Special Issue "Transient Receptor Potential (TRP) Channels"


A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (28 February 2014)

Special Issue Editor

Guest Editor
Dr. Loren W. Runnels
Department of Pharmacology, Rutgers Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA
Website: http://molbiosci.rutgers.edu/faculty/runnels.html
E-Mail: runnellw@rwjms.rutgers.edu
Interests: TRPM6 and TRPM7 ion channels; cell migration; development

Special Issue Information

Dear Colleagues,

Since the original cloning of the transient receptor potential (TRP) ion channel by Montell and Rubin in Drosophila melanogaster in 1989, the TRP ion channel family has grown to encompass seven subfamilies linked together primarily by their sequence homology: TRPC (“canonical”), TRPM (“melastatin”), TRPV (“vanilloid”), TRPA (“ankyrin”), TRPML (“mucolipin”), TRPP (or PKD for “polycystin”), and TRPN (“NOMPC-like”), which is only found in invertebrates and fish. TRP ion channels are widely expressed in many tissues and cell types, and have been shown to affect a broad range of cellular processes, including cell division, cell migration, and stress responses. These ion channels are also involved in the ability of cells to sense and respond to external stimuli, such as temperature, pH, and osmolarity. When activated, most TRP channels conduct cations to depolarize cells, so as to initiate a plethora of cellular responses. However, recent research has revealed important new functions for TRP ion channels in intracellular compartments. This Special Issue will provide an opportunity to publish open access research work and review articles related to the TRP channel family, and will offer comprehensive new insights into current developments within this exciting and important research field.

Dr. Loren W. Runnels
Guest Editor


Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

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  • TRP
  • ion channel
  • calcium
  • magnesium
  • zinc
  • cellular regulation
  • signal transduction
  • development

Published Papers (4 papers)

Cells 2014, 3(2), 288-303; doi:10.3390/cells3020288
Received: 28 February 2014; in revised form: 29 March 2014 / Accepted: 2 April 2014 / Published: 9 April 2014
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Cells 2014, 3(2), 258-287; doi:10.3390/cells3020258
Received: 28 February 2014; in revised form: 25 March 2014 / Accepted: 27 March 2014 / Published: 8 April 2014
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Cells 2014, 3(2), 247-257; doi:10.3390/cells3020247
Received: 18 February 2014; in revised form: 17 March 2014 / Accepted: 25 March 2014 / Published: 4 April 2014
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abstract graphic

Cells 2014, 3(1), 112-128; doi:10.3390/cells3010112
Received: 19 December 2013; in revised form: 22 January 2014 / Accepted: 8 February 2014 / Published: 19 February 2014
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Planned Papers

The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.

Type of Paper: Review
Title: Classical transient receptor potential 1 (TRPC1): Channel or Channel regulator?
Authors: Alexander Dietrich and Thomas Gudermann
Affiliations: Walther-Straub-Institute of Pharmacology and Toxicology, LM-University Munich, Nussbaumstr. 26, D-80336 Munich, Germany; E-Mail: alexander.dietrich@lrz.uni-muenchen.de
Abstract: In contrast to other TRPC channels the function of TRPC1 as an ion channel is a matter of debate, because it is difficult to obtain substantial functional signals over background in response to over-expression of TRPC1 alone. Along these lines, heterologously expressed TRPC1 is poorly translocated as a homotetramer to the plasma membrane and may not act physiologically on its own, but is rather an important linker and regulator protein in other functional heteromeric TRPC channel tetramers. However, due to the lack of highly specific TRPC1 antibodies which detect native TRPC1 channels in primary cells identification of functional TRPC1-containing heteromeric TRPC channel complexes in the plasma membrane is still challenging. This review will give an overview on the current status of research on TRPC1 function in cells using pharmacological and genetic tools like TRPC1 deficient mouse models. Type of Paper: Review

Title: Cellular and Developmental Biology of TRPM7 Channel-Kinase: Implications in Cancer
Authors: Nelson S. Yee 1,2,* Abid A. Kazi 1 and Rosemary K. Yee 3,4
Affiliations: 1. Division of Hematology-Oncology, Department of Medicine, Milton S. Hershey Medical Center and Pennsylvania State University College of Medicine, Hershey, PA, USA
2. Experimental Therapeutics Program, Penn State Hershey Cancer Institute, Hershey, PA, USA
3. Schreyer Honors College, Pennsylvania State University, University Park, PA, USA
4. Penn State Harrisburg School of Humanities, Pennsylvania State University, Middletown, PA, USA E-Mail: nyee@hmc.psu.edu
Abstract: The transient receptor potential TRPM7 channel-kinase plays essential roles in basic cellular processes, normal physiology, and organogenesis. Aberrant expression and/or  activity of the TRPM7 channel-kinase has been implicated in a variety of human diseases  including cancer. Studying the functional roles of TRPM7 and the underlying mechanisms in  normal cells and developmental processes is expected to help elucidate how TRPM7 channel- kinase contributes to pathogenesis such as neoplasia. In this article, we will provide an  updated review of the biological functions of TRPM7 and the associated signaling events,  and discuss potential mechanisms that mediate its roles in malignant diseases.

Type of the Paper: Review
Title: Natural and synthetic modulators of TRPM7
Authors: Sebastian Schäfer, Vladimir Chubanov, and Thomas Gudermann *
Affiliations: Walther-Straub-Institute of Pharmacology and Toxicology, University of Munich, Goethestrasse 33, 80336 Munich, Germany; E-Mail: thomas.gudermann@lrz.uni-muenchen.de
Abstract: Transient receptor potential cation channel subfamily M member 7 (TRPM7) is a bi-functional protein comprising a TRP ion channel segment linked to an α-type protein kinase domain. TRPM7 is essential for proliferation and cell growth. TRPM7 was found to be associated with anoxic neuronal death, cardiac fibrosis and tumor cell proliferation and other pathophysiological processes. Despite the physiological and clinical importance of TRPM7, only a few exogenous modulators of TRPM7 channel are currently available. Recently, independent laboratories identified several small organic compounds enabling to modulate TRPM7 channel activity. Here, we provide a concise overview of this emerging field.

Type of the Paper: Review
Title: Post-Translational Modifications of TRP Channels
Authors: Olaf Voolstra * and Armin Huber
Affiliations: Department of Biosensorics, Institute of Physiology, Universität Hohenheim, D-70599 Stuttgart, Germany; E-Mail: voolstra@uni-hohenheim.de
Abstract: Transient receptor potential (TRP) channels constitute an ancient family of cation channels that have been found in many eucaryotic organisms from yeast to human. TRP channels exert a multitude of physiological functions ranging from Ca2+ homeostasis in the kidney to pain reception and vision. These channels are activated by a wide range of stimuli and undergo covalent post-translational modifications that affect and modulate their subcellular targeting, their biophysical properties, or channel gating. These modifications include N-linked glycosylation, protein phosphorylation, and covalent attachment of chemicals that reversibly bind to specific cysteine residues. The latter modification represents an unusual activation mechanism of ligand-gated ion channels that is in contrast to the lock-and-key paradigm of receptor activation by its agonists. In this review we summarize the post-translational modifications identified on TRP channels and, when available, explain their physiological role.

Type of Paper: Article
Title: Unique responses are observed in Transient Receptor Potential Ankyrin 1 and Vanilloid 1 (TRPA1 and TRPV1) co-expressing cells
Authors: Laura Sadofsky 1, Koti Sreekrishna 2,* , Yakang Lin 2, Renee Schinaman 2, Kate Gorka 2, Chris Haught 2, Thomas Huggins 2, Robert Isfort 2, Charlie Bascom 2 and Alyn Morice 1
1 Cardiovascular and Respiratory Studies, The University of Hull, UK; E-Mails: Sadofsky@hull.ac.uk (L.R.); Morice@hull.uk (A.H.)
2 The Procter & Gamble Company, Cincinnati, Ohio, USA; E-Mails: lin.y.2@Pg.com (Y.L.); schinaman.cr@pg.com (R.S.); gorka.k@pg.com (K.G.); haught.c@pg.com (C.H.); huggins.tg@pg.com (T.H.); Isfort.rj@pg.com (R.I.); bascom.cc@pg.com (C.B.) Author to whom correspondence should be addressed: Sreekrishna.k@pg.com;
Tel.: +1-513-622-1431; Fax: +1-513-622-0887.
Abstract: Transient receptor potential (TRP) ankyrin 1 (A1) and vanilloid 1 (V1) receptors are thought to be involved in modulating cough. In vivo, A1 is expressed in the same sensory neurons as V1, and these two channels can directly interact and form hetero-tetramers. In order to understand the effects of dimerization on receptor function, we created a cell line that permanently coexpresses TRPA1 and TRPV1 receptors (A1V1). Among 600 compounds screened against these receptors at 1 mM, 40 activated A1, V1 and A1V1; 92 activated A1 and A1V1 but not V1; 12 activated V1 and A1V1 but not A1; and one each activated only A1, V1 or A1V1. Of the 40 compounds that activated all three receptors, 20 compounds showed relative receptor activity of A1=A1V1>V1; 4 A1>A1V1>V1, 3 V1>A1V1>A1, 3 A1=A1V1=V1, and 10 A1V1=A1+V1. Of the 92 compounds that activated A1 and A1V1 but not V1, 72 compounds showed relative receptor activity of A1=A1V1, 14 A1V1>A1, and 6 A1>A1V1. Of the 12 compounds that activated V1 and A1V1 but not A1, 5 compounds showed relative receptor activity of V1=A1V1, 4 A1V1>V1 and 3 A1V1<V1. These results suggest that interaction between A1 and V1 impact activation by some but not all compounds.

Last update: 14 January 2014

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