Skip to main content Accessibility help

We use cookies to distinguish you from other users and to provide you with a better experience on our websites. Close this message to accept cookies or find out how to manage your cookie settings.

Close cookie message
×
Hostname: page-component-78c5997874-94fs2 Total loading time: 0 Render date: 2024-11-01T21:29:34.102Z Has data issue: false hasContentIssue false

8 - Targeting the Notch signaling pathway in cancer stem cells

from SECTION III - TARGETING CANCER STEM CELL PATHWAYS

Published online by Cambridge University Press:  15 December 2009

By
Joon T. Park ,
Ie-Ming Shih  and
Tian-Li Wang
Edited by
William L. Farrar
Tian-Li Wang
Affiliation:
Johns Hopkins Medical Institutions
Get access

Summary

NOTCH SIGNALING IN CANCER STEM CELLS

Stem cells are characterized by two unique properties: self-renewal and multilineage differentiation potential. Self-renewal provides the cell with the ability to go through numerous cycles of cell division, while maintaining a stem cell population through asymmetric cell division. For each division, a stem cell divides into two cells: another stem cell and a progenitor cell. It is thought that the stem cell retains the stem cell characteristics, while the progenitor cell can differentiate into tissue-specific cells within a limited number of cell divisions. Embryonic stem cells are active during embryonic differentiation and develop into all of the tissues in the body. Adult stem cells can be found in differentiated tissues and can differentiate into the entirety of cell types in the tissue from which they originate. Normal stem cells are transformed into cancer stem cells by acquiring somatic mutations in oncogenes or tumor suppressor genes. Cancer stem cells share stem cell properties with embryonic stem cells such as self-renewal and differentiation potential. Evidence suggests that many cancers, including leukemia, breast cancer, and glioma, contain a rare population of cells that are highly tumorigenic, in contrast to the bulk of cancer cells that have a limited capacity to form tumors in vivo. Cancer stem cells proliferate slowly, have indefinite self-replication ability, and are highly resistant to chemotherapy.

Type
Chapter
Information
Cancer Stem Cells , pp. 128 - 138
Publisher: Cambridge University Press
Print publication year: 2009

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Reya, T., et al., Stem cells, cancer, and cancer stem cells. Nature, 2001. 414(6859): pp. 105–111.CrossRefGoogle ScholarPubMed
Huntly, B.J.P., and Gilliland, D.G., Leukaemia stem cells and the evolution of cancer-stemcell research. Nat Rev Cancer, 2005. 5(4): pp. 311–321.CrossRefGoogle ScholarPubMed
Patrawala, L., et al., Side population is enriched in tumorigenic, stem-like cancer cells, whereas ABCG2+ and ABCG2− cancer cells are similarly tumorigenic. Cancer Res, 2005. 65(14): pp. 6207–6219.CrossRefGoogle ScholarPubMed
Fan, X., et al., Notch pathway inhibition depletes stem-like cells and blocks engraftment in embryonal brain tumors. Cancer Res, 2006. 66(15): pp. 7445–7452.CrossRefGoogle ScholarPubMed
Bray, S.J., Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol, 2006. 7(9): pp. 678–689.CrossRefGoogle ScholarPubMed
Blaumueller, C.M., et al., Intracellular cleavage of Notch leads to a heterodimeric receptor on the plasma membrane. Cell, 1997. 90(2): pp. 281–291.CrossRefGoogle ScholarPubMed
Logeat, F., et al., The Notch1 receptor is cleaved constitutively by a furin-like convertase. Proc Natl Acad Sci U S A, 1998. 95(14): pp. 8108–8112.CrossRefGoogle ScholarPubMed
Brou, C., et al., A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell, 2000. 5(2): pp. 207–216.CrossRefGoogle ScholarPubMed
Fehon, R.G., et al., Molecular interactions between the protein products of the neurogenic loci Notch and Delta, two EGF-homologous genes in Drosophila. Cell, 1990. 61(3): pp. 523–534.CrossRefGoogle ScholarPubMed
Rebay, I., et al., Specific EGF repeats of Notch mediate interactions with Delta and serrate: implications for Notch as a multifunctional receptor. Cell, 1991. 67(4): pp. 687–699.CrossRefGoogle ScholarPubMed
Tamura, K., et al., Physical interaction between a novel domain of the receptor Notch and the transcription factor RBP-J[kappa]/Su(H). Curr Biol, 1995. 5(12): pp. 1416–1423.CrossRefGoogle Scholar
Blank, V., et al., NF-[kappa]B and related proteins: Rel/dorsal homologies meet ankyrin-like repeats. Trends Biochem Sci, 1992. 17(4): pp. 135–140.CrossRefGoogle ScholarPubMed
Tun, T., et al., Recognition sequence of a highly conserved DNA binding protein RBP-Jx. Nucl Acids Res, 1994. 22(6): pp. 965–971.CrossRefGoogle Scholar
Nakayama, K., Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem J, 1997. 327(Pt 3): pp. 625–635.CrossRefGoogle ScholarPubMed
Bush, G., et al., Ligand-induced signaling in the absence of furin processing of Notch1. Dev Biol, 2001. 229(2): pp. 494–502.CrossRefGoogle ScholarPubMed
Moloney, D.J., et al., Fringe is a glycosyltransferase that modifies Notch. Nature, 2000. 406(6794): pp. 369–375.CrossRefGoogle ScholarPubMed
LaVoie, M.J., and Selkoe, D.J., The Notch ligands, Jagged and Delta, are sequentially processed by {alpha}-secretase and presenilin/{gamma}-secretase and release signaling fragments. J Biol Chem, 2003. 278(36): pp. 34427–34437.CrossRefGoogle ScholarPubMed
Es, J.H., et al., Notch/[gamma]-secretase inhibition turns proliferative cells in intestinal crypts and adenomas into goblet cells. Nature, 2005. 435(7044): pp. 959–963.Google Scholar
Curry, C.L., et al., Gamma secretase inhibitor blocks Notch activation and induces apoptosis in Kaposi's sarcoma tumor cells. Oncogene, 2005. 24(42): pp. 6333–6344.CrossRefGoogle ScholarPubMed
Barten, D.M., et al., Gamma-secretase inhibitors for Alzheimer's disease: balancing efficacy and toxicity. Drugs R D, 2006. 7(2): pp. 87–97.CrossRefGoogle ScholarPubMed
Garces, C., et al., Notch-1 controls the expression of fatty acid-activated transcription factors and is required for adipogenesis. J Biol Chem, 1997. 272(47): pp. 29729–29734.CrossRefGoogle ScholarPubMed
Noguera-Troise, I., et al., Blockade of Dll4 inhibits tumour growth by promoting non-productive angiogenesis. Nature, 2006. 444(7122): pp. 1032–1037.CrossRefGoogle ScholarPubMed
Scehnet, J.S., et al., Inhibition of Dll4-mediated signaling induces proliferation of immature vessels and results in poor tissue perfusion. Blood, 2007. 109(11): pp. 4753–4760.CrossRefGoogle ScholarPubMed
Ridgway, J., et al., Inhibition of Dll4 signalling inhibits tumour growth by deregulating angiogenesis. Nature, 2006. 444(7122): pp. 1083–1087.CrossRefGoogle ScholarPubMed
Li, K., et al., Modulation of Notch signaling by antibodies specific for the extracellular negative regulatory region of NOTCH3. J Biol Chem, 2008. 283(12): pp. 8046–8054.CrossRefGoogle ScholarPubMed
Gordon, W.R., et al., Structural basis for autoinhibition of Notch. Nat Struct Mol Biol, 2007. 14(4): pp. 295–300.CrossRefGoogle ScholarPubMed
Qiu, L., et al., Recognition and ubiquitination of Notch by Itch, a Hect-type E3 ubiquitin ligase. J Biol Chem, 2000. 275(46): pp. 35734–35737.CrossRefGoogle ScholarPubMed
Hubbard, E.J.A., et al., Sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins. Genes Dev, 1997. 11(23): pp. 3182–3193.CrossRefGoogle ScholarPubMed
Gupta-Rossi, N., et al., Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor. J Biol Chem, 2001. 276(37): pp. 34371–34378.CrossRefGoogle ScholarPubMed
Oberg, C., et al., The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. J Biol Chem, 2001. 276(38): pp. 35847–35853.CrossRefGoogle ScholarPubMed
McGill, M.A., and McGlade, C.J., Mammalian numb proteins promote Notch1 receptor ubiquitination and degradation of the Notch1 intracellular domain. J Biol Chem, 2003. 278(25): pp. 23196–23203.CrossRefGoogle ScholarPubMed
Pece, S., et al., Loss of negative regulation by Numb over Notch is relevant to human breast carcinogenesis. J Cell Biol, 2004. 167(2): pp. 215–221.CrossRefGoogle ScholarPubMed
Park, J.T., et al., Notch3 gene amplification in ovarian cancer. Cancer Res, 2006. 66(12): pp. 6312–6318.CrossRefGoogle ScholarPubMed
Wang, Z., et al., Down-regulation of Notch-1 contributes to cell growth inhibition and apoptosis in pancreatic cancer cells. Mol Cancer Ther, 2006. 5(3): pp. 483–493.CrossRefGoogle ScholarPubMed
Purow, B.W., et al., Expression of Notch-1 and its ligands, Delta-Like-1 and Jagged-1, is critical for glioma cell survival and proliferation. Cancer Res, 2005. 65(6): pp. 2353–2363.CrossRefGoogle ScholarPubMed
Sledz, C.A., et al., Activation of the interferon system by short-interfering RNAs. Nat Cell Biol, 2003. 5(9): pp. 834–839.CrossRefGoogle ScholarPubMed
Rossi, J., et al., Wandering eye for RNAi. Nat Med, 2008. 14(6): p. 611.CrossRefGoogle ScholarPubMed
Wu, L., et al., MAML1, a human homologue of Drosophila Mastermind, is a transcriptional co-activator for NOTCH receptors. Nat Genet, 2000. 26(4): pp. 484–489.CrossRefGoogle ScholarPubMed
Kitagawa, M., et al., A human protein with sequence similarity to Drosophila Mastermind coordinates the nuclear form of Notch and a CSL protein to build a transcriptional activator complex on target promoters. Mol Cell Biol, 2001. 21(13): pp. 4337–4346.CrossRefGoogle Scholar
Liu, Z.-J., et al., Notch1 signaling promotes primary melanoma progression by activating mitogen-activated protein kinase/phosphatidylinositol 3-kinase-Akt pathways and up-regulating N-cadherin expression. Cancer Res, 2006. 66(8): pp. 4182–4190.CrossRefGoogle ScholarPubMed
Weng, A.P., et al., Growth suppression of pre-T acute lymphoblastic leukemia cells by inhibition of Notch signaling. Mol Cell Biol, 2003. 23(2): pp. 655–664.CrossRefGoogle ScholarPubMed
Maillard, I., et al., Canonical Notch signaling is dispensable for the maintenance of adult hematopoietic stem cells. Cell Stem Cell, 2008. 2(4): pp. 356–366.CrossRefGoogle ScholarPubMed

Save book to Kindle

To save this book to your Kindle, first ensure coreplatform@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about saving to your Kindle.

Note you can select to save to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be saved to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

Find out more about the Kindle Personal Document Service.

Available formats
×

Save book to Dropbox

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Dropbox.

Available formats
×

Save book to Google Drive

To save content items to your account, please confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your account. Find out more about saving content to Google Drive.

Available formats
×