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Journal articles on the topic 'Tumour suppressor'

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Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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1

Wagner, K. J., and S. G. E. Roberts. "Transcriptional regulation by the Wilms' tumour suppressor protein WT1." Biochemical Society Transactions 32, no. 6 (October 26, 2004): 932–35. http://dx.doi.org/10.1042/bst0320932.

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Wilms' tumour is a paediatric malignancy of the kidneys and is the most common solid tumour found in children. The Wilms' tumour suppressor protein WT1 is mutated in approx. 15% of Wilms' tumours, and is aberrantly expressed in many others. WT1 can manifest both tumour suppressor and oncogenic activities, but the reasons for this are not yet clear. The Wilms' tumour suppressor protein WT1 is a transcriptional activator, the function of which is under cell-context-specific control. We have previously described a small region at the N-terminus of WT1 (suppression domain) that inhibits the transcriptional activation domain by contacting a co-suppressor protein. We recently identified BASP1 as one of the components of the co-suppressor. Here, we analyse the mechanism of action of the WT1 suppression domain, and discuss its function in the context of the role of WT1 as a regulator of development.

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2

Swale, V. J., and A. G. Quinn. "Tumour suppressor genes." Clinical and Experimental Dermatology 25, no. 3 (May 2000): 231–35. http://dx.doi.org/10.1046/j.1365-2230.2000.00620.x.

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3

Cowell, J. K. "Tumour suppressor genes." Annals of Oncology 3, no. 9 (November 1992): 693–98. http://dx.doi.org/10.1093/oxfordjournals.annonc.a058319.

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4

KLEIN, G. "Tumour suppressor genes." Journal of Cell Science 1988, Supplement 10 (February 1, 1988): 171–80. http://dx.doi.org/10.1242/jcs.1988.supplement_10.13.

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5

Vile, R. "Tumour suppressor genes." BMJ 298, no. 6684 (May 20, 1989): 1335–36. http://dx.doi.org/10.1136/bmj.298.6684.1335.

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6

Maehama, T., F. Okahara, and Y. Kanaho. "The tumour suppressor PTEN: involvement of a tumour suppressor candidate protein in PTEN turnover." Biochemical Society Transactions 32, no. 2 (April 1, 2004): 343–47. http://dx.doi.org/10.1042/bst0320343.

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The tumour suppressor PTEN (phosphatase and tensin homologue deleted on chromosome 10) plays essential roles in regulating signalling pathways involved in cell growth and apoptosis, and is inactivated in a wide variety of tumours. The role of PTEN as a tumour suppressor has been firmly established; however, the mechanism(s) by which its function and activity are regulated remains elusive. Here, we summarize recent progress in research directed towards trying to understand the molecular basis of regulatory mechanisms for PTEN. We also describe our novel finding that a tumour suppressor candidate protein binds to extreme C-terminal region of PTEN and regulates PTEN protein turnover.

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7

Clurman, Bruce, and Mark Groudine. "Defining tumour-suppressor genes." Nature 389, no. 6647 (September 1997): 123. http://dx.doi.org/10.1038/38119.

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8

McCarthy, Nicola. "Surviving the tumour suppressor." Nature Reviews Molecular Cell Biology 8, no. 7 (July 2007): 516. http://dx.doi.org/10.1038/nrm2214.

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9

Bangham, Jenny. "Tumour-suppressor super models." Nature Reviews Cancer 5, no. 2 (January 20, 2005): 84. http://dx.doi.org/10.1038/nrc1554.

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10

Bangham, Jenny. "Tumour suppressor super models." Nature Reviews Genetics 6, no. 2 (February 2005): 91. http://dx.doi.org/10.1038/nrg1546.

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11

McCarthy, Nicola. "Surviving the tumour suppressor." Nature Reviews Cancer 7, no. 7 (July 2007): 490. http://dx.doi.org/10.1038/nrc2179.

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12

Gallagher, Stuart J., Richard F. Kefford, and Helen Rizos. "The ARF tumour suppressor." International Journal of Biochemistry & Cell Biology 38, no. 10 (January 2006): 1637–41. http://dx.doi.org/10.1016/j.biocel.2006.02.008.

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13

LESLIE, Nick R., and C. Peter DOWNES. "PTEN function: how normal cells control it and tumour cells lose it." Biochemical Journal 382, no. 1 (August 10, 2004): 1–11. http://dx.doi.org/10.1042/bj20040825.

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The PTEN (phosphatase and tensin homologue deleted on chromosome 10) tumour suppressor is a PI (phosphoinositide) 3-phosphatase that can inhibit cellular proliferation, survival and growth by inactivating PI 3-kinase-dependent signalling. It also suppresses cellular motility through mechanisms that may be partially independent of phosphatase activity. PTEN is one of the most commonly lost tumour suppressors in human cancer, and its deregulation is also implicated in several other diseases. Here we discuss recent developments in our understanding of how the cellular activity of PTEN is regulated, and the closely related question of how this activity is lost in tumours. Cellular PTEN function appears to be regulated by controlling both the expression of the enzyme and also its activity through mechanisms including oxidation and phosphorylation-based control of non-substrate membrane binding. Therefore mutation of PTEN in tumours disrupts not only the catalytic function of PTEN, but also its regulatory aspects. However, although mutation of PTEN is uncommon in many human tumour types, loss of PTEN expression seems to be more frequent. It is currently unclear how these tumours lose PTEN expression in the absence of mutation, and while some data implicate other potential tumour suppressors and oncogenes in this process, this area seems likely to be a key focus of future research.

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14

Bagchi, Sanjit. "New tumour suppressor linked to Wilms' tumour." Lancet Oncology 8, no. 2 (February 2007): 102. http://dx.doi.org/10.1016/s1470-2045(07)70019-0.

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15

Farrell, William E., and Richard N. Clayton. "Tumour suppressor genes in pituitary tumour formation." Best Practice & Research Clinical Endocrinology & Metabolism 13, no. 3 (October 1999): 381–93. http://dx.doi.org/10.1053/beem.1999.0029.

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16

Swat, Aneta, Ignacio Dolado, Ana Igea, Gonzalo Gomez-Lopez, David G. Pisano, Ana Cuadrado, and Angel R. Nebreda. "Expression and functional validation of new p38α transcriptional targets in tumorigenesis." Biochemical Journal 434, no. 3 (February 24, 2011): 549–58. http://dx.doi.org/10.1042/bj20101410.

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p38α MAPK (mitogen-activated protein kinase) plays an important tumour suppressor role, which is mediated by both its negative effect on cell proliferation and its pro-apoptotic activity. Surprisingly, most tumour suppressor mechanisms co-ordinated by p38α have been reported to occur at the post-translational level. This contrasts with the important role of p38α in the regulation of transcription and the profound changes in gene expression that normally occur during tumorigenesis. We have analysed whole-genome expression profiles of Ras-transformed wild-type and p38α-deficient cells and have identified 202 genes that are potentially regulated by p38α in transformed cells. Expression analysis has confirmed the regulation of these genes by p38α in tumours, and functional validation has identified several of them as probable mediators of the tumour suppressor effect of p38α on Ras-induced transformation. Interestingly, approx. 10% of the genes that are negatively regulated by p38α in transformed cells contribute to EGF (epidermal growth factor) receptor signalling. Our results suggest that inhibition of EGF receptor signalling by transcriptional targets of p38α is an important function of this signalling pathway in the context of tumour suppression.

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17

Beghelli, Stefania, Giuseppe Pelosi, Giuseppe Zamboni, Massimo Falconi, Calogero Iacono, Cesare Bordi, and Aldo Scarpa. "Pancreatic endocrine tumours: evidence for a tumour suppressor pathogenesis and for a tumour suppressor gene on chromosome 17p." Journal of Pathology 186, no. 1 (September 1998): 41–50. http://dx.doi.org/10.1002/(sici)1096-9896(199809)186:1<41::aid-path172>3.0.co;2-l.

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18

Kim, Y.-J., Y.-E. Cho, Y.-W. Kim, J.-Y. Kim, S. Lee, and J.-H. Park. "Suppression of putative tumour suppressor geneGLTSCR2expression in human glioblastomas." Journal of Pathology 216, no. 2 (October 2008): 218–24. http://dx.doi.org/10.1002/path.2401.

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19

&NA;. "Important new tumour suppressor identified." Inpharma Weekly &NA;, no. 936 (May 1994): 13. http://dx.doi.org/10.2165/00128413-199409360-00026.

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20

&NA;. "New tumour suppressor gene found." Inpharma Weekly &NA;, no. 892 (June 1993): 11. http://dx.doi.org/10.2165/00128413-199308920-00020.

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21

Venkitaraman, Ashok R. "DUBing down a tumour suppressor." Nature Cell Biology 7, no. 4 (April 2005): 332–33. http://dx.doi.org/10.1038/ncb0405-332.

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22

Ramsey, Matthew R., and Norman E. Sharpless. "ROS as a tumour suppressor?" Nature Cell Biology 8, no. 11 (November 2006): 1213–15. http://dx.doi.org/10.1038/ncb1106-1213.

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23

Harrison, Charlotte. "Reactivating p53 tumour suppressor function." Nature Reviews Drug Discovery 11, no. 9 (August 31, 2012): 674. http://dx.doi.org/10.1038/nrd3834.

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24

Levine, Arnold J., Jamil Momand, and Cathy A. Finlay. "The p53 tumour suppressor gene." Nature 351, no. 6326 (June 1991): 453–56. http://dx.doi.org/10.1038/351453a0.

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25

Nowell, Craig S., and Freddy Radtke. "Notch as a tumour suppressor." Nature Reviews Cancer 17, no. 3 (February 3, 2017): 145–59. http://dx.doi.org/10.1038/nrc.2016.145.

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26

Steele, Thompson, Hall, and Lane. "The p53 tumour suppressor gene." British Journal of Surgery 85, no. 11 (November 20, 1998): 1460–67. http://dx.doi.org/10.1046/j.1365-2168.1998.00910.x.

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27

Paul, J. "Tumour suppressor genes: Oncogenesis update." Histopathology 15, no. 1 (July 1989): 1–9. http://dx.doi.org/10.1111/j.1365-2559.1989.tb03037.x.

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28

Alao, J. P., M. Q. Mohammed, and S. Retsas. "The CDKN2A tumour suppressor gene." Melanoma Research 12, no. 6 (December 2002): 559–63. http://dx.doi.org/10.1097/00008390-200212000-00005.

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29

Aldred, Micheala A. "A cool tumour-suppressor gene." Molecular Medicine Today 6, no. 2 (February 2000): 50. http://dx.doi.org/10.1016/s1357-4310(99)01646-9.

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30

Zaid, O., and J. A. Downs. "Histones as tumour suppressor genes." Cellular and Molecular Life Sciences 62, no. 15 (July 7, 2005): 1653–56. http://dx.doi.org/10.1007/s00018-005-5091-6.

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31

Wunsch, Hannah. "Experts unravel tumour-suppressor pathways." Lancet 350, no. 9092 (December 1997): 1684. http://dx.doi.org/10.1016/s0140-6736(05)64286-9.

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32

Hickman, Emma S., and Kristian Helin. "The p53 Tumour Suppressor Protein." Biotechnology and Genetic Engineering Reviews 17, no. 1 (August 2000): 179–212. http://dx.doi.org/10.1080/02648725.2000.10647992.

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33

Scott, Anthony, and Zhenghe Wang. "Tumour suppressor function of protein tyrosine phosphatase receptor-T." Bioscience Reports 31, no. 5 (April 21, 2011): 303–7. http://dx.doi.org/10.1042/bsr20100134.

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It has long been thought that PTPs (protein tyrosine phosphatases) normally function as tumour suppressors. Recent high-throughput mutational analysis identified loss-of-function mutations in six PTPs in human colon cancers, providing critical cancer genetics evidence that PTPs can act as tumour suppressor genes. PTPRT (protein tyrosine phosphatase receptor-T), a member of the family of type IIB receptor-like PTPs, is the most frequently mutated PTP among them. Consistent with the notion that PTPRT is a tumour suppressor, PTPRT knockout mice are hypersensitive to AOM (azoxymethane)-induced colon cancer. The present review focuses on the physiological and pathological functions of PTPRT as well as the cellular pathways regulated by this phosphatase.

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34

S Patil, Priya, Jaydeep N Pol, and Ashalata D Patil. "ROLE OF TUMOUR SUPPRESSOR GENE P53 IN TRIPLE NEGATIVE BREAST CANCER." International Journal of Anatomy and Research 5, no. 4.2 (November 1, 2017): 4585–89. http://dx.doi.org/10.16965/ijar.2017.402.

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35

Ahmad, I. "The role of WNT signalling in urothelial cell carcinoma." Annals of The Royal College of Surgeons of England 97, no. 7 (October 1, 2015): 481–86. http://dx.doi.org/10.1308/rcsann.2015.0008.

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Urothelial cell carcinoma (UCC) of the bladder is one of the most common malignancies, causing considerable morbidity and mortality worldwide. It is unique among the epithelial carcinomas as two distinct pathways to tumourigenesis appear to exist: low grade, recurring papillary tumours usually contain oncogenic mutations in FGFR3 or HRAS whereas high grade, muscle invasive tumours with metastatic potential generally have defects in the pathways controlled by the tumour suppressors p53 and retinoblastoma. Over the last two decades, a number of transgenic mouse models of UCC, containing deletions or mutations of key tumour suppressor genes or oncogenes, have helped us understand the mechanisms behind tumour development. In this summary, I present my work investigating the role of the WNT signalling cascade in UCC.

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36

Zaidi, Adeel H., and Sunil K. Manna. "Profilin–PTEN interaction suppresses NF-κB activation via inhibition of IKK phosphorylation." Biochemical Journal 473, no. 7 (March 29, 2016): 859–72. http://dx.doi.org/10.1042/bj20150624.

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Profilin-mediated tumour suppression involving nuclear transcription factor κB (NF-κB) is unknown. Profilin interacts with protein phosphatase, phosphatase and tension homologue (PTEN) and stabilizes it. Sustained PTEN level inhibits phosphorylation of IκBα kinase (IKK) and subsequently, down-regulates NF-κB and enhances cell death. Profilin acts as tumor suppressor via NF-κB inhibition.

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37

Green, Victoria L., Michael C. White, Leslie J. Hipkin, Richard V. Jeffreys, Patrick M. Foy, and Stephen L. Atkin. "Apoptosis and p53 suppressor gene protein expression in human anterior pituitary adenomas." European Journal of Endocrinology 136, no. 4 (April 1997): 382–87. http://dx.doi.org/10.1530/eje.0.1360382.

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Abstract Human anterior pituitary adenomas proliferate and express the p53 tumour suppressor gene protein, but it is not known if apoptosis (programmed cell death) occurs. Therefore, the detection of apoptosis was undertaken in tumorous human anterior pituitary tissue and compared with p53 protein expression, tumour type and tumour size. Apoptosis (detected by the in situ end labelling technique) and p53 suppressor gene protein (detected by DO. 1-antibody immunocytochemistry) were determined in formalin-fixed and paraffin-embedded tissue from 37 human pituitary adenomas (2 macroprolactinomas, 9 somatotrophinomas and 26 non-functioning adenomas). Two normal anterior pituitaries were also included in this study. Pre-operative tumour size was scored 1 to 4 from magnetic resonance imaging radiology. Apoptosis was found in 7 of 29 tumours (24%), 11% of somatotrophinomas and 33% of non-functioning adenomas, although this difference was not significant. The p53 tumour suppressor protein was found in 7 of 31 tumours (23%), 33% of somatotrophinomas and 19% of nonfunctioning adenomas. Apoptosis and p53 protein expression were not found in normal anterior pituitary. In conclusion, apoptosis occurs in human anterior pituitary adenomas, but no significant association was found between apoptosis and p53 protein expression, tumour type or tumour size. European Journal of Endocrinology 136 382–387

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38

Brown, Keith W., and Karim T. A. Malik. "The molecular biology of Wilms' tumour." Expert Reviews in Molecular Medicine 3, no. 13 (May 14, 2001): 1–16. http://dx.doi.org/10.1017/s1462399401003027.

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Wilms' tumour (WT; nephroblastoma), a kidney neoplasm, is one of the most frequently occurring solid tumours of childhood. It arises from the developing kidney by genetic and epigenetic changes that lead to the abnormal proliferation of renal stem cells (metanephric blastema). WT serves as a paradigm for understanding the relationship between loss of developmental control and gain of tumourigenic potential. In particular, loss of function of tumour suppressor genes has been implicated in the development of WT, and the Wilms' tumour suppressor gene WT1 (at chromosome 11p13) was the second tumour suppressor gene to be cloned, after the retinoblastoma gene RB-1. WT1 plays an essential role in kidney development, but is mutated in only approximately 20% of WTs, which suggests that further lesions and genetic loci are involved in Wilms' tumourigenesis. Other chromosomal regions associated with WT include 7p, 11p15, 16q and 17q. Although many of these loci probably contain tumour suppressor genes, imprinted genes (genes showing expression of only one parental allele) and oncogenes have also been implicated in WT. Some loci have been shown to be associated with particular clinical outcomes, suggesting that they might be used to determine prognosis, and especially to identify poor prognostic subgroups that can be targeted for aggressive and/or novel therapies.

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39

White, Lydia G., Hannah E. Goy, Alinor J. Rose, and Alexander D. McLellan. "Controlling Cell Trafficking: Addressing Failures in CAR T and NK Cell Therapy of Solid Tumours." Cancers 14, no. 4 (February 15, 2022): 978. http://dx.doi.org/10.3390/cancers14040978.

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The precision guiding of endogenous or adoptively transferred lymphocytes to the solid tumour mass is obligatory for optimal anti-tumour effects and will improve patient safety. The recognition and elimination of the tumour is best achieved when anti-tumour lymphocytes are proximal to the malignant cells. For example, the regional secretion of soluble factors, cytotoxic granules, and cell-surface molecule interactions are required for the death of tumour cells and the suppression of neovasculature formation, tumour-associated suppressor, or stromal cells. The resistance of individual tumour cell clones to cellular therapy and the hostile environment of the solid tumours is a major challenge to adoptive cell therapy. We review the strategies that could be useful to overcoming insufficient immune cell migration to the tumour cell mass. We argue that existing ‘competitive’ approaches should now be revisited as complementary approaches to improve CAR T and NK cell therapy.

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40

Raheja, Radhika, Yuhui Liu, Ellen Hukkelhoven, Nancy Yeh, and Andrew Koff. "The ability of TRIM3 to induce growth arrest depends on RING-dependent E3 ligase activity." Biochemical Journal 458, no. 3 (February 28, 2014): 537–45. http://dx.doi.org/10.1042/bj20131288.

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41

Roehrig, Anne E., Kristina Klupsch, Juan A. Oses-Prieto, Selim Chaib, Stephen Henderson, Warren Emmett, Lucy C. Young, et al. "Cell-cell adhesion regulates Merlin/NF2 interaction with the PAF complex." PLOS ONE 16, no. 8 (August 23, 2021): e0254697. http://dx.doi.org/10.1371/journal.pone.0254697.

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The PAF complex (PAFC) coordinates transcription elongation and mRNA processing and its CDC73/parafibromin subunit functions as a tumour suppressor. The NF2/Merlin tumour suppressor functions both at the cell cortex and nucleus and is a key mediator of contact inhibition but the molecular mechanisms remain unclear. In this study we have used affinity proteomics to identify novel Merlin interacting proteins and show that Merlin forms a complex with multiple proteins involved in RNA processing including the PAFC and the CHD1 chromatin remodeller. Tumour-derived inactivating mutations in both Merlin and the CDC73 PAFC subunit mutually disrupt their interaction and growth suppression by Merlin requires CDC73. Merlin interacts with the PAFC in a cell density-dependent manner and we identify a role for FAT cadherins in regulating the Merlin-PAFC interaction. Our results suggest that in addition to its function within the Hippo pathway, Merlin is part of a tumour suppressor network regulated by cell-cell adhesion which coordinates post-initiation steps of the transcription cycle of genes mediating contact inhibition.

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42

van Aalten, Daan. "Structure of the LKB1 tumour suppressor." Acta Crystallographica Section A Foundations of Crystallography 66, a1 (August 29, 2010): s30. http://dx.doi.org/10.1107/s0108767310099344.

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43

Puccini, J., L. Dorstyn, and S. Kumar. "Caspase-2 as a tumour suppressor." Cell Death & Differentiation 20, no. 9 (June 28, 2013): 1133–39. http://dx.doi.org/10.1038/cdd.2013.87.

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44

Colaluca, Ivan N., Daniela Tosoni, Paolo Nuciforo, Francesca Senic-Matuglia, Viviana Galimberti, Giuseppe Viale, Salvatore Pece, and Pier Paolo Di Fiore. "NUMB controls p53 tumour suppressor activity." Nature 451, no. 7174 (January 2008): 76–80. http://dx.doi.org/10.1038/nature06412.

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45

Chew, Yat Peng, Scott Wilkie, Necati Findikli, and Sibylle Mittnacht. "Regulation of the tumour suppressor pRB." Biochemical Society Transactions 27, no. 3 (June 1, 1999): A63. http://dx.doi.org/10.1042/bst027a063c.

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46

Marignani, P. A. "LKB1, the multitasking tumour suppressor kinase." Journal of Clinical Pathology 58, no. 1 (January 1, 2005): 15–19. http://dx.doi.org/10.1136/jcp.2003.015255.

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47

Hao, Yue, Taria Crenshaw, Thomas Moulton, Elizabeth Newcomb, and Benjamin Tycko. "Tumour-suppressor activity of H19 RNA." Nature 365, no. 6448 (October 1993): 764–67. http://dx.doi.org/10.1038/365764a0.

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48

Weitzman, Jonathan. "SWI/SNF is a tumour suppressor." Genome Biology 1 (2000): spotlight—20001222–01. http://dx.doi.org/10.1186/gb-spotlight-20001222-01.

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49

KOOREY, DAVID J., and GEOFFREY W. McCAUGHAN. "Tumour suppressor genes and colorectal neoplasia." Journal of Gastroenterology and Hepatology 8, no. 2 (April 1993): 174–84. http://dx.doi.org/10.1111/j.1440-1746.1993.tb01511.x.

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50

Harris, Henry. "How Tumour Suppressor Genes Were Discovered." FASEB Journal 7, no. 10 (July 1993): 978–93. http://dx.doi.org/10.1096/fasebj.7.10.8344496.

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