Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

RECK Glycoprotein

  • Wen-Chun Hung
Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_4990-2

Synonyms

Definition

RECK is named after its isolation, identification, and structural characteristics as a “reversion-inducing, cysteine-rich protein with Kazal motif” protein. RECK negatively regulates matrix metalloproteinases (MMPs) and plays an important role in the control of development, extracellular matrix remodeling, angiogenesis, and metastasis.

Characteristics

The RECK gene was originally isolated from a cDNA clone whose expression induces flat morphology in v-ki-RAS-transformed NIH/3T3 cells. The gene product is a 110-kDa glycoprotein, which anchors to the plasma membrane via glycosylphosphatidylinositol (GPI) modification. Several specific features are found in RECK protein. First, RECK is rich in cysteine and has a number of typical cysteine knot motifs at its N-terminal region. Second, RECK is...

Keywords

HDAC Inhibitor DNMT Inhibitor Metastasis Suppressor Gene Epigenetic Inactivation RECK Expression 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Chang HC, Cho CY, Hung WC (2006) Silencing of the metastasis suppressor RECK by RAS oncogene is mediated by DNA methyltransferase 3b-induced promoter methylation. Cancer Res 66:8413–8420CrossRefPubMedGoogle Scholar
  2. Liu LT, Chang HC, Chiang LC et al (2003) Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion. Cancer Res 63:3069–3072PubMedGoogle Scholar
  3. Oh J, Takahashi R, Kondo S et al (2001) The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis. Cell 107:789–800CrossRefPubMedGoogle Scholar
  4. Simizu S, Takagi S, Tamura Y et al (2005) RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines. Cancer Res 65:7455–7461CrossRefPubMedGoogle Scholar
  5. Takahashi C, Sheng Z, Horan TP et al (1998) Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Proc Natl Acad Sci U S A 95:13221–13226CrossRefPubMedPubMedCentralGoogle Scholar

See Also

  1. (2012) FOS. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1446. doi:10.1007/978-3-642-16483-5_2252Google Scholar
  2. (2012) Histone deacetylation. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1702. doi:10.1007/978-3-642-16483-5_2753Google Scholar
  3. (2012) Hypermethylation. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1784. doi:10.1007/978-3-642-16483-5_2910Google Scholar
  4. (2012) Knock-out mouse. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 1957. doi:10.1007/978-3-642-16483-5_3239Google Scholar
  5. (2012) Max. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 2188. doi:10.1007/978-3-642-16483-5_3565Google Scholar
  6. (2012) NIH-3T3 cells. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 2520. doi:10.1007/978-3-642-16483-5_4084Google Scholar
  7. (2012) Nude Mice. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 2584. doi:10.1007/978-3-642-16483-5_4172Google Scholar
  8. (2012) Trichostatin A. In: Schwab M (ed) Encyclopedia of cancer, 3rd edn. Springer Berlin Heidelberg, p 3783. doi:10.1007/978-3-642-16483-5_5973Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  1. 1.National Institute of Cancer ResearchNational Health Research InstitutesTainan TaiwanRepublic of China