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Gene Review

BIRC7  -  baculoviral IAP repeat containing 7

Homo sapiens

Synonyms: Baculoviral IAP repeat-containing protein 7, KIAP, Kidney inhibitor of apoptosis protein, LIVIN, Livin, ...
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Disease relevance of BIRC7

  • SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP) [1].
  • Expression of BIRC7 protein and mRNA in non-Hodgkin's lymphoma [2].
  • BIRC7 protein was exhibited in the cytoplasm of cells in 25 (31%) of 80 cases of B-NHLs, 32 (37%) of 87 cases of T-NHLs, and none in non-specific lymphadenitis [2].
  • However, there are no reported data concerning BIRC7 expression in lymphomas [2].
  • One member protein of the inhibitor of apoptosis protein (IAP) family, Livin, was selectively expressed in the malignant cells at higher levels, particularly in T-ALL CD4(+) T cells, in comparison with the expression in CD4 and CD8 double-positive thymocytes [3].
  • Targeted inhibition of livin could represent a novel therapeutic strategy to increase the sensitivity of renal cancers towards pro-apoptotic agents [4].

High impact information on BIRC7


Chemical compound and disease context of BIRC7

  • RESULTS: Livin cleavage was observed in multiple human melanoma cell lines in response to a variety of apoptotic stimuli (UVB, 4-TBP, cisplatin, TNF, Bax), and not affected by the addition of various protease inhibitors or RNAi-mediated silencing of Omi/HtrA2 [7].

Biological context of BIRC7


Anatomical context of BIRC7


Associations of BIRC7 with chemical compounds

  • Silencing of livin was associated with caspase-3 activation and a strongly increased apoptotic rate in response to different proapoptotic stimuli, such as doxorubicin, UV-irradiation, or TNFalpha [8].
  • In this report, we show that overexpression of KIAP blocks apoptosis induced by menadione or by overexpression of BAX [10].
  • Curcumin determined early changes in COX-2 and c-myc mRNAs, which were down-regulated, and in livin mRNA, which was up-regulated [15].
  • Dissociation constant (Kd) of VCR and apparent inhibitory constant (Kiapp) of verapamil were calculated to be 0.1 +/- 0.1 microM (SD) and 1 +/- 1 microM, respectively [16].
  • Recombinant CDK4-cyclin D1 was inhibited potently by Flavopiridol (Kiapp, 65 nM), competitive with respect to ATP [17].

Physical interactions of BIRC7


Regulatory relationships of BIRC7


Other interactions of BIRC7

  • Here we report that two other members of the IAP family, NAIP and ML-IAP, both activate JNK1 [21].
  • Only IAP-1 and livin protein was expressed in the nucleus of MPM tumours [22].
  • After stimulation with CCL25 and apoptotic induction with TNF-alpha, the expression levels of Livin in these malignant cells were significantly increased [3].
  • Levels of other IAPs were not altered in Survivin-targeted cells, although modest cleavage of XIAP and Livin was observed [23].
  • When we evaluated the dependence between each gene expression and relapse free time of patients, we found that LIVIN, high BCL-2/BAX ratio and BCL-X(L), but not SURVIVIN, reached statistical significance in order to predict relapses [24].

Analytical, diagnostic and therapeutic context of BIRC7


  1. SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP). Vucic, D., Deshayes, K., Ackerly, H., Pisabarro, M.T., Kadkhodayan, S., Fairbrother, W.J., Dixit, V.M. J. Biol. Chem. (2002) [Pubmed]
  2. Expression of BIRC7 protein and mRNA in non-Hodgkin's lymphoma. Wu, H., Ma, Y., Zhu, Y., Shen, Y., Gu, C., Ye, Z., Lin, H. Leuk. Lymphoma (2006) [Pubmed]
  3. CC chemokine ligand 25 enhances resistance to apoptosis in CD4+ T cells from patients with T-cell lineage acute and chronic lymphocytic leukemia by means of livin activation. Qiuping, Z., Jei, X., Youxin, J., Wei, J., Chun, L., Jin, W., Qun, W., Yan, L., Chunsong, H., Mingzhen, Y., Qingping, G., Kejian, Z., Zhimin, S., Qun, L., Junyan, L., Jinquan, T. Cancer Res. (2004) [Pubmed]
  4. Targeted inhibition of Livin resensitizes renal cancer cells towards apoptosis. Crnković-Mertens, I., Wagener, N., Semzow, J., Gröne, E.F., Haferkamp, A., Hohenfellner, M., Butz, K., Hoppe-Seyler, F. Cell. Mol. Life Sci. (2007) [Pubmed]
  5. Inhibition of apoptosis in normal and transformed intestinal epithelial cells by cAMP through induction of inhibitor of apoptosis protein (IAP)-2. Nishihara, H., Kizaka-Kondoh, S., Insel, P.A., Eckmann, L. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  6. Melanoma inhibitor of apoptosis protein (ML-IAP) is a target for immune-mediated tumor destruction. Schmollinger, J.C., Vonderheide, R.H., Hoar, K.M., Maecker, B., Schultze, J.L., Hodi, F.S., Soiffer, R.J., Jung, K., Kuroda, M.J., Letvin, N.L., Greenfield, E.A., Mihm, M., Kutok, J.L., Dranoff, G. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. Proteolytic cleavage of Livin (ML-IAP) in apoptotic melanoma cells potentially mediated by a non-canonical caspase. Yan, H., Brouha, B., Liu, T., Raj, D., Biddle, D., Lee, R., Grossman, D. J. Dermatol. Sci. (2006) [Pubmed]
  8. Induction of apoptosis in tumor cells by siRNA-mediated silencing of the livin/ML-IAP/KIAP gene. Crnkovic-Mertens, I., Hoppe-Seyler, F., Butz, K. Oncogene (2003) [Pubmed]
  9. The melanoma inhibitor of apoptosis protein: a target for spontaneous cytotoxic T cell responses. Andersen, M.H., Reker, S., Becker, J.C., thor Straten, P. J. Invest. Dermatol. (2004) [Pubmed]
  10. KIAP, a novel member of the inhibitor of apoptosis protein family. Lin, J.H., Deng, G., Huang, Q., Morser, J. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  11. Detection of autoantibodies to survivin and livin in sera from patients with breast cancer. Yagihashi, A., Ohmura, T., Asanuma, K., Kobayashi, D., Tsuji, N., Torigoe, T., Sato, N., Hirata, K., Watanabe, N. Clin. Chim. Acta (2005) [Pubmed]
  12. Engineering ML-IAP to produce an extraordinarily potent caspase 9 inhibitor: implications for Smac-dependent anti-apoptotic activity of ML-IAP. Vucic, D., Franklin, M.C., Wallweber, H.J., Das, K., Eckelman, B.P., Shin, H., Elliott, L.O., Kadkhodayan, S., Deshayes, K., Salvesen, G.S., Fairbrother, W.J. Biochem. J. (2005) [Pubmed]
  13. ML-IAP, a novel inhibitor of apoptosis that is preferentially expressed in human melanomas. Vucic, D., Stennicke, H.R., Pisabarro, M.T., Salvesen, G.S., Dixit, V.M. Curr. Biol. (2000) [Pubmed]
  14. Mathematical modeling of the regulation of caspase-3 activation and degradation. Stucki, J.W., Simon, H.U. J. Theor. Biol. (2005) [Pubmed]
  15. Antitumor effects of curcumin, alone or in combination with cisplatin or doxorubicin, on human hepatic cancer cells. Analysis of their possible relationship to changes in NF-kB activation levels and in IAP gene expression. Notarbartolo, M., Poma, P., Perri, D., Dusonchet, L., Cervello, M., D'Alessandro, N. Cancer Lett. (2005) [Pubmed]
  16. Competitive inhibition by verapamil of ATP-dependent high affinity vincristine binding to the plasma membrane of multidrug-resistant K562 cells without calcium ion involvement. Naito, M., Tsuruo, T. Cancer Res. (1989) [Pubmed]
  17. Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase (CDK) 2 and CDK4 in human breast carcinoma cells. Carlson, B.A., Dubay, M.M., Sausville, E.A., Brizuela, L., Worland, P.J. Cancer Res. (1996) [Pubmed]
  18. Design, synthesis, and biological activity of a potent second mitochondrial activator of caspases mimetic that sensitizes cancer cells to apoptosis by antagonizing inhibitor of apoptosis proteins. Varfolomeev, E., Zobel, K., Okawa, D.C., Wallweber, H., Franklin, M.C., Wang, L., Elliott, L.O., Fairbrother, W.J., Vucic, D., Deshayes, K., Flygare, J.A. ACS chemical biology (2006) [Pubmed]
  19. Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathway. Ma, L., Huang, Y., Song, Z., Feng, S., Tian, X., Du, W., Qiu, X., Heese, K., Wu, M. Cell Death Differ. (2006) [Pubmed]
  20. Expression of inhibitor-of-apoptosis protein (IAP) livin by neuroblastoma cells: correlation with prognostic factors and outcome. Kim, D.K., Alvarado, C.S., Abramowsky, C.R., Gu, L., Zhou, M., Soe, M.M., Sullivan, K., George, B., Schemankewitz, E., Findley, H.W. Pediatr. Dev. Pathol. (2005) [Pubmed]
  21. IAP suppression of apoptosis involves distinct mechanisms: the TAK1/JNK1 signaling cascade and caspase inhibition. Sanna, M.G., da Silva Correia, J., Ducrey, O., Lee, J., Nomoto, K., Schrantz, N., Deveraux, Q.L., Ulevitch, R.J. Mol. Cell. Biol. (2002) [Pubmed]
  22. Expression patterns of inhibitor of apoptosis proteins in malignant pleural mesothelioma. Gordon, G.J., Mani, M., Mukhopadhyay, L., Dong, L., Edenfield, H.R., Glickman, J.N., Yeap, B.Y., Sugarbaker, D.J., Bueno, R. J. Pathol. (2007) [Pubmed]
  23. Rapid induction of mitochondrial events and caspase-independent apoptosis in Survivin-targeted melanoma cells. Liu, T., Brouha, B., Grossman, D. Oncogene (2004) [Pubmed]
  24. Expression and prognostic significance of LIVIN, SURVIVIN and other apoptosis-related genes in the progression of superficial bladder cancer. Gazzaniga, P., Gradilone, A., Giuliani, L., Gandini, O., Silvestri, I., Nofroni, I., Saccani, G., Frati, L., Aglianò, A.M. Ann. Oncol. (2003) [Pubmed]
  25. Livin, a novel inhibitor of apoptosis protein family member. Kasof, G.M., Gomes, B.C. J. Biol. Chem. (2001) [Pubmed]
  26. Nuclear expression of survivin is associated with improved survival in metastatic ovarian carcinoma. Kleinberg, L., Flørenes, V.A., Silins, I., Haug, K., Trope, C.G., Nesland, J.M., Davidson, B. Cancer (2007) [Pubmed]
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