Relevant bibliographies by topics / TRPM2 channel

Academic literature on the topic 'TRPM2 channel'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "TRPM2 channel"

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Yang, Xiao-Ru, Mo-Jun Lin, Lionel S. McIntosh, and James S. K. Sham. "Functional expression of transient receptor potential melastatin- and vanilloid-related channels in pulmonary arterial and aortic smooth muscle." American Journal of Physiology-Lung Cellular and Molecular Physiology 290, no. 6 (June 2006): L1267—L1276. http://dx.doi.org/10.1152/ajplung.00515.2005.

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Transient receptor potential melastatin- (TRPM) and vanilloid-related (TRPV) channels are nonselective cation channels pertinent to diverse physiological functions. Multiple TRPM and TRPV channel subtypes have been identified and cloned in different tissues. However, their information in vascular tissue is scant. In this study, we sought to identify TRPM and TRPV channel subtypes expressed in rat deendothelialized intralobar pulmonary arteries (PAs) and aorta. With RT-PCR, mRNA of TRPM2, TRPM3, TRPM4, TRPM7, and TRPM8 of TRPM family and TRPV1, TRPV2, TRPV3, and TRPV4 of TRPV family were detected in both PAs and aorta. Quantitative real-time RT-PCR showed that TRPM8 and TRPV4 were the most abundantly expressed TRPM and TRPV subtypes, respectively. Moreover, Western blot analysis verified expression of TRPM2, TRPM8, TRPV1, and TRPV4 proteins in both types of vascular tissue. To examine the functional activities of these channels, we monitored intracellular Ca2+ transients ([Ca2+]i) in pulmonary arterial smooth muscle cells (PASMCs) and aortic smooth muscle cells (ASMCs). The TRPM8 agonist menthol (300 μM) and the TRPV4 agonist 4α-phorbol 12,13-didecanoate (1 μM) evoked significant increases in [Ca2+]i in PASMCs and ASMCs. These Ca2+ responses were abolished in the absence of extracellular Ca2+ or the presence of 300 μM Ni2+ but were unaffected by 1 μM nifedipine, suggesting Ca2+ influx via nonselective cation channels. Hence, for the first time, our results indicate that multiple functional TRPM and TRPV channels are coexpressed in rat intralobar PAs and aorta. These novel Ca2+ entry pathways may play important roles in the regulation of pulmonary and systemic circulation.
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Marshall-Gradisnik, Sonya M., Peter Smith, Ekua W. Brenu, Bernd Nilius, Sandra B. Ramos, and Donald R. Staines. "Examination of Single Nucleotide Polymorphisms (SNPs) in Transient Receptor Potential (TRP) Ion Channels in Chronic Fatigue Syndrome Patients." Immunology and Immunogenetics Insights 7 (January 2015): III.S25147. http://dx.doi.org/10.4137/iii.s25147.

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Background The transient receptor potential (TRP) superfamily in humans comprises 27 cation channels with permeability to monovalent and divalent cations. These channels are widely expressed within humans on cells and tissues and have significant sensory and regulatory roles on most physiological functions. Chronic fatigue syndrome (CFS) is an unexplained disorder with multiple physiological impairments. OBJECTIVES The purpose of this study was to determine the role of TRPs in CFS. Methods The study comprised 115 CFS patients (age = 48.68 ± 1.06 years) and 90 nonfatigued controls (age = 46.48 ± 1.22 years). CFS patients were defined according to the 1994 Center for Disease Prevention and Control criteria for CFS. A total of 240 single nucleotide polymorphisms (SNPs) for 21 mammalian TRP ion channel genes ( TRPA1, TRPC1, TRPC2, TRPC3, TRPC4, TRPC6, TRPC7, TRPM1, TRPM2, TRPM3, TRPM4, TRPM5, TRPM6, TRPM7, TRPM8, TRPV1, TRPV2, TRPV3, TRPV4, TRPV5, and TRPV6) were examined via the Agena Biosciences iPLEX Gold assay. Statistical analysis was performed using the PLINK analysis software. Results Thirteen SNPs were significantly associated with CFS patients compared with the controls. Nine of these SNPs were associated with TRPM3 (rs12682832; P < 0.003, rs11142508; P < 0.004, rs1160742; P < 0.08, rs4454352; P < 0.013, rs1328153; P < 0.013, rs3763619; P < 0.014, rs7865858; P ≤ 0.021, rs1504401; P ≤ 0041, rs10115622; P ≤ 0.050), while the remainder were associated with TRPA1 (rs2383844; P ≤ 0.040, rs4738202; P ≤ 0.018) and TRPC4 (rs6650469; P ≤ 0.016, rs655207; P ≤ 0.018). Conclusion The data from this pilot study suggest an association between TRP ion channels, predominantly TRPM3 and CFS. This and other TRPs identified may contribute to the etiology and pathomechanism of CFS.
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Lötsch, Jörn, Dario Kringel, Gerd Geisslinger, Bruno G. Oertel, Eduard Resch, and Sebastian Malkusch. "Machine-Learned Association of Next-Generation Sequencing-Derived Variants in Thermosensitive Ion Channels Genes with Human Thermal Pain Sensitivity Phenotypes." International Journal of Molecular Sciences 21, no. 12 (June 19, 2020): 4367. http://dx.doi.org/10.3390/ijms21124367.

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Genetic association studies have shown their usefulness in assessing the role of ion channels in human thermal pain perception. We used machine learning to construct a complex phenotype from pain thresholds to thermal stimuli and associate it with the genetic information derived from the next-generation sequencing (NGS) of 15 ion channel genes which are involved in thermal perception, including ASIC1, ASIC2, ASIC3, ASIC4, TRPA1, TRPC1, TRPM2, TRPM3, TRPM4, TRPM5, TRPM8, TRPV1, TRPV2, TRPV3, and TRPV4. Phenotypic information was complete in 82 subjects and NGS genotypes were available in 67 subjects. A network of artificial neurons, implemented as emergent self-organizing maps, discovered two clusters characterized by high or low pain thresholds for heat and cold pain. A total of 1071 variants were discovered in the 15 ion channel genes. After feature selection, 80 genetic variants were retained for an association analysis based on machine learning. The measured performance of machine learning-mediated phenotype assignment based on this genetic information resulted in an area under the receiver operating characteristic curve of 77.2%, justifying a phenotype classification based on the genetic information. A further item categorization finally resulted in 38 genetic variants that contributed most to the phenotype assignment. Most of them (10) belonged to the TRPV3 gene, followed by TRPM3 (6). Therefore, the analysis successfully identified the particular importance of TRPV3 and TRPM3 for an average pain phenotype defined by the sensitivity to moderate thermal stimuli.
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Müller, Isabel, Philipp Alt, Suhasini Rajan, Lena Schaller, Fabienne Geiger, and Alexander Dietrich. "Transient Receptor Potential (TRP) Channels in Airway Toxicity and Disease: An Update." Cells 11, no. 18 (September 17, 2022): 2907. http://dx.doi.org/10.3390/cells11182907.

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Our respiratory system is exposed to toxicants and pathogens from both sides: the airways and the vasculature. While tracheal, bronchial and alveolar epithelial cells form a natural barrier in the airways, endothelial cells protect the lung from perfused toxic compounds, particulate matter and invading microorganism in the vascular system. Damages induce inflammation by our immune response and wound healing by (myo)fibroblast proliferation. Members of the transient receptor potential (TRP) superfamily of ion channel are expressed in many cells of the respiratory tract and serve multiple functions in physiology and pathophysiology. TRP expression patterns in non-neuronal cells with a focus on TRPA1, TRPC6, TRPM2, TRPM5, TRPM7, TRPV2, TRPV4 and TRPV6 channels are presented, and their roles in barrier function, immune regulation and phagocytosis are summarized. Moreover, TRP channels as future pharmacological targets in chronic obstructive pulmonary disease (COPD), asthma, cystic and pulmonary fibrosis as well as lung edema are discussed.
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Saito, Shigeru, and Ryuzo Shingai. "Evolution of thermoTRP ion channel homologs in vertebrates." Physiological Genomics 27, no. 3 (December 2006): 219–30. http://dx.doi.org/10.1152/physiolgenomics.00322.2005.

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In mammalian thermosensation, nine temperature-sensitive ion channels that are activated by distinct temperature thresholds have been identified as thermosensors. These ion channels belong to the transient receptor potential (TRP) superfamily and are referred to as “thermoTRPs” (TRPV1, TRPV2, TRPV3, TRPV4, TRPM2, TRPM4, TRPM5, TRPM8, and TRPA1). To elucidate the evolutionary processes of thermoTRPs, we conducted comprehensive searches for mammalian thermoTRP gene homologs in the draft genome sequences of chicken ( Gallus gallus), western clawed frog ( Xenopus tropicalis), zebrafish ( Danio rerio), and pufferfish ( Fugu rubripes). Newly identified homologs were compared with known thermoTRPs, and phylogenetic analyses were conducted. Our comparative analyses revealed that most of the mammalian thermo-TRP members already existed in the common ancestor of fishes and tetrapods. Tetrapods shared almost the same repertoire, except that the western clawed frog expanded TRPV4s (six copies) and TRPM8s (two copies), which were diversified considerably. Comparisons of nonsynonymous and synonymous substitution rates among TRPV4s suggested that one copy of the TRPV4 channel in the western clawed frog retained its original function, while the other copies diversified and obtained slightly different properties. In fish lineages, several members of thermo-TRPs have duplicated in the whole genome duplication occurred in the ancestral ray-finned fish; however, some of the copies have subsequently been lost. Furthermore, fishes do not possess the three members of thermoTRPs existed in mammals, e.g., thermoTRPs activated by noxious heat, warm, and cool temperatures. Our results suggest that thermosensation mechanisms have changed through vertebrate evolution with respect to thermosensor repertoires.
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Mei, Zhu-Zhong, Hong-Ju Mao, and Lin-Hua Jiang. "Conserved cysteine residues in the pore region are obligatory for human TRPM2 channel function." American Journal of Physiology-Cell Physiology 291, no. 5 (November 2006): C1022—C1028. http://dx.doi.org/10.1152/ajpcell.00606.2005.

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TRPM2 proteins belong to the melastatin-related transient receptor potential or TRPM subfamily and form Ca2+-permeable cationic channels activated by intracellular adenosine diphosphoribose (ADPR). The TRPM2 channel subunit, like all its close relatives, is structurally homologous to the well-characterized voltage-gated potassium channel subunits, each containing six transmembrane segments and a putative pore loop between the fifth and sixth segments. Nevertheless, the structural elements determining the TRPM2 channel functions are still not well understood. In this study, we investigated the functional role of two conserved cysteine residues (at positions 996 and 1008) in the putative pore region of the human TRPM2 by site-directed mutagenesis, combined with electrophysiological and biochemical approaches. Expression of wild-type hTRPM2 channels in human embryonic kidney (HEK-293) cells resulted in robust ADPR-evoked currents. Substitution of cysteine with alanine or serine generated mutant channels that failed to be activated by ADPR. Furthermore, experiments done by Western blot analysis, immunocytochemistry, biotin labeling, and coimmunoprecipitation techniques showed no obvious changes in protein expression, trafficking or membrane localization, and the ability to interact with neighboring subunits that is required for channel assembly. Coexpression of wild-type and mutant subunits significantly reduced the ADPR-evoked currents; for the combination of wild-type and C996S mutant subunits, the reduction was ∼95%, indicating that incorporation of one or more nonfunctional C996S subunits leads to the loss of channel function. These results taken together suggest that the cysteine residues in the pore region are obligatory for TRPM2 channel function.
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Du Preez, Stanley, Natalie Eaton-Fitch, Helene Cabanas, Donald Staines, and Sonya Marshall-Gradisnik. "Characterization of IL-2 Stimulation and TRPM7 Pharmacomodulation in NK Cell Cytotoxicity and Channel Co-Localization with PIP2 in Myalgic Encephalomyelitis/Chronic Fatigue Syndrome Patients." International Journal of Environmental Research and Public Health 18, no. 22 (November 12, 2021): 11879. http://dx.doi.org/10.3390/ijerph182211879.

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Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS) is a complex multisystemic disorder responsible for significant disability. Although a unifying etiology for ME/CFS is uncertain, impaired natural killer (NK) cell cytotoxicity represents a consistent and measurable feature of this disorder. Research utilizing patient-derived NK cells has implicated dysregulated calcium (Ca2+) signaling, dysfunction of the phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent cation channel, transient receptor potential melastatin (TRPM) 3, as well as altered surface expression patterns of TRPM3 and TRPM2 in the pathophysiology of ME/CFS. TRPM7 is a related channel that is modulated by PIP2 and participates in Ca2+ signaling. Though TRPM7 is expressed on NK cells, the role of TRPM7 with IL-2 and intracellular signaling mechanisms in the NK cells of ME/CFS patients is unknown. This study examined the effect of IL-2 stimulation and TRPM7 pharmacomodulation on NK cell cytotoxicity using flow cytometric assays as well as co-localization of TRPM7 with PIP2 and cortical actin using confocal microscopy in 17 ME/CFS patients and 17 age- and sex-matched healthy controls. The outcomes of this investigation are preliminary and indicate that crosstalk between IL-2 and TRMP7 exists. A larger sample size to confirm these findings and characterization of TRPM7 in ME/CFS using other experimental modalities are warranted.
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Szollosi, Andras. "Two Decades of Evolution of Our Understanding of the Transient Receptor Potential Melastatin 2 (TRPM2) Cation Channel." Life 11, no. 5 (April 27, 2021): 397. http://dx.doi.org/10.3390/life11050397.

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The transient receptor potential melastatin (TRPM) family belongs to the superfamily of TRP ion channels. It consists of eight family members that are involved in a plethora of cellular functions. TRPM2 is a homotetrameric Ca2+-permeable cation channel activated upon oxidative stress and is important, among others, for body heat control, immune cell activation and insulin secretion. Invertebrate TRPM2 proteins are channel enzymes; they hydrolyze the activating ligand, ADP-ribose, which is likely important for functional regulation. Since its cloning in 1998, the understanding of the biophysical properties of the channel has greatly advanced due to a vast number of structure–function studies. The physiological regulators of the channel have been identified and characterized in cell-free systems. In the wake of the recent structural biochemistry revolution, several TRPM2 cryo-EM structures have been published. These structures have helped to understand the general features of the channel, but at the same time have revealed unexplained mechanistic differences among channel orthologues. The present review aims at depicting the major research lines in TRPM2 structure-function. It discusses biophysical properties of the pore and the mode of action of direct channel effectors, and interprets these functional properties on the basis of recent three-dimensional structural models.
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Wang, Longfei, Tian-Min Fu, Yiming Zhou, Shiyu Xia, Anna Greka, and Hao Wu. "Structures and gating mechanism of human TRPM2." Science 362, no. 6421 (November 22, 2018): eaav4809. http://dx.doi.org/10.1126/science.aav4809.

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Transient receptor potential (TRP) melastatin 2 (TRPM2) is a cation channel associated with numerous diseases. It has a C-terminal NUDT9 homology (NUDT9H) domain responsible for binding adenosine diphosphate (ADP)–ribose (ADPR), and both ADPR and calcium (Ca2+) are required for TRPM2 activation. Here we report cryo–electron microscopy structures of human TRPM2 alone, with ADPR, and with ADPR and Ca2+. NUDT9H forms both intra- and intersubunit interactions with the N-terminal TRPM homology region (MHR1/2/3) in the apo state but undergoes conformational changes upon ADPR binding, resulting in rotation of MHR1/2 and disruption of the intersubunit interaction. The binding of Ca2+ further engages transmembrane helices and the conserved TRP helix to cause conformational changes at the MHR arm and the lower gating pore to potentiate channel opening. These findings explain the molecular mechanism of concerted TRPM2 gating by ADPR and Ca2+ and provide insights into the gating mechanism of other TRP channels.
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Nilius, B., F. Mahieu, Y. Karashima, and T. Voets. "Regulation of TRP channels: a voltage–lipid connection." Biochemical Society Transactions 35, no. 1 (January 22, 2007): 105–8. http://dx.doi.org/10.1042/bst0350105.

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TRP (transient receptor potential) channels respond to a plethora of stimuli in a fine-tuned manner. We show here that both membrane potential and the level of PI (phosphatidylinositol) phosphates are efficient regulators of TRP channel gating. Recent work has shown that this regulation applies to several members of the TRPV (TRP vanilloid) subfamily (TRPV1 and TRPV5) and the TRPM (TRP melastatin) subfamily (TRPM4/TRPM5/TRPM7/TRPM8), whereas regulation of members of the TRPC subfamily is still disputed. The mechanism whereby PIP2 (PI 4,5-bisphosphate) acts on TRPM4, a Ca2+- and voltage-activated channel, is shown in detail in this paper: (i) PIP2 may bind directly to the channel, (ii) PIP2 induces sensitization to activation by Ca2+, and (iii) PIP2 shifts the voltage dependence towards negative and physiologically more meaningful potentials. A PIP2-binding pocket seems to comprise a part of the TRP domain and especially pleckstrin homology domains in the C-terminus.
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Dissertations / Theses on the topic "TRPM2 channel"

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Li, Xin. "TRPM2 channel-mediated signalling mechanisms for neuronal cell death." Thesis, University of Leeds, 2017. http://etheses.whiterose.ac.uk/18576/.

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Transient receptor potential melastatin-related 2 (TRPM2) channel is gated by ADP-ribose (ADPR) and potently activated by reactive oxygen species (ROS) through stimulating ADPR-generating mechanisms. Recent studies provide evidence to show a crucial role for TRPM2 in neuronal death and cognitive impairment associated with ischemic stroke and Alzheimer’s disease. However, the underlying mechanisms are poorly understood. Studies described in this thesis adopted genetic and pharmacological interventions, in conjunction with immunofluorescent and live cell imaging, to investigate TRPM2-dependent cell death induced by H2O2 and the 42-residue of amyloid β (Aβ42) in cultured hippocampal neurons. H2O2 and Aβ42 induced significant neuronal death, which was reduced or prevented by TRPM2 knock-out (TRPM2-KO), TRPM2 channel inhibitors, or Zn2+ chelator TPEN. H2O2 and Aβ42 induced intracellular Zn2+ increase, lysosomal dysfunction and Zn2+ release, mitochondrial Zn2+ accumulation, dysfunction and ROS generation. Bafilomycin A1-induced lysosomal dysfunction also resulted in mitochondrial Zn2+ accumulation and ROS generation. These events were abolished by TRPM2-KO or suppressed by inhibiting poly(ADP-ribose) polymerase-1 (PARP-1) or TRPM2 channel. Immunofluorescent imaging suggests mitochondrial localization of TRPM2. ADPR enhanced Zn2+ accumulation in isolated mitochondria from wild-type (WT) but not TRPM2-KO neurons. Finally, the inhibition of protein kinase C (PKC) and NADPH oxidases (NOX), particularly NOX1/4, suppressed H2O2/Aβ42-induced neuronal death and Aβ42-induced intracellular Zn2+ increase, lysosomal and mitochondrial dysfunction, and mitochondrial ROS generation. The inhibition of the proline-rich tyrosine kinase 2 (Pyk2) and the downstream MEK/ERK kinases protected against Aβ42-induced neuronal death. Taken together, these results provide evidence to support a vicious positive feedback signalling loop that drives hippocampal neuronal death in response to ROS and Aβ42, in which the TRPM2 channel in mitochondria integrates multiple mechanisms comprising PKC/NOX-mediated ROS generation, lysosomal dysfunction and Zn2+ release, mitochondrial Zn2+ accumulation, mitochondrial dysfunction and ROS generation. In addition, the Pyk2-MEK-ERK signalling pathway is critically involved in Aβ42-induced TRPM2-dependent neuronal death. These findings provide novel insights into the mechanisms underlying neuronal death and cognitive impairment related to ischemic stroke and AD.
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Lange, Ingo. "The TRPM2 ion channel in nucleotide-gated calcium signaling." kostenfrei, 2008. http://d-nb.info/989951200/34.

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Xia, Rong. "TRPM2 Channel : Assembly, Ion permeability, and regulation by interacting proteins." Thesis, University of Leeds, 2009. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.511157.

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Syed, Mortadza Sharifah Alawieyah. "Microglial TRPM2 channel activation and its relationship to neurodegenerative diseases." Thesis, University of Leeds, 2017. http://etheses.whiterose.ac.uk/19281/.

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Microglial cell plays a key role in neuroinflammation induced by diverse danger associated molecular patterns (DAMP) molecules, such as Zn2+, Aβ42 and TNF-α, and strongly implicated in neurodegenerative diseases. The molecular mechanisms for neuroinflammation are however not fully defined. Reactive oxygen species (ROS) production is critical in DAMP-induced microglial cell activation and cytokine production. Studies presented in this thesis aimed to investigate, using immunocytochemistry, single cell imaging, cell death and ELISA assays in combination with genetic and pharmacological interventions, the role of ROS-sensitive TRPM2 channel in cell death, cell activation and production of TNF-α in primary microglial cells in response to Zn2+, Aβ42 and TNF-α as well as H2O2. H2O2 (10-300 mM) and Zn2+ (10-300 mM) induced concentration-dependent increases in the intracellular Ca2+ concentration ([Ca2+]i) via Ca2+ influx, which were prevented by TRPM2 knockout (TRPM2-KO) or treatment with TRPM2 inhibitor 2-APB or PARP inhibitor PJ34. Pathological concentrations of H2O2 (100-300 mM) and Zn2+ (100-300 mM) induced substantial cell death that was ablated by TRPM2-KO and treatment with 2-APB or PJ34. Zn2+ also induced ROS production and PARP-1 activation. All these Zn2+-induced effects were suppressed by treatment with PKC inhibitor chelerythrine, NOX inhibitors DPI, GKT137831 or Phox-I2. Zn2+-induced PARP-1 stimulation, increase in the [Ca2+]i and cell death were also inhibited by PYK2 inhibitor PF431396 or MEK/ERK inhibitor U0126. Exposure to Aβ42 (30-300 nM) and TNF-α (10-100 ng/ml) resulted in concentration-dependent TRPM2-mediated Ca2+ influx and increases in the [Ca2+]i, microglial cell activation and TNF-α production. Aβ42 and TNF-α stimulated ROS production and PARP-1 activation. These effects induced by Aβ42 or TNF-α were suppressed by inhibiting PKC and NOX. Moreover, Aβ42/TNF-α induced PARP-1 activation, increase in the [Ca2+]i, microglial cell activation and TNF-α production were attenuated by inhibiting PYK2 and MEK/ERK. In summary, studies provide strong evidence to reveal a critical role for the TRPM2 channel in Ca2+ signalling in microglial cells induced by Zn2+, Aβ42 and TNF-α. TRPM2 channel activation by Zn2+, Aβ42 and TNF-α depends on PKC/NOX-mediated ROS production and PARP-1 activation and is additionally enhanced by the PYK2-MEK-ERK signalling pathway. Such mechanisms are critically involved in cell death in response to Zn2+, or microglial cell activation and TNF-α production in response to Aβ42 and TNF-α. These findings provide novel insights into the role of microglial cells in neuroinflammation and in the pathogenesis of neurodegenerative diseases.
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Abuarab, Nada Khaled S. "TRPM2 ion channel trafficking and its role in mitochondrial fragmentation and cell death." Thesis, University of Leeds, 2015. http://etheses.whiterose.ac.uk/12490/.

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Mitochondria play a central role in oxidative stress-induced cell death. By increasing the production of reactive oxygen species, such as H2O2, oxidative stress causes mitochondrial fragmentation and apoptosis. It was hypothesised that Transient Receptor Potential Melastatin 2 (TRPM2) channels play a role in mitochondrial fragmentation and cell death. The rationale behind this hypothesis was the published evidence that oxidative stress stimulates TRPM2 channels, resulting in an increase in the cytosolic levels of Ca2+ and Zn2+, and that both these ions are detrimental to mitochondrial health and cell survival. To test the hypothesis, human umbilical vein endothelial cells (HUVECs) and endothelial cells isolated from wild-type and TRPM2 knock-out mice were used. TRPM2 actions were suppressed using pharmacological agents and small interfering RNA (siRNA). Fluorescent reporters were used to examine changes in intracellular ion distribution and organelle morphology. Molecular biology, biochemical and imaging techniques were used to examine the dynamics of ions and organelles. Exposure of HUVECs to H2O2 or high glucose stress led to TRPM2 activation, resulting in extracellular Ca2+ entry, lysosomal membrane permeability (LMP) and the release of lysosomal free Zn2+. Unexpectedly, this was accompanied by the accumulation of Zn2+ in the mitochondria. The rise in mitochondrial Zn2+ led to extensive mitochondrial fragmentation, mitochondrial outer membrane permeabilisation (MMP) and cell death. Silencing of TRPM2 channels with siRNA prevented intracellular Zn2+ redistribution, mitochondrial fragmentation and cell death. Endothelial cells derived from TRPM2 knock-out mice were resistant to oxidative stress-induced mitochondrial fragmentation. Biochemical and immunostaining experiments revealed an unexpected presence of TRPM2 channels in mitochondria, where they mediated mitochondrial Zn2+ uptake. Accumulation of Zn2+ in the mitochondria led to mitochondrial fragmentation by promoting the recruitment of cytoplasmic Drp1, an enzyme responsible for mitochondrial fission. Taken together, the results of this thesis revealed a novel mechanism for how oxidative stress can cause excessive mitochondrial fragmentation and cell death: the mechanism involves activation of TRPM2 channels leading to increased Ca2+ entry, LMP and release of lysosomal Zn2+; Zn2+ thus released is taken up by the mitochondria, leading to Drp1 recruitment, mitochondrial fragmentation and finally cell death. Since mitochondrial fragmentation is associated with several age-related chronic illnesses, including neuronal (Alzheimer’s, Parkinson’s), cardiovascular (atherosclerosis, myocardial infarction) and metabolic/inflammatory (diabetes) disorders, these results suggest that the TRPM2 channel is a novel target that could be explored for therapeutic intervention of age-related illnesses.
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Kouzai, Daisuke. "Chemical biological studies on oxidation status-sensitive calcium channels." 京都大学 (Kyoto University), 2014. http://hdl.handle.net/2433/188546.

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Ferioli, Silvia [Verfasser], and Barbara [Akademischer Betreuer] Conradt. "Cellular functions of the kinase-coupled TRPM6/TRPM7 channels / Silvia Ferioli ; Betreuer: Barbara Conradt." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2018. http://d-nb.info/1162840501/34.

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Massullo, Pam. "Aberrant subcellular targeting of the G185R neutrophil elastase mutant associated with severe congenital neutropenia induces premature apoptosis of differentiating promyelocytes & expression and function of the transient receptor potential 2 (TRPM2) ion channel in dendritic cells." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1172865905.

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Zou, Jie. "Function and modulation of TRPM2 channels." Thesis, University of Leeds, 2013. http://etheses.whiterose.ac.uk/5902/.

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Melastatin-related transient receptor potential 2 (TRPM2) channel is a Ca2+-permeable cation channel that is gated by ADP-ribose (ADPR) and also activated by reactive oxygen species (ROS) such as H2O2. TRPM2 channel are shown to be critically involved in several physiological and pathological cell processes. Previous studies have reported inhibition of the human TRPM2 channel by extracellular acidic pH. However, the underlying mechanism is not fully understood. In the present study, I performed patch-clamp recordings to examine the effect of extracellular acidic pH on ADPR-induced currents in HEK293 cells heterogeneously expressing human TRPM2 (hTRPM2) or mouse TRPM2 (mTRPM2) channels. The results showed that the inhibition was substantially reversible upon brief exposure to acidic pH but became irreversible after prolonged exposure, supporting the mechanism in which protons bind to and inhibit the open TRPM2 channel and the proton-binding induces further conformational changes leading to channel inactivation. Furthermore, the mTRPM2 channel exhibited a lower sensitivity to, and slower kinetics of, inhibition, than the hTRPM2 channel. A residue in the pore region (His-995 in hTRPM2 and Gln-992 in mTRPM2) had a crucial role in determining such species differences. The pharmacology of the TRPM2 channel is poor, with no specific inhibitor. Here, I examined the effects of 48 hit compounds identified from screening chemical libraries on hTRPM2 channels expressed in HEK293 cells. Four compounds inhibited H2O2-induced Ca2+-response with a micromolar to submicromolar potency and abolished ADPR-induced currents at 10 μM, indicating that they act as TRPM2 channel inhibitors. The TRPM2 channel was reported to be functionally expressed in macrophage cells, but its role in mediating ROS-induced Ca2+ signalling and cell death is largely unclear. This study examined the contribution and mechanism of the TRPM2 channel in H2O2-induced Ca2+-responses and cell death in RAW264.7 and differentiated THP-1 macrophage cells and peritoneal macrophage cells isolated from TRPM2+/+ and TRPM2-/- mice. The results showed that TRPM2 channels operated as cell surface Ca2+-permeable channels and constituted the principal Ca2+ signalling mechanism, but played a limited role in cell death. In summary, the results from my study provided useful information to advance the understanding of the pharmacology and functional roles of the TRPM2 channels.
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Naylor, Jacqueline. "Function and pharmacology of TRPM3 ion channel." Thesis, University of Leeds, 2008. http://etheses.whiterose.ac.uk/330/.

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For many ion channels there are few, if any, pharmacological agents, and even fewer showing specificity. In this study, a set of pharmacological tools were developed to investigate TRPM3, a widely expressed transient receptor potential (TRP) channel for which no functional role has yet been identified. Human TRPM3 was first expressed in HEK 293 cells and shown to be activated by hypo-osmotic challenge or sphingosine, consistent with previous reports. In addition, TRPM3 was activated by pregnenolone sulphate. Hydrophobicity analysis of the TRPM3 amino acid sequence revealed a short and reasonably unique peptide in the 3rd extracellular loop (E3) region, to which polyclonal antiserum (TM3E3) was produced. Extracellular application of TM3E3 inhibited TRPM3 function with a high degree of specificity, having no effect on TRPM2 or example members of other sub-types of mammalian TRP, TRPC5 or TRPV4. The data validate E3-targeting as an approach for production of isoform-specific channel blockers and reveal a specific agent for blocking TRPM3. The cellular and tissue functions of TRPM3 were also investigated. RT-PCR and immunocytochemistry demonstrated TRPM3 expression in human saphenous vein smooth muscle cells, where sphingosine- and pregnenolone sulphate-induced calcium responses were also apparent. These calcium responses could be selectively blocked by TM3E3. Furthermore, TRPM3 activators inhibited matrix metalloproteinase and interleukin-6 secretion, indicating a protective function for TRPM3 in vascular smooth muscle cells. Medium throughput screening systems were employed to screen a library of compounds for further TRPM3 modulators with vascular relevance. Cholesterol, antidepressants, antipsychotics, calmodulin inhibitors, and PIP2 all inhibited TRPM3, whereas nifedipine and elevated temperature activated the channel. TRPM3 appears to be regulated by a large number of different chemicals and mechanisms. In summary, TRPM3 has constitutive, protective, activity which can be suppressed by a multitude of compounds, including known vascular disease factors such as cholesterol.
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Book chapters on the topic "TRPM2 channel"

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Hecquet, Claudie M., Gias U. Ahmmed, and Asrar B. Malik. "TRPM2 Channel Regulates Endothelial Barrier Function." In Advances in Experimental Medicine and Biology, 155–67. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-500-2_10.

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Guinamard, Romain, Laurent Sallé, and Christophe Simard. "The Non-selective Monovalent Cationic Channels TRPM4 and TRPM5." In Transient Receptor Potential Channels, 147–71. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-94-007-0265-3_8.

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Colsoul, Barbara, Miklos Kecskes, Koenraad Philippaert, Aurelie Menigoz, and Rudi Vennekens. "The Ca2+-Activated Monovalent Cation-Selective Channels TRPM4 and TRPM5." In Methods in Pharmacology and Toxicology, 103–25. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-077-9_6.

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Hall, Hannah K., and David W. Koh. "Methods for Investigating Transient Receptor Potential Melastatin-2 (TRPM2): A Cation Channel Activated by ADP-Ribose and Involved in Cell Death." In Methods in Molecular Biology, 213–26. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2891-1_13.

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Hermosura, Meredith C. "Alterations in TRPM2 and TRPM7 Functions in the Immune System Could Confer Susceptibility to Neurodegeneration." In Pathologies of Calcium Channels, 333–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40282-1_18.

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Landau, Daniel, and Hanna Shalev. "TRPM6 and Hypomagnesaemia/Hypocalcaemia." In Pathologies of Calcium Channels, 523–31. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40282-1_25.

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Fleig, Andrea, and Reinhold Penner. "Emerging Roles of TRPM Channels." In Mammalian TRP Channels as Molecular Targets, 248–62. Chichester, UK: John Wiley & Sons, Ltd, 2008. http://dx.doi.org/10.1002/0470862580.ch18.

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Zholos, Alexander, Christopher Johnson, Theodor Burdyga, and Donal Melanaphy. "TRPM Channels in the Vasculature." In Transient Receptor Potential Channels, 707–29. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-94-007-0265-3_37.

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Streets, Andrew, and Albert Ong. "TRPP2 in Polycystic Kidney Disease." In Pathologies of Calcium Channels, 491–522. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40282-1_24.

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Grimm, Christian, and Math P. Cuajungco. "TRPML Channels and Mucolipidosis Type IV." In Pathologies of Calcium Channels, 365–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40282-1_19.

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Conference papers on the topic "TRPM2 channel"

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Koh, David W., Daniel P. Powell, Steven D. Blake, Joy L. Hoffman, and Xiaoxing Feng. "Abstract 1717: Selective induction of breast adenocarcinoma cell death via inhibition of the transient receptor potential melastatin-2 (TRPM2) cation channel." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1717.

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Koh, David W., Steven D. Blake, and Daniel P. Powell. "Abstract 1269: Enhanced cytotoxicity in primary human metastatic melanoma cells via inhibition of the transient receptor potential melastatin-2 (TRPM2) channel." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1269.

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Botta, Davide, Andre' Ballesteros-Tato, Kyle Martin, Louise Hartson, Tirumalai Rangasamy, Thomas J. Mariani, Troy D. Randall, Debra A. Cockayne, Christopher S. Stevenson, and Frances E. Lund. "Deficiency Of The Transient Receptor Potential Melastatin 2 (TRPM2) Cation Channel Provides Protection Against Pulmonary Inflammation In A Murine Model Of Chronic Obstructive Pulmonary Disease (COPD)." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1305.

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Borodin, Evgeniy. "SEARCH FOR POTENTIAL LIGANDS FOR TRPM8 WITH THE HELP OF COMPUTER DESIGN." In XIV International Scientific Conference "System Analysis in Medicine". Far Eastern Scientific Center of Physiology and Pathology of Respiration, 2020. http://dx.doi.org/10.12737/conferencearticle_5fe01d9b2fdca3.97577371.

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A search was carried out for potential ligands to TRPM8 - a representative of the family of cationic channels with a transient receptor potential involved in the development of bronchial hypersensitivity and the occurrence of bronchospasm in response to low temperatures. We used a structural design and molecular docking using the autodock software package (http://autodock.scripps.edu/), which allows automated testing of many potential ligands for TRPM8. Docking was carried out with tyrosine 745 (Y745) amino acid residue as a critical residue for channel sensitivity to menthol, a classic TRPM8 agonist. The selection of potential candidates for the role of drugs intended for the treatment of bronchial cold hyperreactivity using in silico methods can be supplemented by testing their biological activity in vitro experiments with cell and tissue cultures and in vivo with experimental animals.
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Dyrda, P., P. Malinouski, B. Nilius, and LJ Janssen. "Bronchial Thermoplasty Involves Activation of TRPV2 Channels?." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3913.

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Frede, W., R. Medert, M. Freichel, M. Gorenflo, and S. Uhl. "Cardiac Role of the Ion Channel TRPM4 under Right Ventricular Pressure Load in Rat." In 50th Annual Meeting of the German Society for Pediatric Cardiology (DGPK). Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1628318.

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Asuthkar, Swapna, Kiran Velpula, and Eleonora Zakharian. "Abstract 615: TRPM8 channel as a novel molecular target in androgen-regulated prostate cancer cells." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-615.

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Liu, Mingli, Koichi Inoue, Tiandong Leng, Shanchun Guo, and Zhigang Xiong. "Abstract 4067: TRPM7 channels regulate glioma stem cell through STAT3 and Notch signaling pathways." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4067.

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Koomoa, Dana-Lynn T., and Ingo Lange. "Abstract LB-68: MYCN-induced TRPM7 expression and channel activity occurs through a mechanism that involves ornithine decarboxylase." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-lb-68.

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Liu, Mingli. "Abstract 774: Regulation of autophagy and epigenetic modulator micro RNA by transient receptor potential melastatin 7 (TRPM7) channel in glioma." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-774.

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