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      TRPM Family Channels in Cancer

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          Abstract

          Members of the TRPM (“Melastatin”) family fall into the subclass of the TRP channels having varying permeability to Ca 2+ and Mg 2+, with three members of the TRPM family being chanzymes, which contain C-terminal enzyme domains. The role of different TRPM members has been shown in various cancers such as prostate cancer for mostly TRPM8 and TRPM2, breast cancer for mostly TRPM2 and TRPM7, and pancreatic cancer for TRPM2/7/8 channels. The role of TRPM5 channels has been shown in lung cancer, TRPM1 in melanoma, and TRPM4 channel in prostate cancer as well. Thus, the TRPM family of channels may represent an appealing target for the anticancer therapy.

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          TRP channels as cellular sensors.

          David Clapham (2003)
          TRP channels are the vanguard of our sensory systems, responding to temperature, touch, pain, osmolarity, pheromones, taste and other stimuli. But their role is much broader than classical sensory transduction. They are an ancient sensory apparatus for the cell, not just the multicellular organism, and they have been adapted to respond to all manner of stimuli, from both within and outside the cell.
          Article 0 comments Cited 587 times – based on 0 reviews     Review now
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            ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology.

            A L Perraud, A Fleig, C Dunn … (2001)
            Free ADP-ribose (ADPR), a product of NAD hydrolysis and a breakdown product of the calcium-release second messenger cyclic ADPR (cADPR), has no defined role as an intracellular signalling molecule in vertebrate systems. Here we show that a 350-amino-acid protein (designated NUDT9) and a homologous domain (NUDT9 homology domain) near the carboxy terminus of the LTRPC2/TrpC7 putative cation channel both function as specific ADPR pyrophosphatases. Whole-cell and single-channel analysis of HEK-293 cells expressing LTRPC2 show that LTRPC2 functions as a calcium-permeable cation channel that is specifically gated by free ADPR. The expression of native LTRPC2 transcripts is detectable in many tissues including the U937 monocyte cell line, in which ADPR induces large cation currents (designated IADPR) that closely match those mediated by recombinant LTRPC2. These results indicate that intracellular ADPR regulates calcium entry into cells that express LTRPC2.
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              TRP-PLIK, a bifunctional protein with kinase and ion channel activities.

              L W Runnels, L Yue, D. Clapham (2001)
              We cloned and characterized a protein kinase and ion channel, TRP-PLIK. As part of the long transient receptor potential channel subfamily implicated in control of cell division, it is a protein that is both an ion channel and a protein kinase. TRP-PLIK phosphorylated itself, displayed a wide tissue distribution, and, when expressed in CHO-K1 cells, constituted a nonselective, calcium-permeant, 105-picosiemen, steeply outwardly rectifying conductance. The zinc finger containing alpha-kinase domain was functional. Inactivation of the kinase activity by site-directed mutagenesis and the channel's dependence on intracellular adenosine triphosphate (ATP) demonstrated that the channel's kinase activity is essential for channel function.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Pharmaceuticals (Basel)
                Journal ID (iso-abbrev): Pharmaceuticals (Basel)
                Journal ID (publisher-id): pharmaceuticals
                Title: Pharmaceuticals
                Publisher: MDPI
                ISSN (Electronic): 1424-8247
                Publication date (Electronic): 07 June 2018
                Publication date Collection: June 2018
                Volume: 11
                Issue: 2
                Electronic Location Identifier: 58
                Affiliations
                [1 ]Laboratory of Cell Physiology, INSERM U1003, Laboratory of Excellence Ion Channels Science and Therapeutics, Department of Biology, Faculty of Science and Technologies, University of Lille, 59650 Villeneuve d’Ascq, France; ghesquier.aline@ 123456gmail.com (A.H.-G.); aurelien.haustrate@ 123456inserm.fr (A.H.)
                [2 ]FONDATION ARC, 9 rue Guy Môquet 94830 Villejuif, France
                Author notes
                Author information
                https://orcid.org/0000-0003-0806-8766
                Article
                Publisher ID: pharmaceuticals-11-00058
                DOI: 10.3390/ph11020058
                PMC ID: 6027338
                PubMed ID: 29875336
                SO-VID: d0d547bc-4e91-47ce-9bdf-4599afc92363
                Copyright © © 2018 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 25 April 2018
                Date accepted : 01 June 2018
                Categories
                Subject: Review

                Keywords: trpm channels,cancer,target,therapy
                Data availability:
                Keywords: trpm channels, cancer, target, therapy

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