nach oben

Cancer and Metastasis Reviews

Erschienen in:

01.12.2010 | NON-THEMATIC REVIEW

Stem cell marker olfactomedin 4: critical appraisal of its characteristics and role in tumorigenesis

verfasst von: Phulwinder K. Grover, Jennifer E. Hardingham, Adrian G. Cummins

Erschienen in: Cancer and Metastasis Reviews | Ausgabe 4/2010

Einloggen, um Zugang zu erhalten

Abstract

Olfactomedin 4 (OLFM4), a member of the olfactomedin domain-containing proteins, is a glycoprotein with molecular weight of approximately 64 kDa. The protein is a “robust marker” of Lgr5+ stem cells and has been localised to mitochondria, nuclei and cell membranes. The bulk of OLFM4 exists in a polymeric form which is held together by disulfide bonds and carbohydrate interactions. Earlier studies revealed that the protein binds to lectins and cadherins, and facilitates cell–cell adhesion. Recent data demonstrated that the protein possesses several hallmarks of carcinogenesis. OLFM4 has also been purported to be an inducible resistance factor to apoptotic stimuli such as radiation and anticancer drugs. Here, we review its synonyms and classification, gene structure, protein structure, intracellular and tissue distribution, adhesive and antiapoptotic; mitotic; migratory and cell cycle regulatory characteristics. We also critically evaluate recent advances in understanding of the transcriptional regulation of OLFM4 and its upstream signalling pathways with special emphasis on carcinogenesis and outline future perspectives in the field.

Tomarev, S. I., & Nakaya, N. (2009). Olfactomedin domain-containing proteins: possible mechanisms of action and functions in normal development and pathology. Molecular Neurobiology, 40(2), 122–138.PubMedCrossRef

Bal, R. S., & Anholt, R. R. (1993). Formation of the extracellular mucous matrix of olfactory neuroepithelium: identification of partially glycosylated and nonglycosylated precursors of olfactomedin. Biochemistry, 32(4), 1047–1053.PubMedCrossRef

Snyder, D. A., Rivers, A. M., Yokoe, H., Menco, B. P., & Anholt, R. R. (1991). Olfactomedin: purification, characterization, and localization of a novel olfactory glycoprotein. Biochemistry, 30(38), 9143–9153.PubMedCrossRef

Yokoe, H., & Anholt, R. R. (1993). Molecular cloning of olfactomedin, an extracellular matrix protein specific to olfactory neuroepithelium. Proceedings of the National Academy of Sciences of the United States of America, 90(10), 4655–4659.PubMedCrossRef

Clevers, H. (2006). Wnt/[beta]-catenin signaling in development and disease. Cell, 127(3), 469–480.PubMedCrossRef

Croce, J. C., & McClay, D. R. (2008). Evolution of the Wnt pathways. Methods in Molecular Biology, 469, 3–18.PubMedCrossRef

Gregorieff, A., Pinto, D., Begthel, H., Destree, O., Kielman, M., & Clevers, H. (2005). Expression pattern of Wnt signaling components in the adult intestine. Gastroenterology, 129(2), 626–638.PubMed

MacDonald, B. T., Tamai, K., & He, X. (2009). Wnt/beta-catenin signaling: components, mechanisms, and diseases. Developmental Cell, 17(1), 9–26.PubMedCrossRef

Johnson, D. H. (2000). Myocilin and glaucoma: a TIGR by the tail? Archives of Ophthalmology, 118(7), 974–978.PubMed

10.

Resch, Z. T., & Fautsch, M. P. (2009). Glaucoma-associated myocilin: a better understanding but much more to learn. Experimental Eye Research, 88(4), 704–712.PubMedCrossRef

11.

Tamm, E. R. (2002). Myocilin and glaucoma: facts and ideas. Progress in Retinal and Eye Research, 21(4), 395–428.PubMedCrossRef

12.

Adam, M. F., Belmouden, A., Binisti, P., Brezin, A. P., Valtot, F., Bechetoille, A., et al. (1997). Recurrent mutations in a single exon encoding the evolutionarily conserved olfactomedin-homology domain of tigr in familial open-angle glaucoma. Human Molecular Genetics, 6(12), 2091–2097.PubMedCrossRef

13.

Fingert, J. H., Heon, E., Liebmann, J. M., Yamamoto, T., Craig, J. E., Rait, J., et al. (1999). Analysis of myocilin mutations in 1,703 glaucoma patients from five different populations. Human Molecular Genetics, 8(5), 899–905.PubMedCrossRef

14.

Fingert, J. H., Stone, E. M., Sheffield, V. C., & Alward, W. L. (2002). Myocilin glaucoma. Survey of Ophthalmology, 47(6), 547–561.PubMedCrossRef

15.

Kwon, H. S., Lee, H. S., Ji, Y., Rubin, J. S., & Tomarev, S. I. (2009). Myocilin is a modulator of Wnt signaling. Molecular and Cellular Biology, 29(8), 2139–2154.PubMedCrossRef

16.

Kwon, Y. H., Fingert, J. H., Kuehn, M. H., & Alward, W. L. (2009). Primary open-angle glaucoma. The New England Journal of Medicine, 360(11), 1113–1124.PubMedCrossRef

17.

Stone, E. M., Fingert, J. H., Alward, W. L., Nguyen, T. D., Polansky, J. R., Sunden, S. L., et al. (1997). Identification of a gene that causes primary open angle glaucoma. Science, 275(5300), 668–670.PubMedCrossRef

18.

Hillier, B. J., & Vacquier, V. D. (2003). Amassin, an olfactomedin protein, mediates the massive intercellular adhesion of sea urchin coelomocytes. The Journal of Cell Biology, 160(4), 597–604.PubMedCrossRef

19.

Karavanich, C. A., & Anholt, R. R. (1998). Molecular evolution of olfactomedin. Molecular Biology and Evolution, 15(6), 718–726.PubMed

20.

Kulkarni, N. H., Karavanich, C. A., Atchley, W. R., & Anholt, R. R. (2000). Characterization and differential expression of a human gene family of olfactomedin-related proteins. Genetical Research, 76(1), 41–50.PubMedCrossRef

21.

Loria, P. M., Hodgkin, J., & Hobert, O. (2004). A conserved postsynaptic transmembrane protein affecting neuromuscular signaling in Caenorhabditis elegans. The Journal of Neuroscience, 24(9), 2191–2201.PubMedCrossRef

22.

Meyer, E., Aglyamova, G. V., Wang, S., Buchanan-Carter, J., Abrego, D., Colbourne, J. K., et al. (2009). Sequencing and de novo analysis of a coral larval transcriptome using 454 GSFLx. BMC Genomics, 10, 219.PubMedCrossRef

23.

Zeng, L. C., Han, Z. G., & Ma, W. J. (2005). Elucidation of subfamily segregation and intramolecular coevolution of the olfactomedin-like proteins by comprehensive phylogenetic analysis and gene expression pattern assessment. FEBS Letters, 579(25), 5443–5453.PubMedCrossRef

24.

Hillier, B. J., Moy, G. W., & Vacquier, V. D. (2007). Diversity of olfactomedin proteins in the sea urchin. Genomics, 89(6), 721–730.PubMedCrossRef

25.

Mukhopadhyay, A., Talukdar, S., Bhattacharjee, A., & Ray, K. (2004). Bioinformatic approaches for identification and characterization of olfactomedin related genes with a potential role in pathogenesis of ocular disorders. Molecular Vision, 10, 304–314.PubMed

26.

van der Flier, L. G., Haegebarth, A., Stange, D. E., van de Wetering, M., & Clevers, H. (2009). Olfm4 is a robust marker for stem cells in human intestine and marks a subset of colorectal cancer cells. Gastroenterology, 137(1), 15–17.PubMedCrossRef

27.

van der Flier, L. G., van Gijn, M. E., Hatzis, P., Kujala, P., Haegebarth, A., Stange, D. E., et al. (2009). Transcription factor achaete scute-like 2 controls intestinal stem cell fate. Cell, 136(5), 903–912.PubMedCrossRef

28.

Barker, N., & Clevers, H. (2010). Leucine-rich repeat-containing G-protein-coupled receptors as markers of adult stem cells. Gastroenterology, 138(5), 1681–1696.PubMedCrossRef

29.

Barker, N., Ridgway, R. A., van Es, J. H., van de Wetering, M., Begthel, H., van den Born, M., et al. (2009). Crypt stem cells as the cells-of-origin of intestinal cancer. Nature, 457(7229), 608–611.PubMedCrossRef

30.

Boman, B. M., & Wicha, M. S. (2008). Cancer stem cells: a step toward the cure. Journal of Clinical Oncology, 26(17), 2795–2799.PubMedCrossRef

31.

Dalerba, P., Cho, R. W., & Clarke, M. F. (2007). Cancer stem cells: models and concepts. Annual Review of Medicine, 58, 267–284.PubMedCrossRef

32.

Jordan, C. T., Guzman, M. L., & Noble, M. (2006). Cancer stem cells. The New England Journal of Medicine, 355(12), 1253–1261.PubMedCrossRef

33.

Reya, T., Morrison, S. J., Clarke, M. F., & Weissman, I. L. (2001). Stem cells, cancer, and cancer stem cells. Nature, 414(6859), 105–111.PubMedCrossRef

34.

Rosenbauer, F., Wagner, K., Zhang, P., Knobeloch, K. P., Iwama, A., & Tenen, D. G. (2004). pDP4, a novel glycoprotein secreted by mature granulocytes, is regulated by transcription factor PU.1. Blood, 103(11), 4294–4301.PubMedCrossRef

35.

Shinozaki, S., Nakamura, T., Iimura, M., Kato, Y., Iizuka, B., Kobayashi, M., et al. (2001). Upregulation of Reg 1alpha and GW112 in the epithelium of inflamed colonic mucosa. Gut, 48(5), 623–629.PubMedCrossRef

36.

Zhang, J., Liu, W. L., Tang, D. C., Chen, L., Wang, M., Pack, S. D., et al. (2002). Identification and characterization of a novel member of olfactomedin-related protein family, hGC-1, expressed during myeloid lineage development. Gene, 283(1–2), 83–93.PubMedCrossRef

37.

Zhang, X., Huang, Q., Yang, Z., Li, Y., & Li, C. Y. (2004). Gw112, a novel antiapoptotic protein that promotes tumor growth. Cancer Research, 64(7), 2474–2481.PubMedCrossRef

38.

Liu, W., Chen, L., Zhu, J., & Rodgers, G. P. (2006). The glycoprotein hGC-1 binds to cadherin and lectins. Experimental Cell Research, 312(10), 1785–1797.PubMedCrossRef

39.

Fautsch, M. P., & Johnson, D. H. (2001). Characterization of myocilin–myocilin interactions. Invest Ophthalmol Vis Sci, 42(10), 2324–2331.PubMed

40.

Chin, K. L., Aerbajinai, W., Zhu, J., Drew, L., Chen, L., Liu, W., et al. (2008). The regulation of OLFM4 expression in myeloid precursor cells relies on NF-kappaB transcription factor. British Journal Haematology, 143(3), 421–432.CrossRef

41.

Kim, K. K., Park, K. S., Song, S. B., & Kim, K. E. (2010). Up regulation of GW112 gene by NF kappaB promotes an antiapoptotic property in gastric cancer cells. Molecular Carcinogenesis, 49(3), 259–270.PubMed

42.

Ayoubi, T. A., & Van De Ven, W. J. (1996). Regulation of gene expression by alternative promoters. The FASEB Journal, 10(4), 453–460.PubMed

43.

Baek, D., Davis, C., Ewing, B., Gordon, D., & Green, P. (2007). Characterization and predictive discovery of evolutionarily conserved mammalian alternative promoters. Genome Research, 17(2), 145–155.PubMedCrossRef

44.

Davuluri, R. V., Suzuki, Y., Sugano, S., Plass, C., & Huang, T. H. (2008). The functional consequences of alternative promoter use in mammalian genomes. Trends in Genetics, 24(4), 167–177.PubMedCrossRef

45.

Burke, T. W., & Kadonaga, J. T. (1997). The downstream core promoter element, DPE, is conserved from Drosophila to humans and is recognized by TAFII60 of Drosophila. Genes & Development, 11(22), 3020–3031.CrossRef

46.

Deng, W., & Roberts, S. G. (2005). A core promoter element downstream of the TATA box that is recognized by TFIIB. Genes & Development, 19(20), 2418–2423.CrossRef

47.

Lee, D. H., Gershenzon, N., Gupta, M., Ioshikhes, I. P., Reinberg, D., & Lewis, B. A. (2005). Functional characterization of core promoter elements: the downstream core element is recognized by TAF1. Molecular and Cellular Biology, 25(21), 9674–9686.PubMedCrossRef

48.

Smale, S. T., & Kadonaga, J. T. (2003). The RNA polymerase II core promoter. Annual Review of Biochemistry, 72, 449–479.PubMedCrossRef

49.

Liu, W., Yan, M., Liu, Y., Wang, R., Li, C., Deng, C., et al. (2010). Olfactomedin 4 down-regulates innate immunity against Helicobacter pylori infection. Proceedings of the National Academy of Sciences of the United States of America, 107(24), 11056–11061.PubMedCrossRef

50.

Finkel, T. (2000). Redox-dependent signal transduction. FEBS Letters, 476(1–2), 52–54.PubMedCrossRef

51.

Halliwell, B. (2003). Oxidative stress in cell culture: an under-appreciated problem? FEBS Letters, 540(1–3), 3–6.PubMedCrossRef

52.

Torres, M., & Forman, H. J. (2003). Redox signaling and the map kinase pathways. Biofactors, 17(1–4), 287–296.PubMedCrossRef

53.

Duarte, R. F., & Frank, D. A. (2000). SCF and G-CSF lead to the synergistic induction of proliferation and gene expression through complementary signaling pathways. Blood, 96(10), 3422–3430.PubMed

54.

Meplan, C., Richard, M. J., & Hainaut, P. (2000). Redox signalling and transition metals in the control of the p53 pathway. Biochemical Pharmacology, 59(1), 25–33.PubMedCrossRef

55.

Rahman, I., Marwick, J., & Kirkham, P. (2004). Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression. Biochemical Pharmacology, 68(6), 1255–1267.PubMedCrossRef

56.

Rao, G. N., Katki, K. A., Madamanchi, N. R., Wu, Y., & Birrer, M. J. (1999). JunB forms the majority of the AP-1 complex and is a target for redox regulation by receptor tyrosine kinase and G protein-coupled receptor agonists in smooth muscle cells. The Journal of Biological Chemistry, 274(9), 6003–6010.PubMedCrossRef

57.

Renner, F., & Schmitz, M. L. (2009). Autoregulatory feedback loops terminating the NF-kappaB response. Trends in Biochemical Sciences, 34(3), 128–135.PubMedCrossRef

58.

Eichbaum, Q. G., Iyer, R., Raveh, D. P., Mathieu, C., & Ezekowitz, R. A. (1994). Restriction of interferon gamma responsiveness and basal expression of the myeloid human Fc gamma R1b gene is mediated by a functional PU.1 site and a transcription initiator consensus. The Journal of Experimental Medicine, 179(6), 1985–1996.PubMedCrossRef

59.

Hagemeier, C., Bannister, A. J., Cook, A., & Kouzarides, T. (1993). The activation domain of transcription factor PU.1 binds the retinoblastoma (RB) protein and the transcription factor TFIID in vitro: Rb shows sequence similarity to TFIID and TFIIB. Proceedings of the National Academy of Sciences of the United States of America, 90(4), 1580–1584.PubMedCrossRef

60.

Tenen, D. G., Hromas, R., Licht, J. D., & Zhang, D. E. (1997). Transcription factors, normal myeloid development, and leukemia. Blood, 90(2), 489–519.PubMed

61.

Weintraub, S. J., Chow, K. N., Luo, R. X., Zhang, S. H., He, S., & Dean, D. C. (1995). Mechanism of active transcriptional repression by the retinoblastoma protein. Nature, 375(6534), 812–815.PubMedCrossRef

62.

Inoue, J., Gohda, J., Akiyama, T., & Semba, K. (2007). Nf-kappab activation in development and progression of cancer. Cancer Science, 98(3), 268–274.PubMedCrossRef

63.

Van Waes, C. (2007). Nuclear factor-kappaB in development, prevention, and therapy of cancer. Clinical Cancer Research, 13(4), 1076–1082.PubMedCrossRef

64.

Shaulian, E., & Karin, M. (2001). Ap-1 in cell proliferation and survival. Oncogene, 20(19), 2390–2400.PubMedCrossRef

65.

Vesely, P. W., Staber, P. B., Hoefler, G., & Kenner, L. (2009). Translational regulation mechanisms of AP-1 proteins. Mutation Research, 682(1), 7–12.PubMedCrossRef

66.

Gupta, P., Gurudutta, G. U., Verma, Y. K., Kishore, V., Gulati, S., Sharma, R. K., et al. (2006). PU. 1: an ETS family transcription factor that regulates leukemogenesis besides normal hematopoiesis. Stem Cells and Development, 15(4), 609–617.PubMedCrossRef

67.

Kastner, P., & Chan, S. (2008). PU. 1: a crucial and versatile player in hematopoiesis and leukemia. The International Journal of Biochemistry & Cell Biology, 40(1), 22–27.CrossRef

68.

Baud, V., & Karin, M. (2009). Is NF-kappaB a good target for cancer therapy? Hopes and pitfalls. Nature Reviews. Drug Discovery, 8(1), 33–40.PubMedCrossRef

69.

Choe, K. S., Ujhelly, O., Wontakal, S. N., & Skoultchi, A. I. (2010). PU. 1 directly regulates cdk6 gene expression, linking the cell proliferation and differentiation programs in erythroid cells. The Journal of Biological Chemistry, 285(5), 3044–3052.PubMedCrossRef

70.

Eferl, R., & Wagner, E. F. (2003). AP-1: a double-edged sword in tumorigenesis. Nature Reviews. Cancer, 3(11), 859–868.PubMedCrossRef

71.

Lee, C. H., Jeon, Y. T., Kim, S. H., & Song, Y. S. (2007). Nf-kappaB as a potential molecular target for cancer therapy. Biofactors, 29(1), 19–35.PubMedCrossRef

72.

Verde, P., Casalino, L., Talotta, F., Yaniv, M., & Weitzman, J. B. (2007). Deciphering AP-1 function in tumorigenesis: fraternizing on target promoters. Cell Cycle, 6(21), 2633–2639.PubMedCrossRef

73.

Bonadies, N., Neururer, C., Steege, A., Vallabhapurapu, S., Pabst, T., & Mueller, B. U. (2010). PU. 1 is regulated by NF-kappaB through a novel binding site in a 17 kb upstream enhancer element. Oncogene, 29(7), 1062–1072.PubMedCrossRef

74.

Basseres, D. S., & Baldwin, A. S. (2006). Nuclear factor-kappaB and inhibitor of kappaB kinase pathways in oncogenic initiation and progression. Oncogene, 25(51), 6817–6830.PubMedCrossRef

75.

Fan, X. M., Wong, B. C., Wang, W. P., Zhou, X. M., Cho, C. H., Yuen, S. T., et al. (2001). Inhibition of proteasome function induced apoptosis in gastric cancer. International Journal of Cancer, 93(4), 481–488.CrossRef

76.

Nakanishi, C., & Toi, M. (2005). Nuclear factor-kappaB inhibitors as sensitizers to anticancer drugs. Nature Reviews. Cancer, 5(4), 297–309.PubMedCrossRef

77.

Nakshatri, H., Bhat-Nakshatri, P., Martin, D. A., Goulet, R. J., Jr., & Sledge, G. W., Jr. (1997). Constitutive activation of NF-kappaB during progression of breast cancer to hormone-independent growth. Molecular and Cellular Biology, 17(7), 3629–3639.PubMed

78.

Pacifico, F., & Leonardi, A. (2006). NF-kappaB in solid tumors. Biochemical Pharmacology, 72(9), 1142–1152.PubMedCrossRef

79.

Bernard, D., Monte, D., Vandenbunder, B., & Abbadie, C. (2002). The c-Rel transcription factor can both induce and inhibit apoptosis in the same cells via the upregulation of MnSOD. Oncogene, 21(28), 4392–4402.PubMedCrossRef

80.

Kaltschmidt, B., Kaltschmidt, C., Hofmann, T. G., Hehner, S. P., Droge, W., & Schmitz, M. L. (2000). The pro- or anti-apoptotic function of NF-kappaB is determined by the nature of the apoptotic stimulus. European Journal of Biochemistry, 267(12), 3828–3835.PubMedCrossRef

81.

Sheehy, A. M., & Schlissel, M. S. (1999). Overexpression of RelA causes G1 arrest and apoptosis in a pro-B cell line. The Journal of Biological Chemistry, 274(13), 8708–8716.PubMedCrossRef

82.

Tarabin, V., & Schwaninger, M. (2004). The role of NF-kappaB in 6-hydroxydopamine- and TNFalpha-induced apoptosis of PC12 cells. Naunyn-Schmiedebergs Archives of Pharmacology, 369(6), 563–569.CrossRef

83.

Chen, F., & Castranova, V. (2007). Nuclear factor-kappaB, an unappreciated tumor suppressor. Cancer Research, 67(23), 11093–11098.PubMedCrossRef

84.

Karin, M. (2006). Nuclear factor-kappaB in cancer development and progression. Nature, 441(7092), 431–436.PubMedCrossRef

85.

Liu, W., Liu, Y., Zhu, J., Wright, E., Ding, I., & Rodgers, G. P. (2008). Reduced hGC-1 protein expression is associated with malignant progression of colon carcinoma. Clinical Cancer Research, 14(4), 1041–1049.PubMedCrossRef

86.

Conrotto, P., Roesli, C., Rybak, J., Kischel, P., Waltregny, D., Neri, D., et al. (2008). Identification of new accessible tumor antigens in human colon cancer by ex vivo protein biotinylation and comparative mass spectrometry analysis. International Journal of Cancer, 123(12), 2856–2864.CrossRef

87.

Oue, N., Sentani, K., Noguchi, T., Ohara, S., Sakamoto, N., Hayashi, T., et al. (2009). Serum olfactomedin 4 (GW112, hGC-1) in combination with Reg IV is a highly sensitive biomarker for gastric cancer patients. International Journal of Cancer, 125(10), 2383–2392.CrossRef

88.

Liu, W., Zhu, J., Cao, L., & Rodgers, G. P. (2007). Expression of hGC-1 is correlated with differentiation of gastric carcinoma. Histopathology, 51(2), 157–165.PubMedCrossRef

89.

Duband, J. L., Dufour, S., Hatta, K., Takeichi, M., Edelman, G. M., & Thiery, J. P. (1987). Adhesion molecules during somitogenesis in the avian embryo. The Journal of Cell Biology, 104(5), 1361–1374.PubMedCrossRef

90.

Nelson, W. J. (2008). Regulation of cell–cell adhesion by the cadherin–catenin complex. Biochemical Society Transactions, 36(Pt 2), 149–155.PubMedCrossRef

91.

Takeichi, M. (1991). Cadherin cell adhesion receptors as a morphogenetic regulator. Science, 251(5000), 1451–1455.PubMedCrossRef

92.

Takeichi, M. (1995). Morphogenetic roles of classic cadherins. Current Opinion in Cell Biology, 7(5), 619–627.PubMedCrossRef

93.

Makrilia, N., Kollias, A., Manolopoulos, L., & Syrigos, K. (2009). Cell adhesion molecules: role and clinical significance in cancer. Cancer Investigation, 27(10), 1023–1037.PubMedCrossRef

94.

Paschos, K. A., Canovas, D., & Bird, N. C. (2009). The role of cell adhesion molecules in the progression of colorectal cancer and the development of liver metastasis. Cellular Signalling, 21(5), 665–674.PubMedCrossRef

95.

Cavallaro, U., & Christofori, G. (2004). Cell adhesion and signalling by cadherins and Ig-CAMS in cancer. Nature Reviews. Cancer, 4(2), 118–132.PubMed

96.

Angell, J. E., Lindner, D. J., Shapiro, P. S., Hofmann, E. R., & Kalvakolanu, D. V. (2000). Identification of GRIM-19, a novel cell death-regulatory gene induced by the interferon-beta and retinoic acid combination, using a genetic approach. The Journal of Biological Chemistry, 275(43), 33416–33426.PubMedCrossRef

97.

Chidambaram, N. V., Angell, J. E., Ling, W., Hofmann, E. R., & Kalvakolanu, D. V. (2000). Chromosomal localization of human GRIM-19, a novel IFN-beta and retinoic acid-activated regulator of cell death. Journal of Interferon & Cytokine Research, 20(7), 661–665.CrossRef

98.

Fearnley, I. M., Carroll, J., Shannon, R. J., Runswick, M. J., Walker, J. E., & Hirst, J. (2001). GRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I). The Journal of Biological Chemistry, 276(42), 38345–38348.PubMedCrossRef

99.

Lufei, C., Ma, J., Huang, G., Zhang, T., Novotny-Diermayr, V., Ong, C. T., et al. (2003). GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interaction. The EMBO Journal, 22(6), 1325–1335.PubMedCrossRef

100.

Seo, T., Lee, D., Shim, Y. S., Angell, J. E., Chidambaram, N. V., Kalvakolanu, D. V., et al. (2002). Viral interferon regulatory factor 1 of Kaposi’s sarcoma-associated herpesvirus interacts with a cell death regulator, GRIM19, and inhibits interferon/retinoic acid-induced cell death. Journal of Virology, 76(17), 8797–8807.PubMedCrossRef

101.

Liu, X., Kim, C. N., Yang, J., Jemmerson, R., & Wang, X. (1996). Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell, 86(1), 147–157.PubMedCrossRef

102.

Luo, X., Budihardjo, I., Zou, H., Slaughter, C., & Wang, X. (1998). Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell, 94(4), 481–490.PubMedCrossRef

103.

Yang, J., Liu, X., Bhalla, K., Kim, C. N., Ibrado, A. M., Cai, J., et al. (1997). Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science, 275(5303), 1129–1132.PubMedCrossRef

104.

Yin, X. M., Wang, K., Gross, A., Zhao, Y., Zinkel, S., Klocke, B., et al. (1999). Bid-deficient mice are resistant to Fas-induced hepatocellular apoptosis. Nature, 400(6747), 886–891.PubMedCrossRef

105.

Maytin, E. V., Ubeda, M., Lin, J. C., & Habener, J. F. (2001). Stress-inducible transcription factor CHOP/GADD153 induces apoptosis in mammalian cells via p38 kinase-dependent and -independent mechanisms. Experimental Cell Research, 267(2), 193–204.PubMedCrossRef

106.

Polyak, K., Xia, Y., Zweier, J. L., Kinzler, K. W., & Vogelstein, B. (1997). A model for p53-induced apoptosis. Nature, 389(6648), 300–305.PubMedCrossRef

107.

Sun, X., Majumder, P., Shioya, H., Wu, F., Kumar, S., Weichselbaum, R., et al. (2000). Activation of the cytoplasmic c-Abl tyrosine kinase by reactive oxygen species. The Journal of Biological Chemistry, 275(23), 17237–17240.PubMedCrossRef

108.

Kobayashi, D., Koshida, S., Moriai, R., Tsuji, N., & Watanabe, N. (2007). Olfactomedin 4 promotes s-phase transition in proliferation of pancreatic cancer cells. Cancer Science, 98(3), 334–340.PubMedCrossRef

109.

Koshida, S., Kobayashi, D., Moriai, R., Tsuji, N., & Watanabe, N. (2007). Specific overexpression of OLFM4(GW112/hGC-1) mrna in colon, breast and lung cancer tissues detected using quantitative analysis. Cancer Science, 98(3), 315–320.PubMedCrossRef

110.

Semenza, G. L. (2000). Hypoxia, clonal selection, and the role of HIF-1 in tumor progression. Critical Reviews in Biochemistry and Molecular Biology, 35(2), 71–103.PubMedCrossRef

111.

Tannock, I. F., & Rotin, D. (1989). Acid pH in tumors and its potential for therapeutic exploitation. Cancer Research, 49(16), 4373–4384.PubMed

112.

Stratford, I. J., Adams, G. E., Bremner, J. C., Cole, S., Edwards, H. S., Robertson, N., et al. (1994). Manipulation and exploitation of the tumour environment for therapeutic benefit. International Journal of Radiation Biology, 65(1), 85–94.PubMedCrossRef

113.

Xiao, Z., Xue, J., Sowin, T. J., Rosenberg, S. H., & Zhang, H. (2005). A novel mechanism of checkpoint abrogation conferred by Chk1 downregulation. Oncogene, 24(8), 1403–1411.PubMedCrossRef

114.

Liang, J., & Slingerland, J. M. (2003). Multiple roles of the PI3K/PKB (Akt) pathway in cell cycle progression. Cell Cycle, 2(4), 339–345.PubMed

115.

Asanuma, H., Torigoe, T., Kamiguchi, K., Hirohashi, Y., Ohmura, T., Hirata, K., et al. (2005). Survivin expression is regulated by coexpression of human epidermal growth factor receptor 2 and epidermal growth factor receptor via phosphatidylinositol 3-kinase/AKT signaling pathway in breast cancer cells. Cancer Research, 65(23), 11018–11025.PubMedCrossRef

116.

Beltrami, E., Plescia, J., Wilkinson, J. C., Duckett, C. S., & Altieri, D. C. (2004). Acute ablation of survivin uncovers p53-dependent mitotic checkpoint functions and control of mitochondrial apoptosis. The Journal of Biological Chemistry, 279(3), 2077–2084.PubMedCrossRef

117.

Hu, P., Han, Z., Couvillon, A. D., & Exton, J. H. (2004). Critical role of endogenous Akt/IAPS and MEK1/ERK pathways in counteracting endoplasmic reticulum stress-induced cell death. The Journal of Biological Chemistry, 279(47), 49420–49429.PubMedCrossRef

118.

Johnson, N. C., Dan, H. C., Cheng, J. Q., & Kruk, P. A. (2004). BRCA1 185delAG mutation inhibits AKT-dependent, IAP-mediated caspase 3 inactivation in human ovarian surface epithelial cells. Experimental Cell Research, 298(1), 9–16.PubMedCrossRef

119.

Li, F., Ambrosini, G., Chu, E. Y., Plescia, J., Tognin, S., Marchisio, P. C., et al. (1998). Control of apoptosis and mitotic spindle checkpoint by survivin. Nature, 396(6711), 580–584.PubMedCrossRef

120.

Samuel, T., Okada, K., Hyer, M., Welsh, K., Zapata, J. M., & Reed, J. C. (2005). CIAP1 localizes to the nuclear compartment and modulates the cell cycle. Cancer Research, 65(1), 210–218.PubMed

121.

Sommer, K. W., Schamberger, C. J., Schmidt, G. E., Sasgary, S., & Cerni, C. (2003). Inhibitor of apoptosis protein (IAP) survivin is upregulated by oncogenic c-H-Ras. Oncogene, 22(27), 4266–4280.PubMedCrossRef

122.

Nakaya, N., Lee, H. S., Takada, Y., Tzchori, I., & Tomarev, S. I. (2008). Zebrafish olfactomedin 1 regulates retinal axon elongation in vivo and is a modulator of Wnt signaling pathway. The Journal of Neuroscience, 28(31), 7900–7910.PubMedCrossRef

123.

Logan, C. Y., & Nusse, R. (2004). The Wnt signaling pathway in development and disease. Annual Review of Cell and Developmental Biology, 20, 781–810.PubMedCrossRef

124.

van Amerongen, R., & Nusse, R. (2009). Towards an integrated view of Wnt signaling in development. Development, 136(19), 3205–3214.PubMedCrossRef

125.

Mannick, E. E., Schurr, J. R., Zapata, A., Lentz, J. J., Gastanaduy, M., Cote, R. L., et al. (2004). Gene expression in gastric biopsies from patients infected with Helicobacter pylori. Scandinavian Journal of Gastroenterology, 39(12), 1192–1200.PubMedCrossRef

126.

Aung, P. P., Oue, N., Mitani, Y., Nakayama, H., Yoshida, K., Noguchi, T., et al. (2006). Systematic search for gastric cancer-specific genes based on sage data: melanoma inhibitory activity and matrix metalloproteinase-10 are novel prognostic factors in patients with gastric cancer. Oncogene, 25(17), 2546–2557.PubMedCrossRef

127.

Oue, N., Aung, P. P., Mitani, Y., Kuniyasu, H., Nakayama, H., & Yasui, W. (2005). Genes involved in invasion and metastasis of gastric cancer identified by array-based hybridization and serial analysis of gene expression. Oncology, 69(Suppl 1), 17–22.PubMedCrossRef

128.

Yasui, W., Oue, N., Aung, P. P., Matsumura, S., Shutoh, M., & Nakayama, H. (2005). Molecular-pathological prognostic factors of gastric cancer: a review. Gastric Cancer, 8(2), 86–94.PubMedCrossRef

129.

Grutzmann, R., Pilarsky, C., Staub, E., Schmitt, A. O., Foerder, M., Specht, T., et al. (2003). Systematic isolation of genes differentially expressed in normal and cancerous tissue of the pancreas. Pancreatology, 3(2), 169–178.PubMedCrossRef

130.

Wentzensen, N., Wilz, B., Findeisen, P., Wagner, R., Dippold, W., von Knebel Doeberitz, M., et al. (2004). Identification of differentially expressed genes in colorectal adenoma compared to normal tissue by suppression subtractive hybridization. International Journal of Oncology, 24(4), 987–994.PubMed

131.

Li, S. R., Dorudi, S., & Bustin, S. A. (2003). Identification of differentially expressed genes associated with colorectal cancer liver metastasis. European Surgical Research, 35(4), 327–336.PubMedCrossRef

132.

Barker, N., & Clevers, H. (2007). Tracking down the stem cells of the intestine: strategies to identify adult stem cells. Gastroenterology, 133(6), 1755–1760.PubMedCrossRef

133.

Barker, N., van Es, J. H., Kuipers, J., Kujala, P., van den Born, M., Cozijnsen, M., et al. (2007). Identification of stem cells in small intestine and colon by marker gene Lgr5. Nature, 449(7165), 1003–1007.PubMedCrossRef

134.

Barker, N., van de Wetering, M., & Clevers, H. (2008). The intestinal stem cell. Genes & Development, 22(14), 1856–1864.CrossRef

135.

Potten, C. S. (1977). Extreme sensitivity of some intestinal crypt cells to X and gamma irradiation. Nature, 269(5628), 518–521.PubMedCrossRef

136.

Potten, C. S., Kovacs, L., & Hamilton, E. (1974). Continuous labelling studies on mouse skin and intestine. Cell and Tissue Kinetics, 7(3), 271–283.PubMed

137.

Sangiorgi, E., & Capecchi, M. R. (2008). Bmi1 is expressed in vivo in intestinal stem cells. Nature Genetics, 40(7), 915–920.PubMedCrossRef

138.

Kosinski, C., Li, V. S., Chan, A. S., Zhang, J., Ho, C., Tsui, W. Y., et al. (2007). Gene expression patterns of human colon tops and basal crypts and bmp antagonists as intestinal stem cell niche factors. Proceedings of the National Academy of Sciences of the United States of America, 104(39), 15418–15423.PubMedCrossRef

139.

Dalerba, P., Dylla, S. J., Park, I. K., Liu, R., Wang, X., Cho, R. W., et al. (2007). Phenotypic characterization of human colorectal cancer stem cells. Proceedings of the National Academy of Sciences of the United States of America, 104(24), 10158–10163.PubMedCrossRef

140.

O’Brien, C. A., Pollett, A., Gallinger, S., & Dick, J. E. (2007). A human colon cancer cell capable of initiating tumour growth in immunodeficient mice. Nature, 445(7123), 106–110.PubMedCrossRef

141.

Ricci-Vitiani, L., Lombardi, D. G., Pilozzi, E., Biffoni, M., Todaro, M., Peschle, C., et al. (2007). Identification and expansion of human colon-cancer-initiating cells. Nature, 445(7123), 111–115.PubMedCrossRef

142.

Vermeulen, L., Todaro, M., de Sousa Mello, F., Sprick, M. R., Kemper, K., Perez Alea, M., et al. (2008). Single-cell cloning of colon cancer stem cells reveals a multi-lineage differentiation capacity. Proceedings of the National Academy of Sciences of the United States of America, 105(36), 13427–13432.PubMedCrossRef

Titel: Stem cell marker olfactomedin 4: critical appraisal of its characteristics and role in tumorigenesis
verfasst von: Phulwinder K. Grover
Jennifer E. Hardingham
Adrian G. Cummins
Publikationsdatum: 01.12.2010
Verlag: Springer US
Erschienen in: Cancer and Metastasis Reviews / Ausgabe 4/2010
Print ISSN: 0167-7659
Elektronische ISSN: 1573-7233
DOI: https://doi.org/10.1007/s10555-010-9262-z

Neu im Fachgebiet Onkologie

24.04.2024 | DGIM 2024 | Nachrichten

Springer Medizin

Stem cell marker olfactomedin 4: critical appraisal of its characteristics and role in tumorigenesis

Abstract

Neu im Fachgebiet Onkologie

Bei Senioren mit Prostatakarzinom auf Anämie achten!

ICI-Therapie in der Schwangerschaft wird gut toleriert

Krebspatienten impfen: Was? Wen? Und wann nicht?

Müde im Alter? Auch an die Nebenniere denken

Update Onkologie

Springer Medizin

Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 4/2010

Malignant melanoma as a target malignancy for the study of the anti-metastatic properties of the heparins

Distant metastases do not metastasize

The guardians of the genome (p53, TA-p73, and TA-p63) are regulators of tumor suppressor miRNAs network

CXCL12 / CXCR4 / CXCR7 chemokine axis and cancer progression

Expression of tenascin-C and its isoforms in the breast

Minimizing early relapse and maximizing treatment outcomes in hormone-sensitive postmenopausal breast cancer: efficacy review of AI trials

Neu im Fachgebiet Onkologie

Bei Senioren mit Prostatakarzinom auf Anämie achten!

ICI-Therapie in der Schwangerschaft wird gut toleriert

Krebspatienten impfen: Was? Wen? Und wann nicht?

Müde im Alter? Auch an die Nebenniere denken

Update Onkologie