(TRPV2, TRPV3, TRPV4, TRPV5, and TRPV6) Gene and Protein Expression in Patients with Ulcerative Colitis
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Snapshot: Mammalian TRP Channels David E
SnapShot: Mammalian TRP Channels David E. Clapham HHMI, Children’s Hospital, Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA TRP Activators Inhibitors Putative Interacting Proteins Proposed Functions Activation potentiated by PLC pathways Gd, La TRPC4, TRPC5, calmodulin, TRPC3, Homodimer is a purported stretch-sensitive ion channel; form C1 TRPP1, IP3Rs, caveolin-1, PMCA heteromeric ion channels with TRPC4 or TRPC5 in neurons -/- Pheromone receptor mechanism? Calmodulin, IP3R3, Enkurin, TRPC6 TRPC2 mice respond abnormally to urine-based olfactory C2 cues; pheromone sensing 2+ Diacylglycerol, [Ca ]I, activation potentiated BTP2, flufenamate, Gd, La TRPC1, calmodulin, PLCβ, PLCγ, IP3R, Potential role in vasoregulation and airway regulation C3 by PLC pathways RyR, SERCA, caveolin-1, αSNAP, NCX1 La (100 µM), calmidazolium, activation [Ca2+] , 2-APB, niflumic acid, TRPC1, TRPC5, calmodulin, PLCβ, TRPC4-/- mice have abnormalities in endothelial-based vessel C4 i potentiated by PLC pathways DIDS, La (mM) NHERF1, IP3R permeability La (100 µM), activation potentiated by PLC 2-APB, flufenamate, La (mM) TRPC1, TRPC4, calmodulin, PLCβ, No phenotype yet reported in TRPC5-/- mice; potentially C5 pathways, nitric oxide NHERF1/2, ZO-1, IP3R regulates growth cones and neurite extension 2+ Diacylglycerol, [Ca ]I, 20-HETE, activation 2-APB, amiloride, Cd, La, Gd Calmodulin, TRPC3, TRPC7, FKBP12 Missense mutation in human focal segmental glomerulo- C6 potentiated by PLC pathways sclerosis (FSGS); abnormal vasoregulation in TRPC6-/- -
TRPV4: a Physio and Pathophysiologically Significant Ion Channel
International Journal of Molecular Sciences Review TRPV4: A Physio and Pathophysiologically Significant Ion Channel Tamara Rosenbaum 1,* , Miguel Benítez-Angeles 1, Raúl Sánchez-Hernández 1, Sara Luz Morales-Lázaro 1, Marcia Hiriart 1 , Luis Eduardo Morales-Buenrostro 2 and Francisco Torres-Quiroz 3 1 Departamento de Neurociencia Cognitiva, División Neurociencias, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico; [email protected] (M.B.-A.); [email protected] (R.S.-H.); [email protected] (S.L.M.-L.); [email protected] (M.H.) 2 Departamento de Nefrología y Metabolismo Mineral, Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Mexico City 14080, Mexico; [email protected] 3 Departamento de Bioquímica y Biología Estructural, División Investigación Básica, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico; [email protected] * Correspondence: [email protected]; Tel.: +52-555-622-56-24; Fax: +52-555-622-56-07 Received: 3 May 2020; Accepted: 24 May 2020; Published: 28 May 2020 Abstract: Transient Receptor Potential (TRP) channels are a family of ion channels whose members are distributed among all kinds of animals, from invertebrates to vertebrates. The importance of these molecules is exemplified by the variety of physiological roles they play. Perhaps, the most extensively studied member of this family is the TRPV1 ion channel; nonetheless, the activity of TRPV4 has been associated to several physio and pathophysiological processes, and its dysfunction can lead to severe consequences. Several lines of evidence derived from animal models and even clinical trials in humans highlight TRPV4 as a therapeutic target and as a protein that will receive even more attention in the near future, as will be reviewed here. -
Heteromeric TRP Channels in Lung Inflammation
cells Review Heteromeric TRP Channels in Lung Inflammation Meryam Zergane 1, Wolfgang M. Kuebler 1,2,3,4,5,* and Laura Michalick 1,2 1 Institute of Physiology, Charité—Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin, Humboldt-Universität zu Berlin, and Berlin Institute of Health, 10117 Berlin, Germany; [email protected] (M.Z.); [email protected] (L.M.) 2 German Centre for Cardiovascular Research (DZHK), 10785 Berlin, Germany 3 German Center for Lung Research (DZL), 35392 Gießen, Germany 4 The Keenan Research Centre for Biomedical Science, St. Michael’s Hospital, Toronto, ON M5B 1W8, Canada 5 Department of Surgery and Physiology, University of Toronto, Toronto, ON M5S 1A8, Canada * Correspondence: [email protected] Abstract: Activation of Transient Receptor Potential (TRP) channels can disrupt endothelial bar- rier function, as their mediated Ca2+ influx activates the CaM (calmodulin)/MLCK (myosin light chain kinase)-signaling pathway, and thereby rearranges the cytoskeleton, increases endothelial permeability and thus can facilitate activation of inflammatory cells and formation of pulmonary edema. Interestingly, TRP channel subunits can build heterotetramers, whereas heteromeric TRPC1/4, TRPC3/6 and TRPV1/4 are expressed in the lung endothelium and could be targeted as a protec- tive strategy to reduce endothelial permeability in pulmonary inflammation. An update on TRP heteromers and their role in lung inflammation will be provided with this review. Keywords: heteromeric TRP assemblies; pulmonary inflammation; endothelial permeability; TRPC3/6; TRPV1/4; TRPC1/4 Citation: Zergane, M.; Kuebler, W.M.; Michalick, L. Heteromeric TRP Channels in Lung Inflammation. Cells 1. Introduction 2021, 10, 1654. https://doi.org Pulmonary microvascular endothelial cells are a key constituent of the blood air bar- /10.3390/cells10071654 rier that has to be extremely thin (<1 µm) to allow for rapid and efficient alveolo-capillary gas exchange. -
Macromolecular Assembly of Polycystin-2 Intracytosolic C-Terminal Domain
Macromolecular assembly of polycystin-2 intracytosolic C-terminal domain Frederico M. Ferreiraa,b,1, Leandro C. Oliveirac, Gregory G. Germinod, José N. Onuchicc,1, and Luiz F. Onuchica,1 aDivision of Nephrology, University of São Paulo School of Medicine, 01246-903, São Paulo, Brazil; bLaboratory of Immunology, Heart Institute, University of São Paulo School of Medicine, 05403-900, São Paulo, Brazil; cCenter for Theoretical Biological Physics, University of California at San Diego, La Jolla, CA 92093; dNational Institute of Diabetes, Digestive, and Kidney Diseases, Bethesda, MD 20892-2560 Contributed by José N. Onuchic, April 28, 2011 (sent for review March 20, 2011) Mutations in PKD2 are responsible for approximately 15% of the In spite of the aforementioned information and insights, the autosomal dominant polycystic kidney disease cases. This gene macromolecular assembly of PC2t homooligomer continued to encodes polycystin-2, a calcium-permeable cation channel whose be an open question. In the current work, we present the most C-terminal intracytosolic tail (PC2t) plays an important role in its comprehensive set of analyses yet performed and that show interaction with a number of different proteins. In the present PC2t forms a homotetrameric oligomer. We have proposed a study, we have comprehensively evaluated the macromolecular PC2 C-terminal domain delimitation and submitted it to a range assembly of PC2t homooligomer using a series of biophysical of biochemical and biophysical evaluations, including chemical and biochemical analyses. Our studies, based on a new delimitation cross-linking, dynamic light scattering (DLS), circular dichroism of PC2t, have revealed that it is capable of assembling as a homo- (CD) and small angle X-ray scattering (SAXS) analyses. -
Microarray Analysis Reveals the Inhibition of Intestinal Expression Of
www.nature.com/scientificreports OPEN Microarray analysis reveals the inhibition of intestinal expression of nutrient transporters in piglets infected with porcine epidemic diarrhea virus Junmei Zhang1,3, Di Zhao1,3, Dan Yi1,3, Mengjun Wu1, Hongbo Chen1, Tao Wu1, Jia Zhou1, Peng Li1, Yongqing Hou1* & Guoyao Wu2 Porcine epidemic diarrhea virus (PEDV) infection can induce intestinal dysfunction, resulting in severe diarrhea and even death, but the mode of action underlying these viral efects remains unclear. This study determined the efects of PEDV infection on intestinal absorption and the expression of genes for nutrient transporters via biochemical tests and microarray analysis. Sixteen 7-day-old healthy piglets fed a milk replacer were randomly allocated to one of two groups. After 5-day adaption, piglets (n = 8/ group) were orally administrated with either sterile saline or PEDV (the strain from Yunnan province) 4.5 at 10 TCID50 (50% tissue culture infectious dose) per pig. All pigs were orally infused D-xylose (0.1 g/ kg BW) on day 5 post PEDV or saline administration. One hour later, jugular vein blood samples as well as intestinal samples were collected for further analysis. In comparison with the control group, PEDV infection increased diarrhea incidence, blood diamine oxidase activity, and iFABP level, while reducing growth and plasma D-xylose concentration in piglets. Moreover, PEDV infection altered plasma and jejunal amino acid profles, and decreased the expression of aquaporins and amino acid transporters (L-type amino acid -
Transient Receptor Potential Cation Channel Subfamily V and Breast Cancer
Laboratory Investigation (2020) 100:199–206 https://doi.org/10.1038/s41374-019-0348-0 REVIEW ARTICLE Transient receptor potential cation channel subfamily V and breast cancer 1 2 1,3,4 Choon Leng So ● Michael J. G. Milevskiy ● Gregory R. Monteith Received: 27 September 2019 / Revised: 13 November 2019 / Accepted: 14 November 2019 / Published online: 10 December 2019 © The Author(s), under exclusive licence to United States and Canadian Academy of Pathology 2019 Abstract Transient receptor potential cation channel subfamily V (TRPV) channels play important roles in a variety of cellular processes. One example includes the sensory role of TRPV1 that is sensitive to elevated temperatures and acidic environments and is activated by the hot pepper component capsaicin. Another example is the importance of the highly Ca2+ selective channels TRPV5 and TRPV6 in Ca2+ absorption/reabsorption in the intestine and kidney. However, in some cases such as TRPV4 and TRPV6, breast cancer cells appear to overexpress TRPV channels. Moreover, TRPV mediated Ca2+ influx may contribute to enhanced breast cancer cell proliferation and other processes important in tumor progression such as angiogenesis. It appears that the overexpression of some TRPV channels in breast cancer and/or their involvement in breast 1234567890();,: 1234567890();,: cancer cell processes, processes important in the tumor microenvironment or pain may make some TRPV channels potential targets for breast cancer therapy. In this review, we provide an overview of TRPV expression in breast cancer subtypes, the roles of TRPV channels in various aspects of breast cancer progression and consider implications for future therapeutic approaches. Introduction [1]. TRP channel protein subunits have six transmembrane domains that form tetramers to create the ion channel [1, 2]. -
The Ca2+-Permeable Cation Transient Receptor Potential
1521-0111/92/3/193–200$25.00 https://doi.org/10.1124/mol.116.107946 MOLECULAR PHARMACOLOGY Mol Pharmacol 92:193–200, September 2017 Copyright ª 2017 by The American Society for Pharmacology and Experimental Therapeutics MINIREVIEW—MOLECULAR PHARMACOLOGY IN CHINA The Ca21-Permeable Cation Transient Receptor Potential TRPV3 Channel: An Emerging Pivotal Target for Itch and Skin Diseases Gongxin Wang and KeWei Wang Department of Pharmacology, Qingdao University School of Pharmacy and Institute of Innovative Drugs, Qingdao University, Downloaded from Qingdao, Shandong Province, China Received December 20, 2016; accepted March 31, 2017 ABSTRACT Temperature-sensitive transient receptor potential (TRP) chan- syndrome, which is characterized by severe itching and molpharm.aspetjournals.org nels such as TRPA1 and TRPV1 have been identified as down- palmoplantar and periorificial keratoderma, unveils its crucial stream ion channel targets in the transduction of itch. As a member role in chronic itch and skin diseases. In this review, we will of the temperature-sensitive TRP family, the Ca21-permeable focus on recent progress made in the understanding of nonselective cation channel TRPV3 is expressed abundantly TRPV3 that emerges as an attractive target for developing in skin keratinocytes. Recent identification of gain-of-function effective antipruritic therapy for chronic itch or skin-related mutations of human TRPV3 from patients with Olmsted diseases. attractive target for developing antipruritic therapy in chronic Introduction at ASPET Journals on September 28, 2021 itch or skin-related diseases. Itch (also known as pruritus) is an unpleasant sensation of The superfamily of TRP channels is composed of 28 mam- the skin, provoking the desire or reflex to scratch. -
An Aquaporin-4/Transient Receptor Potential Vanilloid 4 (AQP4/TRPV4) Complex Is Essential for Cell-Volume Control in Astrocytes
An aquaporin-4/transient receptor potential vanilloid 4 (AQP4/TRPV4) complex is essential for cell-volume control in astrocytes Valentina Benfenatia,1, Marco Caprinib,1, Melania Doviziob, Maria N. Mylonakouc, Stefano Ferronib, Ole P. Ottersenc, and Mahmood Amiry-Moghaddamc,2 aInstitute for Nanostructured Materials, Consiglio Nazionale delle Ricerche, 40129 Bologna, Italy; bDepartment of Human and General Physiology, University of Bologna, 40127 Bologna, Italy; and cCenter for Molecular Biology and Neuroscience and Department of Anatomy, University of Oslo, 0317 Oslo, Norway Edited* by Peter Agre, Johns Hopkins Malaria Research Institute, Baltimore, MD, and approved December 27, 2010 (received for review September 1, 2010) Regulatory volume decrease (RVD) is a key mechanism for volume channels (VRAC). Osmolyte efflux through VRAC is thought to control that serves to prevent detrimental swelling in response to provide the driving force for water exit (6, 7). The factors that hypo-osmotic stress. The molecular basis of RVD is not understood. initiate RVD have received comparatively little attention. Here Here we show that a complex containing aquaporin-4 (AQP4) and we test our hypothesis that activation of astroglial RVD depends transient receptor potential vanilloid 4 (TRPV4) is essential for RVD on a molecular interaction between AQP4 and TRPV4. fi in astrocytes. Astrocytes from AQP4-KO mice and astrocytes treated Our hypothesis rests on our recent nding that TRPV4 is with TRPV4 siRNA fail to respond to hypotonic stress by increased strongly expressed in astrocytic endfeet membranes abutting the – intracellular Ca2+ and RVD. Coimmunoprecipitation and immunohis- pia (including the extension of the pia that lines the Virchow tochemistry analyses show that AQP4 and TRPV4 interact and coloc- Robin spaces) and in endfeet underlying ependyma of the ven- alize. -
Ion Channels in the Pathogenesis of Endometriosis: a Cutting-Edge Point of View
International Journal of Molecular Sciences Review Ion Channels in The Pathogenesis of Endometriosis: A Cutting-Edge Point of View 1, 2, 1, Gaetano Riemma y , Antonio Simone Laganà y , Antonio Schiattarella * , Simone Garzon 2 , Luigi Cobellis 1, Raffaele Autiero 1, Federico Licciardi 1, Luigi Della Corte 3 , Marco La Verde 1 and Pasquale De Franciscis 1 1 Department of Woman, Child and General and Specialized Surgery, University of Campania “Luigi Vanvitelli”, 80138 Naples, Italy; [email protected] (G.R.); [email protected] (L.C.); raff[email protected] (R.A.); [email protected] (F.L.); [email protected] (M.L.V.); [email protected] (P.D.F.) 2 Department of Obstetrics and Gynecology, “Filippo Del Ponte” Hospital, University of Insubria, 21100 Varese, Italy; [email protected] (A.S.L.); [email protected] (S.G.) 3 Department of Neuroscience, Reproductive Sciences and Dentistry, School of Medicine, University of Naples Federico II, 80131 Naples, Italy; [email protected] * Correspondence: [email protected]; Tel.: +39-392-165-3275 Equal contributions (joint first authors). y Received: 30 December 2019; Accepted: 5 February 2020; Published: 7 February 2020 Abstract: Background: Ion channels play a crucial role in many physiological processes. Several subtypes are expressed in the endometrium. Endometriosis is strictly correlated to estrogens and it is evident that expression and functionality of different ion channels are estrogen-dependent, fluctuating between the menstrual phases. However, their relationship with endometriosis is still unclear. Objective: To summarize the available literature data about the role of ion channels in the etiopathogenesis of endometriosis. -
Role of the TRPV Channels in the Endoplasmic Reticulum Calcium Homeostasis
cells Review Role of the TRPV Channels in the Endoplasmic Reticulum Calcium Homeostasis Aurélien Haustrate 1,2, Natalia Prevarskaya 1,2 and V’yacheslav Lehen’kyi 1,2,* 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; [email protected] (A.H.); [email protected] (N.P.) 2 Univ. Lille, Inserm, U1003 – PHYCEL – Physiologie Cellulaire, F-59000 Lille, France * Correspondence: [email protected]; Tel.: +33-320-337-078 Received: 14 October 2019; Accepted: 21 January 2020; Published: 28 January 2020 Abstract: It has been widely established that transient receptor potential vanilloid (TRPV) channels play a crucial role in calcium homeostasis in mammalian cells. Modulation of TRPV channels activity can modify their physiological function leading to some diseases and disorders like neurodegeneration, pain, cancer, skin disorders, etc. It should be noted that, despite TRPV channels importance, our knowledge of the TRPV channels functions in cells is mostly limited to their plasma membrane location. However, some TRPV channels were shown to be expressed in the endoplasmic reticulum where their modulation by activators and/or inhibitors was demonstrated to be crucial for intracellular signaling. In this review, we have intended to summarize the poorly studied roles and functions of these channels in the endoplasmic reticulum. Keywords: TRPV channels; endoplasmic reticulum; calcium signaling 1. Introduction: TRPV Channels Subfamily Overview Functional TRPV channels are tetrameric complexes and can be both homo or hetero-tetrameric. They can be divided into two groups: TRPV1, TRPV2, TRPV3, and TRPV4 which are thermosensitive channels, and TRPV5 and TRPV6 channels as the second group. -
Structural Insight Into the Assembly of TRPV Channels
Structure Article Structural Insight into the Assembly of TRPV Channels Kevin W. Huynh,1,3,4 Matthew R. Cohen,2,3,4 Sudha Chakrapani,2,3 Heather A. Holdaway,1,3 Phoebe L. Stewart,1,3 and Vera Y. Moiseenkova-Bell1,2,3,* 1Department of Pharmacology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106, USA 2Deparment of Physiology and Biophysics, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106, USA 3Cleveland Center for Membrane and Structural Biology, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106, USA 4These authors contributed equally to this work *Correspondence: [email protected] http://dx.doi.org/10.1016/j.str.2013.11.008 SUMMARY cytoplasmic amino- and carboxy termini (Li et al., 2011; Venka- tachalam and Montell, 2007). Most TRP channels are polymodal Transient receptor potential (TRP) proteins are a receptors that are activated and modulated by a variety of chem- large family of polymodal nonselective cation chan- ical and physical stimuli (Baez-Nieto et al., 2011). nels. The TRP vanilloid (TRPV) subfamily consists The mammalian TRPV subfamily, consisting of six members, is of six homologous members with diverse functions. the most extensively characterized subfamily of TRP channels TRPV1–TRPV4 are nonselective cation channels pro- (Vennekens et al., 2008). TRPV channels are predicted to contain posed to play a role in nociception, while TRPV5 and six homologous N-terminal ankryin repeats per monomer and a C-terminal TRP box domain (Gaudet, 2008; Ramsey et al., 2006). TRPV6 are involved in epithelial Ca2+ homeostasis. -
Ca2+ Signaling by TRPV4 Channels in Respiratory Function and Disease
cells Review Ca2+ Signaling by TRPV4 Channels in Respiratory Function and Disease Suhasini Rajan, Christian Schremmer, Jonas Weber, Philipp Alt, Fabienne Geiger and Alexander Dietrich * Experimental Pharmacotherapy, Walther-Straub-Institute of Pharmacology and Toxicology, Member of the German Center for Lung Research (DZL), LMU-Munich, 80336 Munich, Germany; [email protected] (S.R.); [email protected] (C.S.); [email protected] (J.W.); [email protected] (P.A.); [email protected] (F.G.) * Correspondence: [email protected] Abstract: Members of the transient receptor potential (TRP) superfamily are broadly expressed in our body and contribute to multiple cellular functions. Most interestingly, the fourth member of the vanilloid family of TRP channels (TRPV4) serves different partially antagonistic functions in the respiratory system. This review highlights the role of TRPV4 channels in lung fibroblasts, the lung endothelium, as well as the alveolar and bronchial epithelium, during physiological and pathophysiological mechanisms. Data available from animal models and human tissues confirm the importance of this ion channel in cellular signal transduction complexes with Ca2+ ions as a second messenger. Moreover, TRPV4 is an excellent therapeutic target with numerous specific compounds regulating its activity in diseases, like asthma, lung fibrosis, edema, and infections. Keywords: TRP channels; TRPV4; respiratory system; lung; endothelium; epithelium; Ca2+ signaling; signal transduction Citation: Rajan, S.; Schremmer, C.; Weber, J.; Alt, P.; Geiger, F.; Dietrich, A. Ca2+ Signaling by TRPV4 1. Introduction Channels in Respiratory Function and Cation selective ion channels of the transient receptor potential (TRP) superfamily con- Disease.