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Gene Review

RECK  -  reversion-inducing-cysteine-rich protein...

Homo sapiens

Synonyms: Reversion-inducing cysteine-rich protein with Kazal motifs, ST15, Suppressor of tumorigenicity 15 protein, hRECK
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Disease relevance of RECK


High impact information on RECK

  • These results support a role for RECK in the regulation of MMP-2 in vivo and implicate RECK downregulation in tumor angiogenesis [3].
  • RECK regulates MMP-induced pericellular signaling cascades during embryogenesis and tumorigenesis [5].
  • Thus, RECK may link oncogenic signals to tumor invasion and metastasis [6].
  • While RECK mRNA is expressed in various human tissues and untransformed cells, it is undetectable in tumor-derived cell lines and oncogenically transformed cells [6].
  • Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK [6].

Biological context of RECK

  • Moreover, up-regulation of RECK expression by TSA attenuated MMP-2 activity [1].
  • In this study, we examined the link between glycosylation and the function of RECK in human tumor cell lines [7].
  • TIMP-2 and Ala+TIMP-2 also suppress basal hMVEC migration via a time-dependent mechanism mediated by enhanced expression of RECK, a membrane-anchored MMP inhibitor, which, in turn, inhibits cell migration [4].
  • The predicted amino acid sequence of human RECK includes five putative N-glycosylation sites; however, the precise biochemical role of glycosylated RECK remains unknown [7].
  • BACKGROUND: The reversion-inducing cysteine-rich protein with Kazal motifs (RECK) gene was initially isolated as a transformation suppressor gene [8].

Anatomical context of RECK

  • PURPOSE: RECK, a membrane-anchored regulator of matrix metalloproteinases (MMPs), is widely expressed in healthy tissue, whereas it is expressed at lower levels in many tumor-derived cell lines [2].
  • Studies in mice and cultured cells have shown that restoration of RECK expression inhibits tumor invasion, metastasis, and angiogenesis [2].
  • Tissue inhibitors of metalloproteinase 2 inhibits endothelial cell migration through increased expression of RECK [4].
  • Furthermore, expression of tissue inhibitor of metalloproteinase-1, tissue inhibitor of metalloproteinase-2, and RECK in macrophages was not affected by treatment with PGE(2), indicating the effect of PGE(2) on suppressing MMP-9 activity was not mediated by up-regulation of its inhibitor [9].
  • We also detected a significant inverse correlation between RECK expression and macroscopic tumour growth (P=0.018), lymphatic invasion (P=0.018), lymph node metastasis (P=0.000), stage (P=0.000), and MMP-9 (P=0.039) [10].

Associations of RECK with chemical compounds

  • The histone deacetylase inhibitor trichostatin A reversed HER-2/neu-induced inhibition of RECK [11].
  • TIMP-2 upregulates RECK expression via dephosphorylation of paxillin tyrosine residues 31 and 118 [12].
  • The present study investigated theoretically and experimentally the effects of increases in hematocrit on the clearance of urea by the Baxter ST15 hollow fiber dialyzer [13].

Physical interactions of RECK


Regulatory relationships of RECK

  • Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion [1].
  • Interestingly, this inverse correlation was seen only when VEGF was strongly expressed, which suggests that RECK could suppress the angiogenesis induced by VEGF [15].
  • TIMP-2-induced RECK decreases cell-associated MMP activity [4].
  • Thus, these findings indicate that glycosylation mediates RECK suppression of tumor cell invasion by multiple mechanisms such as suppressing MMP-9 secretion and inhibiting MMP-2 activation [7].
  • Recent works demonstrated that a membrane-anchored MMP inhibitor RECK may potently suppress MMP-2 and -9 activity to inhibit angiogenesis and metastasis in vitro and in vivo [16].
  • We examined whether RECK influences the behavior of MT1-MMP and CD13 during their internalization from the cell surface [17].
  • Taken together, our results suggest that the K23 motifs of RECK protein can inhibit MMP-9 secretion and activity and attenuate metastasis of lung cancer cells [18].

Other interactions of RECK

  • When artificially expressed in such cell lines, RECK negatively regulates at least matrix metalloprotease (MMP)-9, MMP-2, and MT1-MMP activation and suppresses the invasive and metastatic potentials of these cells [8].
  • Expression of RECK and vascular endothelial growth factor (VEGF) in tumour tissues was assessed by immunohistochemical staining (IHS) [15].
  • Genomic characterization of the C9orf19 gene identified five exons extending over 27.2 kb of genomic DNA, located 12 kb centromeric to the tumor suppressor RECK gene [19].
  • mRNA, and latent and active levels MMP-2 and -9 were higher in tumor tissue compared to normal tissue from 63 patients with colorectal cancer, whereas RECK and EMMPRIN levels were lower [20].
  • Third, TIMP-2 can enhance expression of RECK via Rap1 signaling resulting in an indirect, time-dependent inhibition of endothelial cell migration [4].

Analytical, diagnostic and therapeutic context of RECK


  1. Histone deacetylase inhibitor up-regulates RECK to inhibit MMP-2 activation and cancer cell invasion. Liu, L.T., Chang, H.C., Chiang, L.C., Hung, W.C. Cancer Res. (2003) [Pubmed]
  2. The membrane-anchored matrix metalloproteinase (MMP) regulator RECK in combination with MMP-9 serves as an informative prognostic indicator for colorectal cancer. Takeuchi, T., Hisanaga, M., Nagao, M., Ikeda, N., Fujii, H., Koyama, F., Mukogawa, T., Matsumoto, H., Kondo, S., Takahashi, C., Noda, M., Nakajima, Y. Clin. Cancer Res. (2004) [Pubmed]
  3. The membrane-anchored MMP inhibitor RECK is a key regulator of extracellular matrix integrity and angiogenesis. Oh, J., Takahashi, R., Kondo, S., Mizoguchi, A., Adachi, E., Sasahara, R.M., Nishimura, S., Imamura, Y., Kitayama, H., Alexander, D.B., Ide, C., Horan, T.P., Arakawa, T., Yoshida, H., Nishikawa, S., Itoh, Y., Seiki, M., Itohara, S., Takahashi, C., Noda, M. Cell (2001) [Pubmed]
  4. Tissue inhibitors of metalloproteinase 2 inhibits endothelial cell migration through increased expression of RECK. Oh, J., Seo, D.W., Diaz, T., Wei, B., Ward, Y., Ray, J.M., Morioka, Y., Shi, S., Kitayama, H., Takahashi, C., Noda, M., Stetler-Stevenson, W.G. Cancer Res. (2004) [Pubmed]
  5. RECKing MMP function: implications for cancer development. Rhee, J.S., Coussens, L.M. Trends Cell Biol. (2002) [Pubmed]
  6. Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Takahashi, C., Sheng, Z., Horan, T.P., Kitayama, H., Maki, M., Hitomi, K., Kitaura, Y., Takai, S., Sasahara, R.M., Horimoto, A., Ikawa, Y., Ratzkin, B.J., Arakawa, T., Noda, M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. RECK-mediated suppression of tumor cell invasion is regulated by glycosylation in human tumor cell lines. Simizu, S., Takagi, S., Tamura, Y., Osada, H. Cancer Res. (2005) [Pubmed]
  8. RECK expression in pancreatic cancer: its correlation with lower invasiveness and better prognosis. Masui, T., Doi, R., Koshiba, T., Fujimoto, K., Tsuji, S., Nakajima, S., Koizumi, M., Toyoda, E., Tulachan, S., Ito, D., Kami, K., Mori, T., Wada, M., Noda, M., Imamura, M. Clin. Cancer Res. (2003) [Pubmed]
  9. Suppression of matrix metalloproteinase-9 by prostaglandin E(2) in peritoneal macrophage is associated with severity of endometriosis. Wu, M.H., Shoji, Y., Wu, M.C., Chuang, P.C., Lin, C.C., Huang, M.F., Tsai, S.J. Am. J. Pathol. (2005) [Pubmed]
  10. Expression of reversion-inducing-cysteine-rich protein with Kazal motifs (RECK) as a prognostic indicator in gastric cancer. Song, S.Y., Son, H.J., Nam, E., Rhee, J.C., Park, C. Eur. J. Cancer (2006) [Pubmed]
  11. HER-2/neu represses the metastasis suppressor RECK via ERK and Sp transcription factors to promote cell invasion. Hsu, M.C., Chang, H.C., Hung, W.C. J. Biol. Chem. (2006) [Pubmed]
  12. TIMP-2 upregulates RECK expression via dephosphorylation of paxillin tyrosine residues 31 and 118. Oh, J., Diaz, T., Wei, B., Chang, H., Noda, M., Stetler-Stevenson, W.G. Oncogene (2006) [Pubmed]
  13. The impact of erythropoietin on hemodialyzer design and performance. Schmidt, B., Ward, R.A. Artificial organs. (1989) [Pubmed]
  14. Silencing of the Metastasis Suppressor RECK by RAS Oncogene Is Mediated by DNA Methyltransferase 3b-Induced Promoter Methylation. Chang, H.C., Cho, C.Y., Hung, W.C. Cancer Res. (2006) [Pubmed]
  15. Expression of a novel matrix metalloproteinase regulator, RECK, and its clinical significance in resected non-small cell lung cancer. Takenaka, K., Ishikawa, S., Kawano, Y., Yanagihara, K., Miyahara, R., Otake, Y., Morioka, Y., Takahashi, C., Noda, M., Wada, H., Tanaka, F. Eur. J. Cancer (2004) [Pubmed]
  16. Induction of RECK by nonsteroidal anti-inflammatory drugs in lung cancer cells. Liu, L.T., Chang, H.C., Chiang, L.C., Hung, W.C. Oncogene (2002) [Pubmed]
  17. The reversion-inducing cysteine-rich protein with Kazal motifs (RECK) interacts with membrane type 1 matrix metalloproteinase and CD13/aminopeptidase N and modulates their endocytic pathways. Miki, T., Takegami, Y., Okawa, K., Muraguchi, T., Noda, M., Takahashi, C. J. Biol. Chem. (2007) [Pubmed]
  18. The Kazal motifs of RECK protein inhibit MMP-9 secretion and activity and reduce metastasis of lung cancer cells in vitro and in vivo. Chang, C.K., Hung, W.C., Chang, H.C. J. Cell. Mol. Med. (2008) [Pubmed]
  19. Cloning and characterization of a human novel gene C9orf19 encoding a conserved putative protein with an SCP-like extracellular protein domain. Eisenberg, I., Barash, M., Kahan, T., Mitrani-Rosenbaum, S. Gene (2002) [Pubmed]
  20. Correlation of reversion-inducing cysteine-rich protein with kazal motifs (RECK) and extracellular matrix metalloproteinase inducer (EMMPRIN), with MMP-2, MMP-9, and survival in colorectal cancer. van der Jagt, M.F., Sweep, F.C., Waas, E.T., Hendriks, T., Ruers, T.J., Merry, A.H., Wobbes, T., Span, P.N. Cancer Lett. (2006) [Pubmed]
  21. Downregulation of the RECK-tumor and metastasis suppressor gene in glioma invasiveness. Correa, T.C., Brohem, C.A., Winnischofer, S.M., da Silva Cardeal, L.B., Sasahara, R.M., Taboga, S.R., Sogayar, M.C., Maria-Engler, S.S. J. Cell. Biochem. (2006) [Pubmed]
  22. Matrix metalloproteinase inhibitor reversion-inducing cysteine-rich protein with Kazal motifs: a prognostic marker for good clinical outcome in human breast carcinoma. Span, P.N., Sweep, C.G., Manders, P., Beex, L.V., Leppert, D., Lindberg, R.L. Cancer (2003) [Pubmed]
  23. RECK gene expression in hepatocellular carcinoma: correlation with invasion-related clinicopathological factors and its clinical significance. Reverse-inducing--cysteine-rich protein with Kazal motifs. Furumoto, K., Arii, S., Mori, A., Furuyama, H., Gorrin Rivas, M.J., Nakao, T., Isobe, N., Murata, T., Takahashi, C., Noda, M., Imamura, M. Hepatology (2001) [Pubmed]
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