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      Disruption of serine/threonine protein phosphatase 5 inhibits tumorigenesis of urinary bladder cancer cells

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          Abstract

          Serine/threonine protein phosphatase 5 (PPP5C) is a member of the protein serine/threonine phosphatase family and has been shown to participate in multiple signaling cascades and tumor progression. We found that PPP5C was highly expressed in bladder cancer tissues compared to normal urothelial tissues, and positively correlated to tumor stages through ONCOMINE microarray data mining. Knockdown of PPP5C via a lentivirus-mediated short hairpin RNA (shRNA) markedly inhibited cell proliferation and colony formation. Flow cytometric analysis showed that PPP5C-deficient T24 and BT5637 bladder cancer cells were arrested in G0/G1 phase and induced apoptosis. In addition, tumor growth was inhibited in vivo in a xenograft nude mouse model. Further studies indicated that knockdown of PPP5C downregulated c-myc and CDK4, whereas upregulated p27, BAD and Beclin1. These results suggest that PPP5C is associated with bladder cancer (BCa) and plays an oncogenic role in the development and progression of bladder cancer.

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          Silencing of HIV-1 with RNA interference: a multiple shRNA approach.

          Olivier ter Brake, Pavlina Konstantinova, Mustafa Ceylan … (2006)
          Double-stranded RNA can induce gene silencing via a process known as RNA interference (RNAi). Previously, we have shown that stable expression of a single shRNA targeting the HIV-1 Nef gene strongly inhibits HIV-1 replication. However, this was not sufficient to maintain inhibition. One of the hallmarks of RNAi, its sequence specificity, presented a way out for the virus, as single nucleotide substitutions in the target region abolished inhibition. For the development of a durable gene therapy that prevents viral escape, we proposed to combine multiple shRNAs against conserved HIV-1 regions. Therefore, we screened 86 different shRNAs targeting highly conserved regions. We identified multiple shRNAs that act as potent inhibitors of virus replication. We show, for the first time, that expression of three different shRNAs from a single lentiviral vector results in similar levels of inhibition per shRNA compared to single shRNA vectors. Thus, their combined expression results in a much stronger inhibition of virus production. Moreover, when we infected cells transduced with a double shRNA viral vector, virus escape was delayed. These results confirm that RNAi has great potential as an antiviral gene therapy approach and support our efforts to develop this strategy for treatment of HIV-1-infected individuals.
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            Diverse physiological functions for dual-specificity MAP kinase phosphatases.

            Stephen M. Keyse, Eleanor Dickinson (2006)
            A structurally distinct subfamily of ten dual-specificity (Thr/Tyr) protein phosphatases is responsible for the regulated dephosphorylation and inactivation of mitogen-activated protein kinase (MAPK) family members in mammals. These MAPK phosphatases (MKPs) interact specifically with their substrates through a modular kinase-interaction motif (KIM) located within the N-terminal non-catalytic domain of the protein. In addition, MAPK binding is often accompanied by enzymatic activation of the C-terminal catalytic domain, thus ensuring specificity of action. Despite our knowledge of the biochemical and structural basis for the catalytic mechanism of the MKPs, we know much less about their regulation and physiological functions in mammalian cells and tissues. However, recent studies employing a range of model systems have begun to reveal essential non-redundant roles for the MKPs in determining the outcome of MAPK signalling in a variety of physiological contexts. These include development, immune system function, metabolic homeostasis and the regulation of cellular stress responses. Interestingly, these functions may reflect both restricted subcellular MKP activity and changes in the levels of signalling through multiple MAPK pathways.
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              The role of protein phosphorylation in human health and disease. The Sir Hans Krebs Medal Lecture.

              P. Cohen (2001)
              The reversible phosphorylation of proteins regulates almost all aspects of cell life, while abnormal phosphorylation is a cause or consequence of many diseases. Mutations in particular protein kinases and phosphatases gives rise to a number of disorders and many naturally occurring toxins and pathogens exert their effects by altering the phosphorylation states of intracellular proteins. In this lecture, I present an overview of the progress that is being made in developing specific inhibitors of protein kinases for the treatment of cancer and chronic inflammatory diseases and describe how recent advances in our understanding of the specificity and regulation of one particular protein kinase (GSK3) may facilitate the development of drugs to treat diabetes that would not have the potential to be oncogenic. I also discuss the exploitation of specific protein kinase inhibitors for the study of cell signalling and make recommendations for their effective use in cell-based assays.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Oncol
                Journal ID (iso-abbrev): Int. J. Oncol
                Journal ID (publisher-id): IJO
                Title: International Journal of Oncology
                Publisher: D.A. Spandidos
                ISSN (Print): 1019-6439
                ISSN (Electronic): 1791-2423
                Publication date Collection: July 2017
                Publication date (Electronic): 16 May 2017
                Publication date PMC-release: 16 May 2017
                Volume: 51
                Issue: 1
                Pages: 39-48
                Affiliations
                [1 ]Department of Urinary Surgery, Changzheng Hospital, Second Military Medical University, Shanghai 200003
                [2 ]Department of Urinary Surgery, Third Affiliated Hospital, Second Military Medical University, Shanghai 201805
                [3 ]Department of Urinary Surgery, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai 200025, P.R. China
                Author notes
                Correspondence to: Dr Dan-Feng Xu, Department of Urinary Surgery, Ruijin Hospital, Shanghai Jiaotong University School of Medicine, Shanghai 200025, P.R. China, E-mail: danfengxu_urology@ 123456163.com
                Dr Yi Gao, Department of Urinary Surgery, Changzheng Hospital, Second Military Medical University, Shanghai 200003, P.R. China, E-mail: gaoyismmu@ 123456163.com
                [*]

                Contributed equally

                Article
                Publisher ID: ijo-51-01-0039
                DOI: 10.3892/ijo.2017.3997
                PMC ID: 5467789
                PubMed ID: 28534961
                SO-VID: fcb9b1a3-601d-45d1-b3b5-c2307b268aef
                Copyright © Copyright: © Chen et al.
                License:

                This is an open access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.

                History
                Date received : 20 January 2017
                Date accepted : 20 March 2017
                Categories
                Subject: Articles

                Keywords: ppp5c,bladder cancer,tumorigenesis,shrna
                Data availability:
                Keywords: ppp5c, bladder cancer, tumorigenesis, shrna

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