metalloproteinase-1 in development of "HanWoo" (Bos taurus coreanae) oocytes co-cultured with bovine oviduct epithelial cells. Hwang, W., Kim, H., Lee, E., Lim, J., Roh, S., Shin, T., Hwang, K., Lee, B. J. Vet. Med. Sci. (2000) [Pubmed]
  18. Effects of polysulfated glycosaminoglycan and triamcinolone acetonid on the production of proteinases and their inhibitors by IL-1alpha treated articular chondrocytes. Sadowski, T., Steinmeyer, J. Biochem. Pharmacol. (2002) [Pubmed]
  19. Cyclic tensile strain and cyclic hydrostatic pressure differentially regulate expression of hypertrophic markers in primary chondrocytes. Wong, M., Siegrist, M., Goodwin, K. Bone (2003) [Pubmed]
  20. Interleukin-4 blocks the release of collagen fragments from bovine nasal cartilage treated with cytokines. Cawston, T.E., Ellis, A.J., Bigg, H., Curry, V., Lean, E., Ward, D. Biochim. Biophys. Acta (1996) [Pubmed]
  21. ERK1-2 and p38 MAPK regulate MMP/TIMP balance and function in response to thrombospondin-1 fragments in the microvascular endothelium. Donnini, S., Morbidelli, L., Taraboletti, G., Ziche, M. Life Sci. (2004) [Pubmed]
  22. Molecular cloning and in vivo expression of the bovine steroidogenic acute regulatory protein. Hartung, S., Rust, W., Balvers, M., Ivell, R. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  23. Identification, purification and partial characterization of tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) in bovine pulmonary artery smooth muscle. Mandal, M., Das, S., Chakraborti, T., Mandal, A., Chakraborti, S. Mol. Cell. Biochem. (2003) [Pubmed]
WikiGenes - Universities