TIMP2
TIMP metallopeptidase inhibitor 2, a tissue inhibitor of metalloproteinases, also known as TIMP2, is a human gene, thought to be a metastasis suppressor.
This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix.[1]
In melanocytic cells TIMP2 gene expression may be regulated by MITF[2].
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[edit] Interactions
TIMP2 has been shown to interact with MMP14[3] and MMP2.[4][5][6][7]
[edit] References
- ^ "Entrez Gene: TIMP2 TIMP metallopeptidase inhibitor 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7077.
- ^ Hoek KS, Schlegel NC, Eichhoff OM, et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
- ^ Zucker, S; Drews M, Conner C, Foda H D, DeClerck Y A, Langley K E, Bahou W F, Docherty A J, Cao J (Jan. 1998). "Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)". J. Biol. Chem. (UNITED STATES) 273 (2): 1216–22. doi:10.1074/jbc.273.2.1216. ISSN 0021-9258. PMID 9422789.
- ^ Morgunova, Ekaterina; Tuuttila Ari, Bergmann Ulrich, Tryggvason Karl (May. 2002). "Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (11): 7414–9. doi:10.1073/pnas.102185399. ISSN 0027-8424. PMC 124245. PMID 12032297. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=124245.
- ^ Overall, C M; Tam E, McQuibban G A, Morrison C, Wallon U M, Bigg H F, King A E, Roberts C R (Dec. 2000). "Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation". J. Biol. Chem. (UNITED STATES) 275 (50): 39497–506. doi:10.1074/jbc.M005932200. ISSN 0021-9258. PMID 10991943.
- ^ Bigg, H F; Shi Y E, Liu Y E, Steffensen B, Overall C M (Jun. 1997). "Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2". J. Biol. Chem. (UNITED STATES) 272 (24): 15496–500. doi:10.1074/jbc.272.24.15496. ISSN 0021-9258. PMID 9182583.
- ^ Kai, Heidi S-T; Butler Georgina S, Morrison Charlotte J, King Angela E, Pelman Gayle R, Overall Christopher M (Dec. 2002). "Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain". J. Biol. Chem. (United States) 277 (50): 48696–707. doi:10.1074/jbc.M209177200. ISSN 0021-9258. PMID 12374789.
[edit] Further reading
- Liotta LA, Stetler-Stevenson W, Steeg PS (1991). "Metastasis suppressor genes.". Important Adv. Oncol.: 85–100. PMID 1869284.
- Stetler-Stevenson WG, Seo DW (2005). "TIMP-2: an endogenous inhibitor of angiogenesis.". Trends in molecular medicine 11 (3): 97–103. doi:10.1016/j.molmed.2005.01.007. PMID 15760767.
[edit] External Links
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