DUSP12 Rabbit Pab

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Leader in Biomolecular Solutions for Life Science DUSP12 Rabbit pAb Catalog No.: A13247 1 Publications Basic Information Background Catalog No. The protein encoded by this gene is a member of the dual specificity protein A13247 phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. Observed MW They negatively regulate members of the mitogen-activated protein (MAP) kinase 36kDa superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases Calculated MW show distinct substrate specificities for various MAP kinases, different tissue distribution 37kDa and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product is the human ortholog of the Saccharomyces Category cerevisiae YVH1 protein tyrosine phosphatase. It is localized predominantly in the nucleus, and is novel in that it contains, and is regulated by a zinc finger domain. Primary antibody Applications WB Cross-Reactivity Human, Mouse Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 11266 Q9UNI6 Immunogen Recombinant fusion protein containing a sequence corresponding to amino acids 130-270 of human DUSP12 (NP_009171.1). Synonyms DUSP12;DUSP1;YVH1 Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using DUSP12 antibody (A13247) at 1:3000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 30s. Antibody | Protein | ELISA Kits | Enzyme | NGS | Service For research use only. Not for therapeutic or diagnostic purposes. Please visit http://abclonal.com for a complete listing of recommended products..

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A Computational Approach for Defining a Signature of Β-Cell Golgi Stress in Diabetes Mellitus
Page 1 of 781 Diabetes A Computational Approach for Defining a Signature of β-Cell Golgi Stress in Diabetes Mellitus Robert N. Bone1,6,7, Olufunmilola Oyebamiji2, Sayali Talware2, Sharmila Selvaraj2, Preethi Krishnan3,6, Farooq Syed1,6,7, Huanmei Wu2, Carmella Evans-Molina 1,3,4,5,6,7,8* Departments of 1Pediatrics, 3Medicine, 4Anatomy, Cell Biology & Physiology, 5Biochemistry & Molecular Biology, the 6Center for Diabetes & Metabolic Diseases, and the 7Herman B. Wells Center for Pediatric Research, Indiana University School of Medicine, Indianapolis, IN 46202; 2Department of BioHealth Informatics, Indiana University-Purdue University Indianapolis, Indianapolis, IN, 46202; 8Roudebush VA Medical Center, Indianapolis, IN 46202. *Corresponding Author(s): Carmella Evans-Molina, MD, PhD ([email protected]) Indiana University School of Medicine, 635 Barnhill Drive, MS 2031A, Indianapolis, IN 46202, Telephone: (317) 274-4145, Fax (317) 274-4107 Running Title: Golgi Stress Response in Diabetes Word Count: 4358 Number of Figures: 6 Keywords: Golgi apparatus stress, Islets, β cell, Type 1 diabetes, Type 2 diabetes 1 Diabetes Publish Ahead of Print, published online August 20, 2020 Diabetes Page 2 of 781 ABSTRACT The Golgi apparatus (GA) is an important site of insulin processing and granule maturation, but whether GA organelle dysfunction and GA stress are present in the diabetic β-cell has not been tested. We utilized an informatics-based approach to develop a transcriptional signature of β-cell GA stress using existing RNA sequencing and microarray datasets generated using human islets from donors with diabetes and islets where type 1(T1D) and type 2 diabetes (T2D) had been modeled ex vivo. To narrow our results to GA-specific genes, we applied a filter set of 1,030 genes accepted as GA associated.
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9. Atypical Dusps: 19 Phosphatases in Search of a Role
View metadata, citation and similar papers at core.ac.uk brought to you by CORE provided by Digital.CSIC Transworld Research Network 37/661 (2), Fort P.O. Trivandrum-695 023 Kerala, India Emerging Signaling Pathways in Tumor Biology, 2010: 185-208 ISBN: 978-81-7895-477-6 Editor: Pedro A. Lazo 9. Atypical DUSPs: 19 phosphatases in search of a role Yolanda Bayón and Andrés Alonso Instituto de Biología y Genética Molecular, CSIC-Universidad de Valladolid c/ Sanz y Forés s/n, 47003 Valladolid, Spain Abstract. Atypical Dual Specificity Phosphatases (A-DUSPs) are a group of 19 phosphatases poorly characterized. They are included among the Class I Cys-based PTPs and contain the active site motif HCXXGXXR conserved in the Class I PTPs. These enzymes present a phosphatase domain similar to MKPs, but lack any substrate targeting domain similar to the CH2 present in this group. Although most of these phosphatases have no more than 250 amino acids, their size ranges from the 150 residues of the smallest A-DUSP, VHZ/DUSP23, to the 1158 residues of the putative PTP DUSP27. The substrates of this family include MAPK, but, in general terms, it does not look that MAPK are the general substrates for the whole group. In fact, other substrates have been described for some of these phosphatases, like the 5’CAP structure of mRNA, glycogen, or STATs and still the substrates of many A-DUSPs have not been identified. In addition to the PTP domain, most of these enzymes present no additional recognizable domains in their sequence, with the exception of CBM-20 in laforin, GTase in HCE1 and a Zn binding domain in DUSP12.
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The Emerging Role of Dual‐Specific Phosphatase 12 in the Regulation
This is a repository copy of ASKing No More: The Emerging Role of Dual‐ Specific Phosphatase 12 in the Regulation of Hepatic Lipid Metabolism. White Rose Research Online URL for this paper: http://eprints.whiterose.ac.uk/148668/ Version: Accepted Version Article: Bubici, C, Lepore, A orcid.org/0000-0002-2037-673X and Papa, S orcid.org/0000-0002-8369-6538 (2019) ASKing No More: The Emerging Role of Dual‐ Specific Phosphatase 12 in the Regulation of Hepatic Lipid Metabolism. Hepatology, 70 (4). pp. 1091-1094. ISSN 0270-9139 https://doi.org/10.1002/hep.30851 © 2019 by the American Association for the Study of Liver Diseases.. All rights reserved. This is the post-peer reviewed version of the following article: Bubici, C. , Lepore, A. and Papa, S. (2019), ASKing No More: The Emerging Role of Dual‐ Specific Phosphatase 12 in the Regulation of Hepatic Lipid Metabolism. Hepatology, 70: 1091-1094, which has been published in final form at https://doi.org/10.1002/hep.30851. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. Reuse Items deposited in White Rose Research Online are protected by copyright, with all rights reserved unless indicated otherwise. They may be downloaded and/or printed for private study, or other acts as permitted by national copyright laws. The publisher or other rights holders may allow further reproduction and re-use of the full text version. This is indicated by the licence information on the White Rose Research Online record for the item.
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Lipopolysaccharide Macrophage Responses to Tristetraprolin
Dual-Specificity Phosphatase 1 and Tristetraprolin Cooperate To Regulate Macrophage Responses to Lipopolysaccharide This information is current as of August 28, 2019. Tim Smallie, Ewan A. Ross, Alaina J. Ammit, Helen E. Cunliffe, Tina Tang, Dalya R. Rosner, Michael L. Ridley, Downloaded from Christopher D. Buckley, Jeremy Saklatvala, Jonathan L. Dean and Andrew R. Clark J Immunol 2015; 195:277-288; Prepublished online 27 May 2015; http://www.jimmunol.org/ doi: 10.4049/jimmunol.1402830 http://www.jimmunol.org/content/195/1/277 Supplementary http://www.jimmunol.org/content/suppl/2015/05/27/jimmunol.140283 Material 0.DCSupplemental at Aston Univ - SciTech Faculty Team on August 28, 2019 References This article cites 65 articles, 28 of which you can access for free at: http://www.jimmunol.org/content/195/1/277.full#ref-list-1 Why The JI? Submit online. • Rapid Reviews! 30 days* from submission to initial decision • No Triage! Every submission reviewed by practicing scientists • Fast Publication! 4 weeks from acceptance to publication *average Subscription Information about subscribing to The Journal of Immunology is online at: http://jimmunol.org/subscription Permissions Submit copyright permission requests at: http://www.aai.org/About/Publications/JI/copyright.html Email Alerts Receive free email-alerts when new articles cite this article. Sign up at: http://jimmunol.org/alerts The Journal of Immunology is published twice each month by The American Association of Immunologists, Inc., 1451 Rockville Pike, Suite 650, Rockville, MD 20852 Copyright © 2015 The Authors All rights reserved. Print ISSN: 0022-1767 Online ISSN: 1550-6606. The Journal of Immunology Dual-Speciﬁcity Phosphatase 1 and Tristetraprolin Cooperate To Regulate Macrophage Responses to Lipopolysaccharide Tim Smallie,*,1 Ewan A.
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RT² Profiler PCR Array (96-Well Format and 384-Well [4 X 96] Format)
RT² Profiler PCR Array (96-Well Format and 384-Well [4 x 96] Format) Human Protein Phosphatases Cat. no. 330231 PAHS-045ZA For pathway expression analysis Format For use with the following real-time cyclers RT² Profiler PCR Array, Applied Biosystems® models 5700, 7000, 7300, 7500, Format A 7700, 7900HT, ViiA™ 7 (96-well block); Bio-Rad® models iCycler®, iQ™5, MyiQ™, MyiQ2; Bio-Rad/MJ Research Chromo4™; Eppendorf® Mastercycler® ep realplex models 2, 2s, 4, 4s; Stratagene® models Mx3005P®, Mx3000P®; Takara TP-800 RT² Profiler PCR Array, Applied Biosystems models 7500 (Fast block), 7900HT (Fast Format C block), StepOnePlus™, ViiA 7 (Fast block) RT² Profiler PCR Array, Bio-Rad CFX96™; Bio-Rad/MJ Research models DNA Format D Engine Opticon®, DNA Engine Opticon 2; Stratagene Mx4000® RT² Profiler PCR Array, Applied Biosystems models 7900HT (384-well block), ViiA 7 Format E (384-well block); Bio-Rad CFX384™ RT² Profiler PCR Array, Roche® LightCycler® 480 (96-well block) Format F RT² Profiler PCR Array, Roche LightCycler 480 (384-well block) Format G RT² Profiler PCR Array, Fluidigm® BioMark™ Format H Sample & Assay Technologies Description The Human Protein Phosphatases RT² Profiler PCR Array profiles the gene expression of the 84 most important and well-studied phosphatases in the mammalian genome. By reversing the phosphorylation of key regulatory proteins mediated by protein kinases, phosphatases serve as a very important complement to kinases and attenuate activated signal transduction pathways. The gene classes on this array include both receptor and non-receptor tyrosine phosphatases, catalytic subunits of the three major protein phosphatase gene families, the dual specificity phosphatases, as well as cell cycle regulatory and other protein phosphatases.
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International Journal of Molecular Sciences Review Dual-Specificity Phosphatases in Immunity and Infection: An Update Roland Lang * and Faizal A.M. Raffi Institute of Clinical Microbiology, Immunology and Hygiene, Universitätsklinikum Erlangen, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91054 Erlangen, Germany * Correspondence: [email protected]; Tel.: +49-9131-85-22979 Received: 15 May 2019; Accepted: 30 May 2019; Published: 2 June 2019 Abstract: Kinase activation and phosphorylation cascades are key to initiate immune cell activation in response to recognition of antigen and sensing of microbial danger. However, for balanced and controlled immune responses, the intensity and duration of phospho-signaling has to be regulated. The dual-specificity phosphatase (DUSP) gene family has many members that are differentially expressed in resting and activated immune cells. Here, we review the progress made in the field of DUSP gene function in regulation of the immune system during the last decade. Studies in knockout mice have confirmed the essential functions of several DUSP-MAPK phosphatases (DUSP-MKP) in controlling inflammatory and anti-microbial immune responses and support the concept that individual DUSP-MKP shape and determine the outcome of innate immune responses due to context-dependent expression and selective inhibition of different mitogen-activated protein kinases (MAPK). In addition to the canonical DUSP-MKP, several small-size atypical DUSP proteins regulate immune cells and are therefore also reviewed here. Unexpected and complex findings in DUSP knockout mice pose new questions regarding cell type-specific and redundant functions. Another emerging question concerns the interaction of DUSP-MKP with non-MAPK binding partners and substrate proteins.
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Protein Tyrosine Phosphatase Profiling Studies During Brown Adipogenic Differentiation of Mouse Primary Brown Preadipocytes
BMB Rep. 2013; 46(11): 539-543 BMB www.bmbreports.org Reports Protein tyrosine phosphatase profiling studies during brown adipogenic differentiation of mouse primary brown preadipocytes Hye-Ryung Choi1, Won Kon Kim1, Anna Park1, Hyeyun Jung1, Baek Soo Han1,2, Sang Chul Lee1,2,* & Kwang-Hee Bae1,2,* 1Research Center for Integrated Cellulomics, KRIBB, 2Department of Functional Genomics, University of Science and Technology (UST), Daejeon 305-806, Korea There is a correlation between obesity and the amount of has been considered to be limited to human infants. However, brown adipose tissue; however, the molecular mechanism of mounting evidence of the existence of BAT in human adults brown adipogenic differentiation has not been as extensively has been reported (1, 2). Furthermore, a strong correlation be- studied. In this study, we performed a protein tyrosine tween obesity and the amount of BAT in the body has been re- phosphatase (PTP) profiling analysis during the brown ported by many research groups (1-3). Therefore, a deep un- adipogenic differentiation of mouse primary brown preadi- derstanding of molecular mechanisms for brown adipogenesis pocytes. Several PTPs, including PTPRF, PTPRZ, and DUSP12 is critical with regard to the treatment and prevention of showing differential expression patterns were identified. In the obesity. Research on the molecular mechanisms and signal case of DUSP12, the expression level is dramatically downre- transduction activities related to brown adipogenic differ- gulated during brown adipogenesis. The ectopic expression of entiation has not been as extensive as that pertaining to white DUSP12 using a retroviral expression system induces the adipogenic differentiation because it was only recently identi- suppression of adipogenic differentiation, whereas a catalytic fied in adult humans (3, 4).
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Anti-DUSP12 (GW22594)
3050 Spruce Street, Saint Louis, MO 63103 USA Tel: (800) 521-8956 (314) 771-5765 Fax: (800) 325-5052 (314) 771-5757 email: [email protected] Product Information Anti-DUSP12 antibody produced in chicken, affinity isolated antibody Catalog Number GW22594 Formerly listed as GenWay Catalog Number 15-288-22594, Dual specificity phosphatase 12 Antibody. – Storage Temperature Store at 20 °C The product is a clear, colorless solution in phosphate buffered saline, pH 7.2, containing 0.02% sodium azide. Synonyms: Dual specificity phosphatase 12 Species Reactivity: Human Product Description The protein encoded by this gene is a member of the dual Tested Applications: WB specificity protein phosphatase subfamily. These phospha- Recommended Dilutions: Recommended starting dilution tases inactivate their target kinases by dephosphorylating for Western blot analysis is 1:500, for tissue or cell staining both the phosphoserine/threonine and phosphotyrosine 1:200. residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ Note: Optimal concentrations and conditions for each ERK, SAPK/JNK, p38), which is associated with cellular application should be determined by the user. proliferation and differentiation. Different members of the Precautions and Disclaimer family of dual specificity phosphatases show distinct This product is for R&D use only, not for drug, household, or substrate specificities for various MAP kinases. different other uses. Due to the sodium azide content a material tissue distribution and subcellular localization. and different safety data sheet (MSDS) for this product has been sent to modes of inducibility of their expression by extracellular the attention of the safety officer of your institution.
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DDIAS Promotes STAT3 Activation by Preventing STAT3 Recruitment To
Im et al. Oncogenesis (2020)9:1 https://doi.org/10.1038/s41389-019-0187-2 Oncogenesis ARTICLE Open Access DDIAS promotes STAT3 activation by preventing STAT3 recruitment to PTPRM in lung cancer cells Joo-Young Im 1,Bo-KyungKim 1,Kang-WooLee2, So-Young Chun1, Mi-Jung Kang1 and Misun Won1,3 Abstract DNA damage-induced apoptosis suppressor (DDIAS) regulates cancer cell survival. Here we investigated the involvement of DDIAS in IL-6–mediated signaling to understand the mechanism underlying the role of DDIAS in lung cancer malignancy. We showed that DDIAS promotes tyrosine phosphorylation of signal transducer and activator of transcription 3 (STAT3), which is constitutively activated in malignant cancers. Interestingly, siRNA protein tyrosine phosphatase (PTP) library screening revealed protein tyrosine phosphatase receptor mu (PTPRM) as a novel STAT3 PTP. PTPRM knockdown rescued the DDIAS-knockdown-mediated decrease in STAT3 Y705 phosphorylation in the presence of IL-6. However, PTPRM overexpression decreased STAT3 Y705 phosphorylation. Moreover, endogenous PTPRM interacted with endogenous STAT3 for dephosphorylation at Y705 following IL-6 treatment. As expected, PTPRM bound to wild-type STAT3 but not the STAT3 Y705F mutant. PTPRM dephosphorylated STAT3 in the absence of DDIAS, suggesting that DDIAS hampers PTPRM/STAT3 interaction. In fact, DDIAS bound to the STAT3 transactivation domain (TAD), which competes with PTPRM to recruit STAT3 for dephosphorylation. Thus we show that DDIAS prevents PTPRM/STAT3 binding and blocks STAT3 Y705 dephosphorylation, thereby sustaining STAT3 activation in lung cancer. DDIAS expression strongly correlates with STAT3 phosphorylation in human lung cancer cell lines and tissues. Thus DDIAS may be considered as a potential biomarker and therapeutic target in malignant lung cancer cells with aberrant STAT3 activation.
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Dual-Specificity Phosphatase 3 Deletion Promotes Obesity, Non
www.nature.com/scientificreports OPEN Dual‑specifcity phosphatase 3 deletion promotes obesity, non‑alcoholic steatohepatitis and hepatocellular carcinoma Sophie Jacques1,10, Arash Arjomand1,10, Hélène Perée1, Patrick Collins2, Alice Mayer3, Arnaud Lavergne3, Marie Wéry1, Myriam Mni1, Alexandre Hego4, Virginie Thuillier1, Guillaume Becker5, Mohamed Ali Bahri5, Alain Plenevaux5, Emmanuel Di Valentin6, Cécile Oury7, Michel Moutschen8, Philippe Delvenne2, Nicolas Paquot9 & Souad Rahmouni1* Non‑alcoholic fatty liver disease (NAFLD) is the most common chronic hepatic pathology in Western countries. It encompasses a spectrum of conditions ranging from simple steatosis to more severe and progressive non‑alcoholic steatohepatitis (NASH) that can lead to hepatocellular carcinoma (HCC). Obesity and related metabolic syndrome are important risk factors for the development of NAFLD, NASH and HCC. DUSP3 is a small dual‑specifcity protein phosphatase with a poorly known physiological function. We investigated its role in metabolic syndrome manifestations and in HCC using a mouse knockout (KO) model. While aging, DUSP3‑KO mice became obese, exhibited insulin resistance, NAFLD and associated liver damage. These phenotypes were exacerbated under high fat diet (HFD). In addition, DEN administration combined to HFD led to rapid HCC development in DUSP3‑KO compared to wild type (WT) mice. DUSP3‑KO mice had more serum triglycerides, cholesterol, AST and ALT compared to control WT mice under both regular chow diet (CD) and HFD. The level of fasting insulin was higher compared to WT mice, though, fasting glucose as well as glucose tolerance were normal. At the molecular level, HFD led to decreased expression of DUSP3 in WT mice. DUSP3 deletion was associated with increased and consistent phosphorylation of the insulin receptor (IR) and with higher activation of the downstream signaling pathway.
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Live-Cell Imaging Rnai Screen Identifies PP2A–B55α and Importin-Β1 As Key Mitotic Exit Regulators in Human Cells
LETTERS Live-cell imaging RNAi screen identifies PP2A–B55α and importin-β1 as key mitotic exit regulators in human cells Michael H. A. Schmitz1,2,3, Michael Held1,2, Veerle Janssens4, James R. A. Hutchins5, Otto Hudecz6, Elitsa Ivanova4, Jozef Goris4, Laura Trinkle-Mulcahy7, Angus I. Lamond8, Ina Poser9, Anthony A. Hyman9, Karl Mechtler5,6, Jan-Michael Peters5 and Daniel W. Gerlich1,2,10 When vertebrate cells exit mitosis various cellular structures can contribute to Cdk1 substrate dephosphorylation during vertebrate are re-organized to build functional interphase cells1. This mitotic exit, whereas Ca2+-triggered mitotic exit in cytostatic-factor- depends on Cdk1 (cyclin dependent kinase 1) inactivation arrested egg extracts depends on calcineurin12,13. Early genetic studies in and subsequent dephosphorylation of its substrates2–4. Drosophila melanogaster 14,15 and Aspergillus nidulans16 reported defects Members of the protein phosphatase 1 and 2A (PP1 and in late mitosis of PP1 and PP2A mutants. However, the assays used in PP2A) families can dephosphorylate Cdk1 substrates in these studies were not specific for mitotic exit because they scored pro- biochemical extracts during mitotic exit5,6, but how this relates metaphase arrest or anaphase chromosome bridges, which can result to postmitotic reassembly of interphase structures in intact from defects in early mitosis. cells is not known. Here, we use a live-cell imaging assay and Intracellular targeting of Ser/Thr phosphatase complexes to specific RNAi knockdown to screen a genome-wide library of protein substrates is mediated by a diverse range of regulatory and targeting phosphatases for mitotic exit functions in human cells. We subunits that associate with a small group of catalytic subunits3,4,17.
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Expression Profile of Tyrosine Phosphatases in HER2 Breast
Cellular Oncology 32 (2010) 361–372 361 DOI 10.3233/CLO-2010-0520 IOS Press Expression profile of tyrosine phosphatases in HER2 breast cancer cells and tumors Maria Antonietta Lucci a, Rosaria Orlandi b, Tiziana Triulzi b, Elda Tagliabue b, Andrea Balsari c and Emma Villa-Moruzzi a,∗ a Department of Experimental Pathology, University of Pisa, Pisa, Italy b Molecular Biology Unit, Department of Experimental Oncology, Istituto Nazionale Tumori, Milan, Italy c Department of Human Morphology and Biomedical Sciences, University of Milan, Milan, Italy Abstract. Background: HER2-overexpression promotes malignancy by modulating signalling molecules, which include PTPs/DSPs (protein tyrosine and dual-specificity phosphatases). Our aim was to identify PTPs/DSPs displaying HER2-associated expression alterations. Methods: HER2 activity was modulated in MDA-MB-453 cells and PTPs/DSPs expression was analysed with a DNA oligoar- ray, by RT-PCR and immunoblotting. Two public breast tumor datasets were analysed to identify PTPs/DSPs differentially ex- pressed in HER2-positive tumors. Results: In cells (1) HER2-inhibition up-regulated 4 PTPs (PTPRA, PTPRK, PTPN11, PTPN18) and 11 DSPs (7 MKPs [MAP Kinase Phosphatases], 2 PTP4, 2 MTMRs [Myotubularin related phosphatases]) and down-regulated 7 DSPs (2 MKPs, 2 MTMRs, CDKN3, PTEN, CDC25C); (2) HER2-activation with EGF affected 10 DSPs (5 MKPs, 2 MTMRs, PTP4A1, CDKN3, CDC25B) and PTPN13; 8 DSPs were found in both groups. Furthermore, 7 PTPs/DSPs displayed also altered protein level. Analysis of 2 breast cancer datasets identified 6 differentially expressed DSPs: DUSP6, strongly up-regulated in both datasets; DUSP10 and CDC25B, up-regulated; PTP4A2, CDC14A and MTMR11 down-regulated in one dataset.
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