Pan-cancer analysis of the prognostic and immunological roles of SHP-1/ptpn6.
ptpn6
Immune infiltration
Pan-cancer
Prognosis
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
04 Oct 2024
04 Oct 2024
Historique:
received:
04
06
2024
accepted:
23
09
2024
medline:
5
10
2024
pubmed:
5
10
2024
entrez:
4
10
2024
Statut:
epublish
Résumé
SHP-1, a nonreceptor protein tyrosine phosphatase encoded by ptpn6, has been regarded as a regulatory protein of hematopoietic cell biology for years. However, there is now increasing evidence to support its role in tumors. Thus, the role of ptpn6 for prognosis and immune regulation across 33 tumors was investigated, aiming to explore its functional heterogeneity and clinical significance in pan-cancer. Differential expression of ptpn6 was found between cancer and adjacent normal tissues, and its expression was significantly correlated with the prognosis of tumor patients. In most cancers, ptpn6 expression was significantly associated with immune infiltration. This was further confirmed by ptpn6-related genes/proteins enrichment analysis. Additionally, genetic alterations in ptpn6 was observed in most cancers. As for epigenetic changes, it's phosphorylation levels significantly altered in 6 tumors, while methylation levels significantly altered in 12 tumors. Notably, the methylation levels of ptpn6 were significantly decreased in 11 tumors, accompanied by its increased expression in 8 of them, suggesting that the hypomethylation may be related to its increased expression. Our results show that ptpn6 plays a specific role in tumor immunity and exerts a pleiotropic effect in a variety of tumors. It can serve as a prognostic factor for some cancers. Especially in LGG, KIRC, UCS and TGCT, the increased expression of ptpn6 is associated with poor prognosis and high immune infiltration. This aids in understanding the role of ptpn6 in tumor biology, and can provide insight into presenting a potential biomarker for poor prognosis and immune infiltration in cancers.
Identifiants
pubmed: 39367146
doi: 10.1038/s41598-024-74037-9
pii: 10.1038/s41598-024-74037-9
doi:
Substances chimiques
Protein Tyrosine Phosphatase, Non-Receptor Type 6
EC 3.1.3.48
PTPN6 protein, human
EC 3.1.3.48
Biomarkers, Tumor
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
23083Subventions
Organisme : the National Natural Science Foundation of China
ID : NSFC 82002134
Organisme : One Thousand of Young and Middle-aged Key Teachers Training Program in Guangxi Colleges and Universities
ID : DC2300017000
Organisme : 2022 Innovation and Entrepreneurship Training Program of Guangxi Medical University
ID : 202210598034
Organisme : 2022 Innovation and Entrepreneurship Training Program of Guangxi Medical University
ID : 202210598034
Organisme : National Natural Science Foundation of Guangxi
ID : 2023GXNSFDA026036
Informations de copyright
© 2024. The Author(s).
Références
Bray, F. et al. Global cancer statistics 2018: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. Cancer J. Clin. 68, 394–424. https://doi.org/10.3322/caac.21492 (2018).
doi: 10.3322/caac.21492
Dumitrescu, R. G. in Cancer Epigenetics for Precision Medicine: Methods and Protocols (eds Ramona G. Dumitrescu & Mukesh Verma) 3–17. (Springer New York, 2018).
Costa-Pinheiro, P., Montezuma, D., Henrique, R. & Jerónimo, C. Diagnostic and prognostic epigenetic biomarkers in cancer. Epigenomics 7, 1003–1015. https://doi.org/10.2217/epi.15.56 (2015).
doi: 10.2217/epi.15.56
pubmed: 26479312
Sharma, Y., Bashir, S., Bhardwaj, P., Ahmad, A. & Khan, F. Protein tyrosine phosphatase SHP-1: resurgence as new drug target for human autoimmune disorders. Immunol. Res. 64, 804–819. https://doi.org/10.1007/s12026-016-8805-y (2016).
doi: 10.1007/s12026-016-8805-y
pubmed: 27216862
He, R. J., Yu, Z. H., Zhang, R. Y. & Zhang, Z. Y. Protein tyrosine phosphatases as potential therapeutic targets. Acta Pharmacol. Sin. 35, 1227–1246. https://doi.org/10.1038/aps.2014.80 (2014).
doi: 10.1038/aps.2014.80
pubmed: 25220640
Marín-Juez, R., Jong-Raadsen, S., Yang, S. & Spaink, H. P. Hyperinsulinemia induces insulin resistance and immune suppression via Ptpn6/Shp1 in zebrafish. J. Endocrinol. 222, 229–241. https://doi.org/10.1530/joe-14-0178 (2014).
doi: 10.1530/joe-14-0178
pubmed: 24904114
Lorenz, U. SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels. Immunol. Rev. 228, 342–359. https://doi.org/10.1111/j.1600-065X.2008.00760.x (2009).
doi: 10.1111/j.1600-065X.2008.00760.x
pubmed: 19290938
Abram, C. L. & Lowell, C. A. Shp1 function in myeloid cells. J. Leukoc. Biol. 102, 657–675. https://doi.org/10.1189/jlb.2MR0317-105R (2017).
doi: 10.1189/jlb.2MR0317-105R
pubmed: 28606940
Garg, M., Wahid, M. & Khan, F. D. Regulation of peripheral and central immunity: understanding the role of src homology 2 domain-containing tyrosine phosphatases, SHP-1 & SHP-2. Immunobiology 225, 151847. https://doi.org/10.1016/j.imbio.2019.09.006 (2020).
doi: 10.1016/j.imbio.2019.09.006
pubmed: 31561841
Wu, C., Guan, Q., Wang, Y., Zhao, Z. J. & Zhou, G. W. SHP-1 suppresses cancer cell growth by promoting degradation of JAK kinases. J. Cell. Biochem. 90, 1026–1037. https://doi.org/10.1002/jcb.10727 (2003).
doi: 10.1002/jcb.10727
pubmed: 14624462
Wang, F. et al. Comprehensive analysis of PTPN gene family revealing PTPN7 as a novel biomarker for immuno-hot tumors in breast cancer. Front. Genet. 13, 981603. https://doi.org/10.3389/fgene.2022.981603 (2022).
doi: 10.3389/fgene.2022.981603
pubmed: 36226189
Mok, S. C., Kwok, T. T., Berkowitz, R. S., Barrett, A. J. & Tsui, F. W. Overexpression of the protein tyrosine phosphatase, nonreceptor type 6 (PTPN6), in human epithelial ovarian cancer. Gynecol. Oncol. 57, 299–303. https://doi.org/10.1006/gyno.1995.1146 (1995).
doi: 10.1006/gyno.1995.1146
pubmed: 7774833
Xu, S. B. et al. DNA methylation regulates constitutive expression of Stat6 regulatory genes SOCS-1 and SHP-1 in colon cancer cells. J. Cancer Res. Clin. Oncol. 135, 1791–1798. https://doi.org/10.1007/s00432-009-0627-z (2009).
doi: 10.1007/s00432-009-0627-z
pubmed: 19551406
Li, Y. et al. Methylation and decreased expression of SHP-1 are related to disease progression in chronic myelogenous leukemia. Oncol. Rep. 31, 2438–2446. https://doi.org/10.3892/or.2014.3098 (2014).
doi: 10.3892/or.2014.3098
pubmed: 24647617
Zhang, Q. et al. STAT3- and DNA methyltransferase 1-mediated epigenetic silencing of SHP-1 tyrosine phosphatase tumor suppressor gene in malignant T lymphocytes. Proc. Natl. Acad. Sci. U. S. A. 102, 6948–6953. https://doi.org/10.1073/pnas.0501959102 (2005).
doi: 10.1073/pnas.0501959102
pubmed: 15870198
Wen, L. Z. et al. SHP-1 acts as a tumor suppressor in Hepatocarcinogenesis and HCC Progression. Cancer Res. 78, 4680–4691. https://doi.org/10.1158/0008-5472.Can-17-3896 (2018).
doi: 10.1158/0008-5472.Can-17-3896
pubmed: 29776962
Fang, H., Ma, W., Guo, X. & Wang, J. PTPN6 promotes chemosensitivity of colorectal cancer cells via inhibiting the SP1/MAPK signalling pathway. Cell Biochem. Funct. 39, 392–400. https://doi.org/10.1002/cbf.3604 (2021).
doi: 10.1002/cbf.3604
pubmed: 33615510
Wu, C., Sun, M., Liu, L. & Zhou, G. W. The function of the protein tyrosine phosphatase SHP-1 in cancer. Gene 306, 1–12. https://doi.org/10.1016/s0378-1119(03)00400-1 (2003).
doi: 10.1016/s0378-1119(03)00400-1
pubmed: 12657462
Peng, D. H. et al. Collagen promotes anti-PD-1/PD-L1 resistance in cancer through LAIR1-dependent CD8(+) T cell exhaustion. Nat. Commun. 11, 4520. https://doi.org/10.1038/s41467-020-18298-8 (2020).
doi: 10.1038/s41467-020-18298-8
pubmed: 32908154
Acharya, N. et al. Endogenous glucocorticoid signaling regulates CD8(+) T cell differentiation and development of dysfunction in the Tumor Microenvironment. Immunity 53, 658–671e656. https://doi.org/10.1016/j.immuni.2020.08.005 (2020).
doi: 10.1016/j.immuni.2020.08.005
pubmed: 32937153
pmcid: 7682805
Zhang, L. et al. Novel targets for immunotherapy associated with exhausted CD8 + T cells in cancer. J. Cancer Res. Clin. Oncol. 149, 2243–2258. https://doi.org/10.1007/s00432-022-04326-1 (2023).
doi: 10.1007/s00432-022-04326-1
pubmed: 36107246
Snook, J. P., Soedel, A. J., Ekiz, H. A., O’Connell, R. M. & Williams, M. A. Inhibition of SHP-1 expands the Repertoire of Antitumor T Cells Available to Respond to Immune Checkpoint Blockade. Cancer Immunol. Res. 8, 506–517. https://doi.org/10.1158/2326-6066.Cir-19-0690 (2020).
doi: 10.1158/2326-6066.Cir-19-0690
pubmed: 32075800
pmcid: 7125038
Watson, H. A., Wehenkel, S., Matthews, J. & Ager, A. SHP-1: the next checkpoint target for cancer immunotherapy? Biochem. Soc. Trans. 44, 356–362. https://doi.org/10.1042/bst20150251 (2016).
doi: 10.1042/bst20150251
pubmed: 27068940
pmcid: 5264497
Vasiljević, N., Scibior-Bentkowska, D., Brentnall, A. R., Cuzick, J. & Lorincz, A. T. Credentialing of DNA methylation assays for human genes as diagnostic biomarkers of cervical intraepithelial neoplasia in high-risk HPV positive women. Gynecol. Oncol. 132, 709–714. https://doi.org/10.1016/j.ygyno.2014.02.001 (2014).
doi: 10.1016/j.ygyno.2014.02.001
pubmed: 24508839
Tang, Z., Kang, B., Li, C., Chen, T. & Zhang, Z. GEPIA2: an enhanced web server for large-scale expression profiling and interactive analysis. Nucleic Acids Res. 47, W556–w560. https://doi.org/10.1093/nar/gkz430 (2019).
doi: 10.1093/nar/gkz430
pubmed: 31114875
Hou, G. X., Liu, P., Yang, J. & Wen, S. Mining expression and prognosis of topoisomerase isoforms in non-small-cell lung cancer by using Oncomine and Kaplan-Meier plotter. PloS One 12, e0174515. https://doi.org/10.1371/journal.pone.0174515 (2017).
doi: 10.1371/journal.pone.0174515
pubmed: 28355294
Peng, L. et al. A Pan-cancer analysis of SMARCA4 alterations in human cancers. Front. Immunol. 12, 762598. https://doi.org/10.3389/fimmu.2021.762598 (2021).
doi: 10.3389/fimmu.2021.762598
pubmed: 34675941
Li, T. et al. TIMER2.0 for analysis of tumor-infiltrating immune cells. Nucleic Acids Res. 48, W509–w514. https://doi.org/10.1093/nar/gkaa407 (2020).
doi: 10.1093/nar/gkaa407
pubmed: 32442275
Szklarczyk, D. et al. The STRING database in 2021: customizable protein-protein networks, and functional characterization of user-uploaded gene/measurement sets. Nucleic Acids Res. 49, D605–d612. https://doi.org/10.1093/nar/gkaa1074 (2021).
doi: 10.1093/nar/gkaa1074
pubmed: 33237311
Bardou, P., Mariette, J., Escudié, F., Djemiel, C. & Klopp, C. Jvenn: an interactive Venn diagram viewer. BMC Bioinform. 15, 293. https://doi.org/10.1186/1471-2105-15-293 (2014).
doi: 10.1186/1471-2105-15-293
Kanehisa, M. Toward understanding the origin and evolution of cellular organisms. Protein Sci. Publ. Protein Soc. 28, 1947–1951. https://doi.org/10.1002/pro.3715 (2019).
doi: 10.1002/pro.3715
Kanehisa, M., Furumichi, M., Sato, Y., Kawashima, M. & Ishiguro-Watanabe, M. KEGG for taxonomy-based analysis of pathways and genomes. Nucleic Acids Res. 51, D587–d592. https://doi.org/10.1093/nar/gkac963 (2023).
doi: 10.1093/nar/gkac963
pubmed: 36300620
Kanehisa, M. & Goto, S. KEGG: kyoto encyclopedia of genes and genomes. Nucleic Acids Res. 28, 27–30. https://doi.org/10.1093/nar/28.1.27 (2000).
doi: 10.1093/nar/28.1.27
pubmed: 10592173
pmcid: 102409
Yuan, H. et al. CancerSEA: a cancer single-cell state atlas. Nucleic Acids Res. 47, D900–d908. https://doi.org/10.1093/nar/gky939 (2019).
doi: 10.1093/nar/gky939
pubmed: 30329142
Cerami, E. et al. The cBio cancer genomics portal: an open platform for exploring multidimensional cancer genomics data. Cancer Discov. 2, 401–404. https://doi.org/10.1158/2159-8290.Cd-12-0095 (2012).
doi: 10.1158/2159-8290.Cd-12-0095
pubmed: 22588877
Chandrashekar, D. S. et al. An update to the integrated cancer data analysis platform. Neoplasia (New York N Y) 25 UALCAN, 18–27. https://doi.org/10.1016/j.neo.2022.01.001 (2022).
doi: 10.1016/j.neo.2022.01.001
Uhlén, M. et al. Proteomics. Tissue-based map of the human proteome. Science 347, 1260419. https://doi.org/10.1126/science.1260419 (2015).
doi: 10.1126/science.1260419
pubmed: 25613900
Uhlen, M. et al. A pathology atlas of the human cancer transcriptome. Science 357 https://doi.org/10.1126/science.aan2507 (2017).
Pan, T. et al. Identification and validation of a prognostic gene signature for diffuse large B-Cell lymphoma based on Tumor Microenvironment-related genes. Front. Oncol. 11, 614211. https://doi.org/10.3389/fonc.2021.614211 (2021).
doi: 10.3389/fonc.2021.614211
pubmed: 33692952
pmcid: 7938316
Mao, X. et al. Crosstalk between cancer-associated fibroblasts and immune cells in the tumor microenvironment: new findings and future perspectives. Mol. Cancer 20, 131. https://doi.org/10.1186/s12943-021-01428-1 (2021).
doi: 10.1186/s12943-021-01428-1
pubmed: 34635121
Yao, J. et al. Development and validation of a prognostic gene signature correlated with M2 macrophage infiltration in esophageal squamous cell carcinoma. Front. Oncol. 11, 769727. https://doi.org/10.3389/fonc.2021.769727 (2021).
doi: 10.3389/fonc.2021.769727
pubmed: 34926275
Zhang, C. et al. Tumor Purity as an underlying key factor in Glioma. Clin. Cancer Res. 23, 6279–6291. https://doi.org/10.1158/1078-0432.Ccr-16-2598 (2017).
doi: 10.1158/1078-0432.Ccr-16-2598
pubmed: 28754819
Mao, Y. et al. Low tumor purity is associated with poor prognosis, heavy mutation burden, and intense immune phenotype in colon cancer. Cancer Manag. Res. 10, 3569–3577. https://doi.org/10.2147/CMAR.S171855 (2018).
doi: 10.2147/CMAR.S171855
pubmed: 30271205
Zhao, K., Ma, Z. & Zhang, W. Comprehensive Analysis to identify SPP1 as a Prognostic Biomarker in Cervical Cancer. Front. Genet. 12, 732822. https://doi.org/10.3389/fgene.2021.732822 (2021).
doi: 10.3389/fgene.2021.732822
pubmed: 35058964
Koch, A. et al. Analysis of DNA methylation in cancer: location revisited. Nat. Rev. Clin. Oncol. 15, 459–466. https://doi.org/10.1038/s41571-018-0004-4 (2018).
doi: 10.1038/s41571-018-0004-4
pubmed: 29666440
Feng, G. S. et al. Receptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Syp. Oncogene 9, 1545–1550 (1994).
pubmed: 8183548
Wu, W. et al. SHP1 loss augments DLBCL cellular response to ibrutinib: a candidate predictive biomarker. Oncogene 42, 409–420. https://doi.org/10.1038/s41388-022-02565-7 (2023).
doi: 10.1038/s41388-022-02565-7
pubmed: 36482202
Shen, C. et al. The Analysis of PTPN6 for Bladder Cancer: An Exploratory Study Based on TCGA. Disease markers 4312629. https://doi.org/10.1155/2020/4312629 (2020).
Liu, C. Y. et al. Sorafenib analogue SC-60 induces apoptosis through the SHP-1/STAT3 pathway and enhances docetaxel cytotoxicity in triple-negative breast cancer cells. Mol. Oncol. 11, 266–279. https://doi.org/10.1002/1878-0261.12033 (2017).
doi: 10.1002/1878-0261.12033
pubmed: 28084011
Tao, T. et al. PDZK1 inhibits the development and progression of renal cell carcinoma by suppression of SHP-1 phosphorylation. Oncogene 36, 6119–6131. https://doi.org/10.1038/onc.2017.199 (2017).
doi: 10.1038/onc.2017.199
pubmed: 28692056
Huang, Z. et al. Knockdown of RNF6 inhibits gastric cancer cell growth by suppressing STAT3 signaling. OncoTargets Therapy 11, 6579–6587. https://doi.org/10.2147/ott.S174846 (2018).
doi: 10.2147/ott.S174846
pubmed: 30323630
Sooman, L. et al. PTPN6 expression is epigenetically regulated and influences survival and response to chemotherapy in high-grade gliomas. Tumour Biol. J. Int. Soc. Oncodev. Biol. Med. 35, 4479–4488. https://doi.org/10.1007/s13277-013-1590-5 (2014).
doi: 10.1007/s13277-013-1590-5
Shanmugam, M. K. et al. Abrogation of STAT3 signaling cascade by zerumbone inhibits proliferation and induces apoptosis in renal cell carcinoma xenograft mouse model. Mol. Carcinog. 54, 971–985. https://doi.org/10.1002/mc.22166 (2015).
doi: 10.1002/mc.22166
pubmed: 24797723
Sheng, Y. et al. Methylation of tumor suppressor gene CDH13 and SHP1 promoters and their epigenetic regulation by the UHRF1/PRMT5 complex in endometrial carcinoma. Gynecol. Oncol. 140, 145–151. https://doi.org/10.1016/j.ygyno.2015.11.017 (2016).
doi: 10.1016/j.ygyno.2015.11.017
pubmed: 26597461
Marx, A. et al. Thymus and autoimmunity. Semin. Immunopathol. 43, 45–64. https://doi.org/10.1007/s00281-021-00842-3 (2021).
doi: 10.1007/s00281-021-00842-3
pubmed: 33537838
Lougaris, V., Baronio, M., Gazzurelli, L., Benvenuto, A. & Plebani, A. RAC2 and primary human immune deficiencies. J. Leukoc. Biol. 108, 687–696. https://doi.org/10.1002/jlb.5mr0520-194rr (2020).
doi: 10.1002/jlb.5mr0520-194rr
pubmed: 32542921
Muro, R., Nitta, T., Kitajima, M., Okada, T. & Suzuki, H. Rasal3-mediated T cell survival is essential for inflammatory responses. Biochem. Biophys. Res. Commun. 496, 25–30. https://doi.org/10.1016/j.bbrc.2017.12.159 (2018).
doi: 10.1016/j.bbrc.2017.12.159
pubmed: 29291408
Wang, J. et al. ArhGAP30 promotes p53 acetylation and function in colorectal cancer. Nat. Commun. 5, 4735. https://doi.org/10.1038/ncomms5735 (2014).
doi: 10.1038/ncomms5735
pubmed: 25156493
Sun, J. et al. ARHGAP9 inhibits colorectal cancer cell proliferation, invasion and EMT via targeting PI3K/AKT/mTOR signaling pathway. Tissue Cell. 77, 101817. https://doi.org/10.1016/j.tice.2022.101817 (2022).
doi: 10.1016/j.tice.2022.101817
pubmed: 35679685
Zhang, H. et al. ARHGAP9 suppresses the migration and invasion of hepatocellular carcinoma cells through up-regulating FOXJ2/E-cadherin. Cell Death Dis. 9 https://doi.org/10.1038/s41419-018-0976-0 (2018).
Lu, C. et al. FERMT3 contributes to glioblastoma cell proliferation and chemoresistance to temozolomide through integrin mediated wnt signaling. Neurosci. Lett. 657, 77–83. https://doi.org/10.1016/j.neulet.2017.07.057 (2017).
doi: 10.1016/j.neulet.2017.07.057
pubmed: 28778805
Farago, M., Yarnitzky, T., Shalom, B. & Katzav, S. Vav1 mutations: what makes them oncogenic? Cell. Signal. 65, 109438. https://doi.org/10.1016/j.cellsig.2019.109438 (2020).
doi: 10.1016/j.cellsig.2019.109438
pubmed: 31654719
Fan, T., Li, C. & He, J. Prognostic value of immune-related genes and comparative analysis of immune cell infiltration in lung adenocarcinoma: sex differences. Biology sex. Differences 12, 64. https://doi.org/10.1186/s13293-021-00406-y (2021).
doi: 10.1186/s13293-021-00406-y
Wang, Z. & Peng, M. A novel prognostic biomarker LCP2 correlates with metastatic melanoma-infiltrating CD8(+) T cells. Sci. Rep. 11, 9164. https://doi.org/10.1038/s41598-021-88676-9 (2021).
doi: 10.1038/s41598-021-88676-9
pubmed: 33911146
pmcid: 8080722
Warnecke, P. M. & Bestor, T. H. Cytosine methylation and human cancer. Curr. Opin. Oncol. 12, 68–73. https://doi.org/10.1097/00001622-200001000-00012 (2000).
doi: 10.1097/00001622-200001000-00012
pubmed: 10687732
Parris, T. Z. et al. Frequent MYC coamplification and DNA hypomethylation of multiple genes on 8q in 8p11-p12-amplified breast carcinomas. Oncogenesis 3, e95. https://doi.org/10.1038/oncsis.2014.8 (2014).
doi: 10.1038/oncsis.2014.8
pubmed: 24662924
pmcid: 4038389
El-Osta, A., Baker, E. K. & Wolffe, A. P. Profiling methyl-CpG specific determinants on transcriptionally silent chromatin. Mol. Biol. Rep. 28, 209–215. https://doi.org/10.1023/a:1015744625049 (2001).
doi: 10.1023/a:1015744625049
pubmed: 12153140
Oka, T. et al. Gene silencing of the tyrosine phosphatase SHP1 gene by aberrant methylation in leukemias/lymphomas. Cancer Res. 62, 6390–6394 (2002).
pubmed: 12438221
Ding, K. et al. Plasma DNA methylation of p16 and shp1 in patients with B cell non-hodgkin lymphoma. Int. J. Clin. Oncol. 22, 585–592. https://doi.org/10.1007/s10147-017-1100-7 (2017).
doi: 10.1007/s10147-017-1100-7
pubmed: 28210822
Liu, J. et al. Promoter methylation attenuates SHP1 expression and function in patients with primary central nervous system lymphoma. Oncol. Rep. 37, 887–894. https://doi.org/10.3892/or.2016.5308 (2017).
doi: 10.3892/or.2016.5308
pubmed: 27959415
Liu, L., Zhang, S., Liu, X. & Liu, J. Aberrant promoter 2 methylation–mediated downregulation of protein tyrosine phosphatase, non–receptor type 6, is associated with progression of esophageal squamous cell carcinoma. Mol. Med. Rep. 19, 3273–3282. https://doi.org/10.3892/mmr.2019.9971 (2019).
doi: 10.3892/mmr.2019.9971
pubmed: 30816454
Joo, M. K. et al. Epigenetic regulation and anti-tumorigenic effects of SH2-containing protein tyrosine phosphatase 1 (SHP1) in human gastric cancer cells. Tumour Biol. J. Int. Soc. Oncodev. Biol. Med. 37, 4603–4612. https://doi.org/10.1007/s13277-015-4228-y (2016).
doi: 10.1007/s13277-015-4228-y
Hachana, M., Trimeche, M., Ziadi, S., Amara, K. & Korbi, S. Evidence for a role of the Simian Virus 40 in human breast carcinomas. Breast Cancer Res. Treat. 113, 43–58. https://doi.org/10.1007/s10549-008-9901-z (2009).
doi: 10.1007/s10549-008-9901-z
pubmed: 18205041
Challouf, S. et al. Patterns of aberrant DNA hypermethylation in nasopharyngeal carcinoma in Tunisian patients. Clin. Chim. Acta 413, 795–802. https://doi.org/10.1016/j.cca.2012.01.018 (2012).
doi: 10.1016/j.cca.2012.01.018
pubmed: 22296674
Zhang, M. et al. SHP1 decreases level of P-STAT3 (Ser727) and inhibits Proliferation and Migration of Pancreatic Cancer cells. J. Environ. Pathol. Toxicol. Oncology: Official Organ. Int. Soc. Environ. Toxicol. Cancer 40, 17–27. https://doi.org/10.1615/JEnvironPatholToxicolOncol.2020035980 (2021).
doi: 10.1615/JEnvironPatholToxicolOncol.2020035980
Myers, D. R. et al. Shp1 loss enhances macrophage effector function and promotes Anti-tumor Immunity. Front. Immunol. 11. https://doi.org/10.3389/fimmu.2020.576310 (2020).
Chen, J., Zhao, X., Yuan, Y. & Jing, J. J. The expression patterns and the diagnostic/prognostic roles of PTPN family members in digestive tract cancers. Cancer Cell Int. 20, 238. https://doi.org/10.1186/s12935-020-01315-7 (2020).
doi: 10.1186/s12935-020-01315-7
pubmed: 32536826
pmcid: 7291430