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Elevation of SIPL1 (SHARPIN) Increases Breast Cancer Risk
Open accessAbstract
SIPL1 (Sharpin) or Sharpin plays a role in tumorigenesis. However, its involvement in breast cancer tumorigenesis remains largely unknown. To investigate this issue, we have systemically analyzed SIPL1 gene amplification and expression data available from Oncomine datasets, which were derived from 17 studies and contained approximately 20,000 genes, 3438 breast cancer cases, and 228 normal individuals. We found a SIPL1 gene amplification in invasive ductal breast cancers compared to normal breast tissues and a significant elevation of SIPL1 mRNA in breast cancers in comparison to non-tumor breast tissues. These results collectively reveal that increases in SIPL1 expression occur during breast cancer tumorigenesis. To further investigate this association, we observed increases in the SIPL1 gene and mRNA in the breast cancer subtypes of estrogen receptor (ER)+, progesterone receptor (PR)+, HER2+, or triple negative. Additionally, a gain of the SIPL1 gene correlated with breast cancer grade and the levels of SIPL1 mRNA associated with both breast cancer stages and grades. Elevation of SIPL1 gene copy and mRNA is linked to a decrease in patient survival, especially for those with PR+, ER+, or HER2- breast cancers. These results are supported by our analysis of SIPL1 protein expression using a tissue microarray containing 224 breast cancer cases, in which higher levels of SIPL1 relate to ER+ and PR+ tumors and AKT activation. Furthermore, we were able to show that progesterone significantly reduced SIPL1 mRNA and protein expression in MCF7 cells. As progesterone enhances breast cancer tumorigenesis in a context dependent manner, inhibition of SIPL1 expression may contribute to progesterone's non-tumorigenic function which might be countered by SIPL1 upregulation. Taken together, we demonstrate a positive correlation of SIPL1 with BC tumorigenesis.
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SHARPIN gene amplification and protein overexpression has been observed in several human cancer types.
“SHARPIN gene amplification and protein overexpression has been observed in several human cancer types (Fig. S1A) (Bii et al., 2015, De Melo & Tang, 2015, He et al., 2010, Jung et al., 2010).”
From SHARPIN S146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis (2022) · cites this paper as De Melo & Tang, 2015
The Results sections on SIPL1 gene amplification and protein expression report increased gene copy number in breast cancer and higher protein levels in certain breast tumors. The paper does not establish that both findings have been observed across several distinct human cancer types; its reported analyses focus on breast cancer and its subtypes. (LLM, conf=0.86)
Experimental — accuracy not yet measuredSHARPIN gene is amplified in a variety of human cancers.
“SHARPIN gene is amplified, and at the protein level it is overexpressed in a variety of human cancers (Fig. S1A)”
From SHARPIN S146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis (2022) · cites this paper as De Melo & Tang, 2015
The Results section, “Amplification of the SIPL1 gene in breast cancer” (page not provided), reports increased SHARPIN/SIPL1 gene copy number in breast cancer, including several breast cancer subtypes. It does not establish amplification across a variety of distinct human cancers. (LLM, conf=0.86)
Experimental — accuracy not yet measuredSHARPIN protein is overexpressed in a variety of human cancers.
“SHARPIN gene is amplified, and at the protein level it is overexpressed in a variety of human cancers (Fig. S1A)”
From SHARPIN S146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis (2022) · cites this paper as De Melo & Tang, 2015
The Introduction (page not available) reports SIPL1/SHARPIN upregulation in ovarian, renal-cell, and cervical cancers. The Results section on protein expression (page not available) detects SHARPIN protein in breast carcinomas, but does not establish protein overexpression across those other cancer types. The claim is therefore supported for upregulation across several cancers, not specifically for protein-level overexpression across them. (LLM, conf=0.84)
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Cites
1 retracted
Bonnefoi, H. R., Potti, A., Delorenzi, M., Mauriac, L., Campone, M., Tubiana-Hulin, M., Petit, T., Rouanet, P., Jassem, J., Blot, E., et al. (2007) · The Lancet Oncology · doi:10.1016/s1470-2045(07)70345-5 · Cited by 212
RetractedWriting Group for the Women's Health Initiative Investigators (2002) · JAMA: The Journal of the American Medical Association · doi:10.1001/jama.288.3.321 · Cited by 15,889
Slamon, D. J., Clark, G. M., Wong, S. G., Levin, W. J., Ullrich, A., & McGuire, W. L. (1987) · Science · doi:10.1126/science.3798106 · Cited by 11,760
Sørlie, T., Perou, C. M., Tibshirani, R. J., Aas, T., Geisler, S. B., Johnsen, H., Hastie, T. J., Eisen, M. B., van de Rijn, M., Jeffrey, S. S., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191367098 · Cited by 11,506
Elston, C. W., & Ellis, I. O. (1991) · Histopathology · doi:10.1111/j.1365-2559.1991.tb00229.x · Cited by 6,181
The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups
METABRIC Group, Curtis, C., Shah, S. P., Chin, S.-F., Turashvili, G., Rueda, O. M., Dunning, M. J., Speed, D., Lynch, A. G., Samarajiwa, S., et al. (2012) · Nature · doi:10.1038/nature10983 · Cited by 6,097
Repeated observation of breast tumor subtypes in independent gene expression data sets
Sørlie, T., Tibshirani, R. J., Parker, J. S., Hastie, T. J., Marron, J. S., Nobel, A. B., Deng, S., Johnsen, H., Pesich, R., Geisler, S. B., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0932692100 · Cited by 5,508
The complexity of NF-κB signaling in inflammation and cancer
Hoesel, B., & Schmid, J. A. (2013) · Molecular Cancer · doi:10.1186/1476-4598-12-86 · Cited by 3,277
A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
Neve, R. M., Chin, K., Fridlyand, J., Yeh, J., Baehner, F. L., Fevr, T., Clark, L., Bayani, N., Coppé, J., Tong, F. K., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.10.008 · Cited by 3,224
Breast cancer and hormone-replacement therapy in the Million Women Study
Beral, V. (2003) · The Lancet · doi:10.1016/s0140-6736(03)14065-2 · Cited by 2,986
Mammographic Density and the Risk and Detection of Breast Cancer
Boyd, N. F., Guo, H., Martin, L. J., Sun, L., Stone, J., Fishell, E., Jong, R. A., Hislop, G., Chiarelli, A. M., Minkin, S., et al. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa062790 · Cited by 2,482
NF-κB in cancer: from innocent bystander to major culprit
Karin, M., Cao, Y., Greten, F. R., & Li, Z. (2002) · Nature reviews. Cancer · doi:10.1038/nrc780 · Cited by 2,476
Breast Density and Parenchymal Patterns as Markers of Breast Cancer Risk: A Meta-analysis
McCormack, V., & dos‐Santos‐Silva, I. (2006) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-06-0034 · Cited by 2,174
Sotiriou, C. P., Neo, S.-Y., McShane, L. M., Korn, E. L., Long, P. M., Jazaeri, A. A., Martiat, P., Fox, S. B., Harris, A. L., & Liu, E. T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1732912100 · Cited by 2,024
Genome-wide analysis of DNA copy-number changes using cDNA microarrays
Pollack, J. R., Perou, C. M., Alizadeh, A. A., Eisen, M. B., Pergamenschikov, A., Williams, C. F., Jeffrey, S. S., Botstein, D., & Brown, P. O. (1999) · Nature Genetics · doi:10.1038/12640 · Cited by 1,416
Inflammation meets cancer, with NF-κB as the matchmaker
Ben‐Neriah, Y., & Karin, M. (2011) · Nature Immunology · doi:10.1038/ni.2060 · Cited by 1,408
Breast cancer and hormone-replacement therapy: the Million Women Study
Beral, V., Banks, E., REEVES, G. K., & Bull, D. (2003) · The Lancet · doi:10.1016/s0140-6736(03)14596-5 · Cited by 1,270
Pollack, J. R., Sørlie, T., Perou, C. M., Rees, C. A., Jeffrey, S. S., Lønning, P. E., Tibshirani, R. J., Botstein, D., Børresen‐Dale, A., & Brown, P. O. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.162471999 · Cited by 1,167
NF-kB in development and progression of human cancer
Dolcet, X., Llobet‐Navàs, D., Pallarés, J., & Matías‐Guiu, X. (2005) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-005-1264-9 · Cited by 1,165
Desmedt, C., Piette, F., Loi, S., Wang, Y., Lallemand, F., Haibe‐Kains, B., Viale, G., Delorenzi, M., Zhang, Y., Saghatchian, M., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2765 · Cited by 963
Ma, X.-J., Wang, Z., Ryan, P. D., Isakoff, S. J., Barmettler, A., Fuller, A. P., Muir, B., Mohapatra, G., Salunga, R. C., Tuggle, J. T., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.05.015 · Cited by 959
Linear ubiquitination prevents inflammation and regulates immune signalling
Gerlach, B., Cordier, S. M., Schmukle, A. C., Emmerich, C. H., Rieser, E., Haas, T. L., Webb, A. I., Rickard, J. A., Anderton, H., Wong, W. W.-L., et al. (2011) · Nature · doi:10.1038/nature09816 · Cited by 940
SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
Ikeda, F., Deribe, Y. L., Skånland, S. S., Stieglitz, B., Grabbe, C., Franz-Wachtel, M., van Wijk, S. J. L., Goswami, P., Nagy, V., Terzic, J., et al. (2011) · Nature · doi:10.1038/nature09814 · Cited by 745
Kallioniemi, A. H., Kallioniemi, O., Piper, J., Tanner, M., Stokke, T., Chen, L., Smith, H. S., Pinkel, D., Gray, J. W., & Waldman, F. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.6.2156 · Cited by 739
Modelling breast cancer: one size does not fit all
Vargo-Gogola, T. C., & Rosen, J. M. (2007) · Nature reviews. Cancer · doi:10.1038/nrc2193 · Cited by 702
Genome-wide analysis of DNA copy number variation in breast cancer using DNA microarrays
Pollack, J. R., Perou, C. M., Sørlie, T., Alizadeh, A. A., Rees, C. A., Eise, M. B., Pergamenschikov, A., Williams, C. F., van de Rijn, M., Jeffrey, S. S., et al. (1999) · Nature Genetics · doi:10.1038/14385 · Cited by 632
SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
Tokunaga, F., Nakagawa, T., Nakahara, M., Saeki, Y., Taniguchi, M., Sakata, S.-I., Tanaka, K., Nakano, H., & Iwai, K. (2011) · Nature · doi:10.1038/nature09815 · Cited by 609
Estrogen Plus Progestin and Breast Cancer Incidence and Mortality in Postmenopausal Women
Chlebowski, R. T., Anderson, G. L., Gass, M. L. S., Lane, D. S., Aragaki, A. K., Kuller, L. H., Manson, J. E., Stefanick, M. L., Ockene, J. K., Sarto, G. E., et al. (2010) · JAMA · doi:10.1001/jama.2010.1500 · Cited by 565
Basal-like breast cancer and the BRCA1 phenotype
Turner, N. C., & Reis-Filho, J. S. (2006) · Oncogene · doi:10.1038/sj.onc.1209876 · Cited by 492
Different Gene Expression Patterns in Invasive Lobular and Ductal Carcinomas of the Breast
Zhao, H., Langerød, A., Ji, Y., Nowels, K. W., Nesland, J. M., Tibshirani, R. J., Bukholm, I. K., Kåresen, R., Botstein, D., Børresen‐Dale, A., et al. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-11-0786 · Cited by 447
Genomic Targets of Nuclear Estrogen Receptors
O’Lone, R. B., Frith, M. C., Karlsson, E. K., & Hansen, U. M. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0044 · Cited by 439
Kaaks, R., Berrino, F., Key, T. J., Rinaldi, S., Dossus, L., Biessy, C., Secreto, G., Amiano, P., Bingham, S. A., Boeing, H., et al. (2005) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/dji132 · Cited by 423
Elston, C. W., & Ellis, I. O. (2002) · Histopathology · doi:10.1046/j.1365-2559.2002.14691.x · Cited by 387
Molecular and Cellular Heterogeneity in Breast Cancer
Rivenbark, A. G., O’Connor, S., & Coleman, W. B. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.08.002 · Cited by 365
The I-SPY 1 TRIAL Investigators, Esserman, L. J., Berry, D. A., Cheang, M. C. U., Yau, C. S. F., Perou, C. M., Carey, L., DeMichele, A. M., Gray, J. W., Conway‐Dorsey, K., et al. (2011) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1895-2 · Cited by 365
Hofseth, L. J., Raafat, A. M., Osuch, J. R., Pathak, D. R., Slomski, C. A., & Haslam, S. Z. (1999) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jcem.84.12.6194 · Cited by 350
Perillo, B., Sasso, A., Abbondanza, C., & Palumbo, G. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.8.2890-2901.2000 · Cited by 328
Benson, J. R., Jatoi, I., Keisch, M. E., Esteva, F. J., Makris, A., & Jordan, V. C. (2009) · The Lancet · doi:10.1016/s0140-6736(09)60316-0 · Cited by 275
Progesterone signalling in breast cancer: a neglected hormone coming into the limelight
Brisken, C. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3518 · Cited by 274
Dong, L., Wang, W., Wang, F., Stoner, M. A., Reed, J. C., Harigai, M., Samudio, I. J., Kladde, M. P., Vyhlidal, C., & Safe, S. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32099 · Cited by 259
Predicting features of breast cancer with gene expression patterns
Lu, X., Lu, X. L., Wang, Z. C., Iglehart, J. D., Zhang, X., & Richardson, A. L. (2007) · Breast Cancer Research and Treatment · doi:10.1007/s10549-007-9596-6 · Cited by 234
LUBAC synthesizes linear ubiquitin chains via a thioester intermediate
Stieglitz, B., Morris-Davies, A. C., Koliopoulos, M. G., Christodoulou, E., & Rittinger, K. (2012) · EMBO Reports · doi:10.1038/embor.2012.105 · Cited by 224
The gene associated with trichorhinophalangeal syndrome in humans is overexpressed in breast cancer
Radvanyi, L. G., Singh-Sandhu, D., Gallichan, S., Lovitt, C., Pędyczak, A., Mallo, G. V., Gish, K., Kwok, K., Hanna, W. M., Zubovits, J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500904102 · Cited by 223
Smit, J. J., Monteferrario, D., Noordermeer, S. M., van Dijk, W. J., van der Reijden, B. A., & Sixma, T. K. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.217 · Cited by 220
Mannella, P., & Brinton, R. D. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1443-06.2006 · Cited by 213
Seymour, R. E., Hasham, M. G., Cox, G. A., Shultz, L. D., HogenEsch, H., Roopenian, D. C., & Sundberg, J. P. (2007) · Genes and Immunity · doi:10.1038/sj.gene.6364403 · Cited by 212
Tabchy, A. B., Valero, V., Vidaurre, T., Lluch, A. M., Gómez, H., Martín, M., Qi, Y., Barajas-Figueroa, L. J., Souchon, E. A., Coutant, C., et al. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-1265 · Cited by 210
Rennstam, K., Ahlstedt-Soini, M., Baldetorp, B., Bendahl, P.-O., Borg, Å., Karhu, R., Tanner, M., Tirkkonen, M., & Isola, J. J. (2003) · PubMed · Cited by 164
Lim, S., Sala, C., Yoon, J., Park, S., Kuroda, S., Sheng, M., & Kim, E. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0940 · Cited by 151
Cyclic Variation of DNA Synthesis in Human Breast Epithelium
Masters, J. R., Drife, J., & Scarisbrick, J. J. (1977) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/58.5.1263 · Cited by 149
Zhou, W., & Slingerland, J. M. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3622 · Cited by 148
Zheng, A., Kallio, A., & Härkönen, P. L. (2007) · Endocrinology · doi:10.1210/en.2006-1269 · Cited by 146
Endogenous sex hormones and subsequent breast cancer in premenopausal women
Micheli, A., Muti, P. C., Secreto, G., Krogh, V., Meneghini, E., Venturelli, E., Sieri, S., Pala, V. M., & Berrino, F. (2004) · International Journal of Cancer · doi:10.1002/ijc.20403 · Cited by 135
Belgnaoui, S. M., Paz, S., Samuel, S., Goulet, M.-L., Sun, Q., Kikkert, M., Iwaï, K., Đikić, I., Hiscott, J. B., & Lin, R. (2012) · Cell Host & Microbe · doi:10.1016/j.chom.2012.06.009 · Cited by 119
Breast Density and Breast Cancer Risk: A Practical Review
Wang, A. T., Vachon, C. M., Brandt, K. R., & Ghosh, K. (2014) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2013.12.014 · Cited by 116
Mechanism Underlying IκB Kinase Activation Mediated by the Linear Ubiquitin Chain Assembly Complex
Fujita, H., Rahighi, S., Akita, M., Kato, R., Sasaki, Y., Soichi Wakatsuki, A., & Iwaï, K. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01538-13 · Cited by 114
Shank-interacting protein–like 1 promotes tumorigenesis via PTEN inhibition in human tumor cells
He, L., Ingram, A. J., Rybak, A. P., & Tang, D. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40778 · Cited by 99
Self-citationGenome-Wide Functional Synergy between Amplified and Mutated Genes in Human Breast Cancer
Nikolsky, Y., Sviridov, E., Yao, J., Dosymbekov, D., Ustyansky, V., Kaznacheev, V., Dezső, Z., Mulvey, L. A., MacConaill, L. E., Winckler, W., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-3082 · Cited by 99
The Emerging Role of Linear Ubiquitination in Cell Signaling
Emmerich, C. H., Schmukle, A. C., & Walczak, H. (2011) · Science Signaling · doi:10.1126/scisignal.2002187 · Cited by 82
Molecular determinants of context-dependent progesterone receptor action in breast cancer
Hagan, C. R., & Lange, C. A. (2014) · BMC Medicine · doi:10.1186/1741-7015-12-32 · Cited by 82
E3 Ubiquitin Ligase HOIP Attenuates Apoptotic Cell Death Induced by Cisplatin
MacKay, C., Carroll, E., Ibrahim, A. F. M., Garg, A. K., Inman, G. J., Hay, R. T., & Alpi, A. F. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-2131 · Cited by 65
A sequence in the 5′ flanking region confers progestin responsiveness on the human c-myc gene
Moore, M. R., Zhou, J.-L., Blankenship, K. A., Strobl, J. S., Edwards, D. P., & Gentry, R. N. (1997) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/s0960-0760(97)00036-8 · Cited by 63
Newly identified tumor-associated role of human Sharpin
Jung, J., Kim, J. M., Park, B., Cheon, Y., Lee, B., Choo, S. H., Koh, S. S., & Lee, S. (2010) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0413-x · Cited by 59
SHARPIN regulates uropod detachment in migrating lymphocytes
Pouwels, J., De Franceschi, N., Rantakari, P., Auvinen, K., Karikoski, M., Mattila, E., Potter, C., Sundberg, J. P., Hogg, N., Gahmberg, C. G., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.10.011 · Cited by 55
Endogenous sex steroids in premenopausal women and risk of breast cancer: the ORDET cohort
Schernhammer, E. S., Sperati, F., Razavi, P., Agnoli, C., Sieri, S., Berrino, F., Krogh, V., Abbagnato, C. A., Grioni, S., Blandino, G., et al. (2013) · Breast Cancer Research · doi:10.1186/bcr3438 · Cited by 42
SHARPIN regulates mitochondria-dependent apoptosis in keratinocytes
Liang, Y., & Sundberg, J. P. (2011) · Journal of Dermatological Science · doi:10.1016/j.jdermsci.2011.04.012 · Cited by 40
Seute, A., Sinn, H., Schlenk, R. F., Emig, R., Wallwiener, D. R., Grischke, E., Hohaus, S., Döhner, H., Haas, R. R., & Bentz, M. (2001) · International Journal of Cancer · doi:10.1002/ijc.1296 · Cited by 40
Tomonaga, M. (2011) · International Journal of Oncology · doi:10.3892/ijo.2011.1209 · Cited by 35
Wang, Z., Sokolovska, A., Seymour, R. E., Sundberg, J. P., & HogenEsch, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031809 · Cited by 33
Iwaï, K. (2011) · Cell Cycle · doi:10.4161/cc.10.18.17437 · Cited by 32
Glass, A. G., Donis-Keller, H., Mies, C., Russo, J., Zehnbauer, B. A., Taube, S. E., & Aamodt, R. (2001) · PubMed · Cited by 31
Stieglitz, B., Haire, L. F., Đikić, I., & Rittinger, K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.359547 · Cited by 30
Sharpin Contributes to TNFα Dependent NFκB Activation and Anti-Apoptotic Signalling in Hepatocytes
Sieber, S., Lange, N., Kollmorgen, G., Erhardt, A., Quaas, A., Gontarewicz, A., Sass, G., Tiegs, G., & Kreienkamp, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029993 · Cited by 28
Daigo, Y., Takayama, I., Ward, S. M., Sanders, K. M., & Fujino, M. (2003) · Journal of Gastroenterology and Hepatology · doi:10.1046/j.1440-1746.2003.03046.x · Cited by 17
SIPL1 enhances the proliferation, attachment, and migration of CHO cells by inhibiting PTEN function
Melo, J. D., Wu, V., He, L., Yan, J., & Tang, D. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1840 · Cited by 12
Self-citationProgesterone sensitizes breast cancer MCF7 cells to imatinib inhibitory effects
Rocha, A., Azevedo, I., & Soares, R. A. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21432 · Cited by 12
The second ETV6 allele is not necessarily deleted in acute leukemias with aETV6/ABL fusion
Hannemann, J., Healy, L. E., Ridge, S. A., & Wiedemann, L. M. (1998) · Genes Chromosomes and Cancer · doi:10.1002/(sici)1098-2264(199803)21:3 · Cited by 8
Jacobs, H. (2011) · EMBO Reports · doi:10.1038/embor.2011.228 · Cited by 4
Li, C., Yao, A.-M., Chang, X.-N., Guo, Y., & Xu, R. C. (2013) · PubMed · Cited by 1
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Zhou, S., Liang, Y., Zhang, X., Liao, L., Yang, Y., Ouyang, W., & Xu, H. (2019) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2019.07.696 · Cited by 51
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Peuhu, E., Kaukonen, R., Lerche, M., Saari, M. A., Guzmán, C., Rantakari, P., Franceschi, N. D., Wärri, A. M., Γεωργιάδου, Μ., Jacquemet, G., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694387 · Cited by 49
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Yang, H., Yu, S., Wang, W., Li, X., Hou, Y., Liu, Z., Shi, Y., Mu, K., Niu, G., Xu, J., et al. (2017) · Neoplasia · doi:10.1016/j.neo.2016.12.002 · Cited by 46
SHARPIN Inhibits Esophageal Squamous Cell Carcinoma Progression by Modulating Hippo Signaling
Zhang, A., Wang, W., Chen, Z., Pang, D., Zhou, X., Lu, K., Hou, J., Wang, S., Gao, C., Lv, B., et al. (2019) · Neoplasia · doi:10.1016/j.neo.2019.12.001 · Cited by 44
A novel SHARPIN-PRMT5-H3R2me1 axis is essential for lung cancer cell invasion
Fu, T.-X., Lv, X., Kong, Q., & Yuan, C. (2017) · Oncotarget · doi:10.18632/oncotarget.18957 · Cited by 37
SHARPIN stabilizes estrogen receptor α and promotes breast cancer cell proliferation
Zhuang, T., Yu, S., Zhang, L., Yang, H., Li, X., Hou, Y., Liu, Z., Shi, Y., Wang, W., Yu, N. H., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.20368 · Cited by 36
Sharpin promotes hepatocellular carcinoma progression via transactivation of Versican expression
Tanaka, Y., Tateishi, K., Nakatsuka, T., Kudo, Y., Takahashi, R., Miyabayashi, K., Yamamoto, K., Asaoka, Y., Ijichi, H., Tateishi, R., et al. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.76 · Cited by 34
A six-mRNA signature model for the prognosis of head and neck squamous cell carcinoma
Guo, W., Chen, X., Zhu, L., & Wang, Q. (2017) · Oncotarget · doi:10.18632/oncotarget.21786 · Cited by 34
A Five-Gene Signature Predicts Prognosis in Patients with Kidney Renal Clear Cell Carcinoma
Zhan, Y., Guo, W., Zhang, Y., Wang, Q., Xu, X., & Zhu, L. (2015) · Computational and Mathematical Methods in Medicine · doi:10.1155/2015/842784 · Cited by 29
Bii, V. M., Rae, D. T., & Trobridge, G. D. (2015) · Oncotarget · doi:10.18632/oncotarget.6232 · Cited by 28
Song, X., & Lin, Q. (2022) · Technology in Cancer Research & Treatment · doi:10.1177/15330338221090351 · Cited by 23
Expression of the three components of linear ubiquitin assembly complex in breast cancer
Razavirad, A., Gao, H., Ghiasvand, R., Haldosén, L.-A., & Zendehdel, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0197183 · Cited by 18
Zhang, L., Liu, Q., Liu, K., Qin, Z., Zhu, G.-X., Shen, L., Zhang, N., Liu, B.-Y., Che, L., Li, J.-Y., et al. (2020) · Gastric Cancer · doi:10.1007/s10120-020-01138-5 · Cited by 18
Keratinocyte-specific deletion of SHARPIN induces atopic dermatitis-like inflammation in mice
Sundberg, J. P., Pratt, C. H., Goodwin, L. O., Silva, K. A., Kennedy, V. E., Potter, C. S., Dunham, A. D., Sundberg, B. A., & HogenEsch, H. (2020) · PLoS ONE · doi:10.1371/journal.pone.0235295 · Cited by 17
Kang, K., Lee, S., Piao, X., & Hur, G. M. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-018-01107-8 · Cited by 17
Matrine in cancer therapy: antitumor mechanisms and nano-delivery strategies
Meng, D., Cui, Z., Li, L., Shang, Q., & Chen, X. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1656862 · Cited by 14
68Ga-DOTA-E[c(RGDfK)]2 PET Imaging of SHARPIN-Regulated Integrin Activity in Mice
Viitanen, R., Peuhu, E., Autio, A. K., Liljenbäck, H., Mattila, E., Metsälä, O., Käkelä, M., Saanijoki, T., Dijkgraaf, I., Jalkanen, S., et al. (2019) · Journal of Nuclear Medicine · doi:10.2967/jnumed.118.222026 · Cited by 14
The Sharpin interactome reveals a role for Sharpin in lamellipodium formation via the Arp2/3 complex
Khan, M. H., Salomaa, S. I., Jacquemet, G., Butt, U., Miihkinen, M., Deguchi, T., Kremneva, E., Lappalainen, P., Humphries, M. J., & Pouwels, J. (2017) · Journal of Cell Science · doi:10.1242/jcs.200329 · Cited by 14
Krishnan, D., Menon, R. N., & Gopala, S. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-01023-w · Cited by 12
Ojo, D., Seliman, M., & Tang, D. (2017) · BBA Clinical · doi:10.1016/j.bbacli.2017.07.004 · Cited by 11
Self-citationA role of SIPL1/SHARPIN in promoting resistance to hormone therapy in breast cancer
Ojo, D., Wu, Y., Bane, A. L., & Tang, D. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.12.018 · Cited by 11
Self-citationCancer invasion and metastasis: Insights from murine pubertal mammary gland morphogenesis
Githaka, J. M., Pirayeshfard, L., & Goping, I. S. (2023) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2023.130375 · Cited by 10
Zhang, J., Xu, M., Gao, H. J., Guo, J., Guo, Y., Zou, M., & Wu, X. (2018) · Oncology Letters · doi:10.3892/ol.2018.7778 · Cited by 10
Shen, J., Wang, M., Li, F., Yan, H., & Zhou, J. (2022) · Bioengineered · doi:10.1080/21655979.2021.2016088 · Cited by 8
RetractedZhou, Y.-C., Wang, Q.-Q., Zhou, G.-Y.-J., Yin, T., Zhao, D.-Y., Sun, X., Tan, C., Zhou, L., & Yao, S. (2024) · World Journal of Gastrointestinal Oncology · doi:10.4251/wjgo.v16.i12.4700 · Cited by 7
Chen, B., Zheng, Y., Zhu, J., & Liang, Y. (2019) · Experimental Dermatology · doi:10.1111/exd.14026 · Cited by 7
SHARPIN S146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis
Butt, U., Khan, M. H., Pouwels, J., & Westermarck, J. (2022) · Journal of Cell Science · doi:10.1242/jcs.260627 · Cited by 6
Identifying Cancer Driver Genes Using Replication-Incompetent Retroviral Vectors
Bii, V. M., & Trobridge, G. D. (2016) · Cancers · doi:10.3390/cancers8110099 · Cited by 5
Aberrant expression and high‑frequency mutations of SHARPIN in nonmelanoma skin cancer
Zheng, Y., Yang, Y., Wang, J., & Liang, Y. (2019) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2019.7261 · Cited by 5
Yang, Y., Liang, Y., Zheng, Y., Tang, L., Zhou, S., & Zhu, J. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.10981 · Cited by 5
Liang, Y., Chen, B., Liu, F., Wang, J., Yang, Y., Zheng, Y., & Tan, S. (2018) · Oncology Letters · doi:10.3892/ol.2018.9514 · Cited by 4
WITHDRAWN: Overexpression of SHARPIN promotes tumor progression in ovarian cancer
Wang, G., Zhuang, Z., Cheng, J., Yang, F., Zhu, D., Jiang, Z., Du, W., Shen, S., Huang, J., Hua, L., et al. (2022) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2022.104806 · Cited by 2
RetractedEmerging role of SHARPIN in hepatocellular carcinoma progression
Tanaka, Y., Tateishi, R., & Koike, K. (2017) · Cancer Cell & Microenvironment · doi:10.14800/ccm.1540 · Cited by 1
SHARPIN serine 146 phosphorylation mediates ARP2/3 interaction, cancer cell invasion and metastasis
Butt, U., Khan, M. H., Pouwels, J., & Westermarck, J. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.21.477220 · Cited by 6
“S1A) (Bii et al., 2015, De Melo & Tang, 2015, He et al., 2010, Jung et al., 2010).”
Crosstalk between cell adhesion and the actin cytoskeleton
Salomaa, S. I. (2020) · UTUPub (University of Turku)
Metadata
- Authors
- De Melo, J., & Tang, D.
- Affiliations
- St. Joseph’s Healthcare Hamilton (CA)
- Corresponding author
- Tang, Damu
- ORCID
- Tang, Damu
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-05-19
- Volume
- 10
- Issue
- 5
- Pages
- e0127546
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4438068
- OpenAlex
- W227156250
- Cited by
- 33
- References
- 80
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 6 · 2018: 3 · 2017: 8 · 2016: 3 · 2015: 2
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- Canadian Institutes of Health Research (107971)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Breast Cancer Treatment Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Endocrinology › Estrogen and related hormone effects
- Health Sciences › Medicine › Pathology and Forensic Medicine › Breast Lesions and Carcinomas
- Keywords
- SHARPIN, breast cancer, carcinogenesis, gene amplification, mRNA expression, breast cancer subtypes, progesterone receptor, estrogen receptor, HER2, triple-negative breast cancer, Akt activation, progesterone, MCF-7 cells, patient survival, tumor grade
- MeSH terms
- Breast Neoplasms, Female, Gene Amplification, Humans, Risk Factors, RNA, Messenger, Ubiquitins, Up-Regulation, Survival Rate, Disease Progression, MCF-7 Cells
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