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      TRPV2 Mediates Adrenomedullin Stimulation of Prostate and Urothelial Cancer Cell Adhesion, Migration and Invasion

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          Abstract

          Adrenomedullin (AM) is a 52-amino acid peptide initially isolated from human pheochromocytoma. AM is expressed in a variety of malignant tissues and cancer cell lines and was shown to be a mitogenic factor capable of stimulating growth of several cancer cell types. In addition, AM is a survival factor for certain cancer cells. Some data suggest that AM might be involved in the progression cancer metastasis via angiogenesis and cell migration and invasion control. The Transient Receptor Potential channel TRPV2 is known to promote in prostate cancer cell migration and invasive phenotype and is correlated with the stage and grade of bladder cancer. In this work we show that AM induces prostate and urothelial cancer cell migration and invasion through TRPV2 translocation to plasma membrane and the subsequent increase in resting calcium level.

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          The TRP ion channel family.

          D. Clapham, L W Runnels, C Strübing (2001)
          Mammalian homologues of the Drosophila transient receptor potential (TRP) channel gene encode a family of at least 20 ion channel proteins. They are widely distributed in mammalian tissues, but their specific physiological functions are largely unknown. A common theme that links the TRP channels is their activation or modulation by phosphatidylinositol signal transduction pathways. The channel subunits have six transmembrane domains that most probably assemble into tetramers to form non-selective cationic channels, which allow for the influx of calcium ions into cells. Three subgroups comprise the TRP channel family; the best understood of these mediates responses to painful stimuli. Other proposed functions include repletion of intracellular calcium stores, receptor-mediated excitation and modulation of the cell cycle.
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            Adrenomedullin, a multifunctional regulatory peptide.

            Ashley R. P. Hinson, S Kapas, Simon Smith (2000)
            Since the discovery of adrenomedullin in 1993 several hundred papers have been published regarding the regulation of its secretion and the multiplicity of its actions. It has been shown to be an almost ubiquitous peptide, with the number of tissues and cell types synthesizing adrenomedullin far exceeding those that do not. In Section II of this paper we give a comprehensive review both of tissues and cell lines secreting adrenomedullin and of the mechanisms regulating gene expression. The data on circulating adrenomedullin, obtained with the various assays available, are also reviewed, and the disease states in which plasma adrenomedullin is elevated are listed. In Section III the pharmacology and biochemistry of adrenomedullin binding sites, both specific sites and calcitonin gene-related peptide (CGRP) receptors, are discussed. In particular, the putative adrenomedullin receptor clones and signal transduction pathways are described. In Section IV the various actions of adrenomedullin are discussed: its actions on cellular growth, the cardiovascular system, the central nervous system, and the endocrine system are all considered. Finally, in Section V, we consider some unresolved issues and propose future areas for research.
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              Role of cationic channel TRPV2 in promoting prostate cancer migration and progression to androgen resistance.

              François Rassendren, Dimitra Gkika, Sandrine Humez … (2010)
              Castration resistance in prostate cancer (PCa) constitutes an advanced, aggressive disease with poor prognosis, associated with uncontrolled cell proliferation, resistance to apoptosis, and enhanced invasive potential. The molecular mechanisms involved in the transition of PCa to castration resistance are obscure. Here, we report that the nonselective cationic channel transient receptor potential vanilloid 2 (TRPV2) is a distinctive feature of castration-resistant PCa. TRPV2 transcript levels were higher in patients with metastatic cancer (stage M1) compared with primary solid tumors (stages T2a and T2b). Previous studies of the TRPV2 channel indicated that it is primarily involved in cancer cell migration and not in cell growth. Introducing TRPV2 into androgen-dependent LNCaP cells enhanced cell migration along with expression of invasion markers matrix metalloproteinase (MMP) 9 and cathepsin B. Consistent with the likelihood that TRPV2 may affect cancer cell aggressiveness by influencing basal intracellular calcium levels, small interfering RNA-mediated silencing of TRPV2 reduced the growth and invasive properties of PC3 prostate tumors established in nude mice xenografts, and diminished expression of invasive enzymes MMP2, MMP9, and cathepsin B. Our findings establish a role for TRPV2 in PCa progression to the aggressive castration-resistant stage, prompting evaluation of TRPV2 as a potential prognostic marker and therapeutic target in the setting of advanced PCa.
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                Author and article information

                Contributors
                Natasha Kyprianou: Role: Editor
                Journal
                Journal ID (nlm-ta): PLoS One
                Journal ID (iso-abbrev): PLoS ONE
                Journal ID (publisher-id): plos
                Journal ID (pmc): plosone
                Title: PLoS ONE
                Publisher: Public Library of Science (San Francisco, USA )
                ISSN (Electronic): 1932-6203
                Publication date Collection: 2013
                Publication date (Electronic): 31 May 2013
                Volume: 8
                Issue: 5
                Electronic Location Identifier: e64885
                Affiliations
                [1 ]INSERM U1003, Equipe Labellisée par la Ligue Nationale contre le Cancer, Villeneuve d’Ascq, France
                [2 ]Laboratory of Excellence, Ion Channels Science and Therapeutics, Universite des Sciences et Technologies de Lille (USTL), Villeneuve d’Ascq, France
                [3 ]Inserm UMR 911-CRO2, Faculté de Médecine Timone, Marseille, France
                University of Kentucky College of Medicine, United States of America
                Author notes

                Competing Interests: The authors have declared that no competing interests exist.

                Conceived and designed the experiments: AO DG BM NP. Performed the experiments: AO AB DG FV. Analyzed the data: AO AB DG FV. Contributed reagents/materials/analysis tools: VL LO BM. Wrote the paper: AO DG NP.

                Article
                Publisher ID: PONE-D-13-03539
                DOI: 10.1371/journal.pone.0064885
                PMC ID: 3669125
                PubMed ID: 23741410
                SO-VID: 8b44359c-834f-4d06-bd3f-e9cb786527d3
                Copyright statement: Copyright @ 2013
                License:

                This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

                History
                Date received : 21 January 2013
                Date accepted : 19 April 2013
                Page count
                Pages: 7
                Funding
                This work was supported by grants from the Institut National de la Sante et de la Recherche Medicale (INSERM), Ligue Nationale Contre le Cancer, Region Nord Pas de Calais and Université Catholique de Lille. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
                Categories
                Subject: Research Article
                Subject: Biology
                Subject: Anatomy and Physiology
                Subject: Cell Physiology
                Subject: Biochemistry
                Subject: Proteins
                Subject: Ion Channels
                Subject: Molecular Cell Biology
                Subject: Cell Adhesion
                Subject: Integrins
                Subject: Membranes and Sorting
                Subject: Medicine
                Subject: Oncology
                Subject: Cancers and Neoplasms
                Subject: Genitourinary Tract Tumors
                Subject: Bladder Cancer
                Subject: Prostate Cancer
                Subject: Basic Cancer Research

                ScienceOpen disciplines: Uncategorized
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                ScienceOpen disciplines: Uncategorized

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