388 research outputs found

    Redox-Sensitive TRP Channels: TRPA1 and TRPM2

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    The transient receptor potential (TRP) family includes cation-permeable ion channels activated by diverse stimuli ranging from chemical compounds, mechanical force and temperature. TRPA1, TRPV1, TRPC5, TRPM2, and TRPM7 are reported to be activated by reactive oxygen species (ROS). The sensitivity of TRPs to ROS is in part associated with pathogenesis caused by ROS and physiological adaptations to redox signals. The present review focuses on the well-defined ROS-sensitive TRP channels, TRPA1 and TRPM2, and summarizes recent reports regarding their activation mechanism by ROS and their relevance to pathological conditions and physiological functions in which ROS are involved

    Brain Activity Stimulated by Prism Adaptation Tasks Utilized for the Treatment of Unilateral Spatial Neglect: A Study with fNIRS

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    We investigated the neurological basis for efficacy of prism adaptation therapy, which is used for the treatment of poststroke unilateral spatial neglect (USN). Study subjects were 6 USN-positive (+), 6 USN-negative patients, and 6 healthy volunteer control subjects. USN was identified by the Behavioural Inattention Test (BIT). During the tasks, brain activity was assessed with fNIRS via changes in oxyHb concentration per unit length. There was no significant difference in the number of errors in the task between the 3 groups. However, in the USN(+) group there was a significantly greater reduction in oxyHb levels in the right parietal association cortex during the prism adaptation task than in the other 2 groups (P < 0.05). There was an immediate improvement in USN symptoms as well as a significant increase in oxyHb levels during the prism adaptation in the channels covering the right frontal and parietal lobes in 2 patients in the USN(+) group (P < 0.05). This result suggested that decreased activity in the right parietal association cortex, which is related to spatial perception, during the prism adaptation task and task-induced reorganization of the right frontal and parietal areas were involved in improvement in USN symptoms

    Study on the Transport Characteristics of Floating Garbage in Hori River

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    Source: ICHE Conference Archive - https://mdi-de.baw.de/icheArchiv

    Evolutionary conservation and changes in insect TRP channels

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    <p>Abstract</p> <p>Background</p> <p>TRP (Transient Receptor Potential) channels respond to diverse stimuli and thus function as the primary integrators of varied sensory information. They are also activated by various compounds and secondary messengers to mediate cell-cell interactions as well as to detect changes in the local environment. Their physiological roles have been primarily characterized only in mice and fruit flies, and evolutionary studies are limited. To understand the evolution of insect TRP channels and the mechanisms of integrating sensory inputs in insects, we have identified and compared TRP channel genes in <it>Drosophila melanogaster, Bombyx mori, Tribolium castaneum, Apis mellifera, Nasonia vitripennis</it>, and <it>Pediculus humanus </it>genomes as part of genome sequencing efforts.</p> <p>Results</p> <p>All the insects examined have 2 TRPV, 1 TRPN, 1 TRPM, 3 TRPC, and 1 TRPML subfamily members, demonstrating that these channels have the ancient origins in insects. The common pattern also suggests that the mechanisms for detecting mechanical and visual stimuli and maintaining lysosomal functions may be evolutionarily well conserved in insects. However, a TRPP channel, the most ancient TRP channel, is missing in <it>B. mori</it>, <it>A. mellifera</it>, and <it>N. vitripennis</it>. Although <it>P. humanus </it>and <it>D. melanogaster </it>contain 4 TRPA subfamily members, the other insects have 5 TRPA subfamily members. <it>T. castaneum</it>, <it>A. mellifera</it>, and <it>N. vitripennis </it>contain TRPA5 channels, which have been specifically retained or gained in Coleoptera and Hymenoptera. Furthermore, TRPA1, which functions for thermotaxis in <it>Drosophila</it>, is missing in <it>A. mellifera </it>and <it>N. vitripennis</it>; however, they have other Hymenoptera-specific TRPA channels (AmHsTRPA and NvHsTRPA). NvHsTRPA expressed in HEK293 cells is activated by temperature increase, demonstrating that HsTRPAs function as novel thermal sensors in Hymenoptera.</p> <p>Conclusion</p> <p>The total number of insect TRP family members is 13-14, approximately half that of mammalian TRP family members. As shown for mammalian TRP channels, this may suggest that single TRP channels are responsible for integrating diverse sensory inputs to maintain the insect sensory systems. The above results demonstrate that there are both evolutionary conservation and changes in insect TRP channels. In particular, the evolutionary processes have been accelerated in the TRPA subfamily, indicating divergence in the mechanisms that insects use to detect environmental temperatures.</p

    Sensitization of TRPV1 by EP(1 )and IP reveals peripheral nociceptive mechanism of prostaglandins

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    Prostaglandin E(2 )(PGE(2)) and prostaglandin I(2 )(PGI(2)) are major inflammatory mediators that play important roles in pain sensation and hyperalgesia. The role of their receptors (EP and IP, respectively) in inflammation has been well documented, although the EP receptor subtypes involved in this process and the underlying cellular mechanisms remain to be elucidated. The capsaicin receptor TRPV1 is a nonselective cation channel expressed in sensory neurons and activated by various noxious stimuli. TRPV1 has been reported to be critical for inflammatory pain mediated through PKA- and PKC-dependent pathways. PGE(2 )or PGI(2)increased or sensitized TRPV1 responses through EP(1 )or IP receptors, respectively predominantly in a PKC-dependent manner in both HEK293 cells expressing TRPV1 and mouse DRG neurons. In the presence of PGE(2 )or PGI(2), the temperature threshold for TRPV1 activation was reduced below 35°C, so that temperatures near body temperature are sufficient to activate TRPV1. A PKA-dependent pathway was also involved in the potentiation of TRPV1 through EP(4 )and IP receptors upon exposure to PGE(2 )and PGI(2), respectively. Both PGE(2)-induced thermal hyperalgesia and inflammatory nociceptive responses were diminished in TRPV1-deficient mice and EP(1)-deficient mice. IP receptor involvement was also demonstrated using TRPV1-deficient mice and IP-deficient mice. Thus, the potentiation or sensitization of TRPV1 activity through EP(1 )or IP activation might be one important mechanism underlying the peripheral nociceptive actions of PGE(2 )or PGI(2)

    Isoform-specific modulation of the chemical sensitivity of conserved TRPA1 channel in the major honeybee ectoparasitic mite, Tropilaelaps mercedesae

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    We identified and characterized the TRPA1 channel of Tropilaelaps mercedesae (TmTRPA1), one of two major species of honeybee ectoparasitic mite. Three TmTRPA1 isoforms with unique N-terminal sequences were activated by heat, and the isoform highly expressed in the mite's front legs, TmTRPA1b, was also activated by 27 plant-derived compounds including electrophiles. This suggests that the heat- and electrophile-dependent gating mechanisms as nocisensitive TRPA1 channel are well conserved between arthropod species. Intriguingly, one TmTRPA1 isoform, TmTRPA1a, was activated by only six compounds compared with two other isoforms, demonstrating that the N-terminal sequences are critical determinants for the chemical sensitivity. This is the first example of isoform-specific modulation of chemical sensitivity of TRPA1 channel in one species. α-terpineol showed repellent activity towards T. mercedesae in a laboratory assay and repressed T. mercedesae entry for reproduction into the brood cells with fifth instar larvae in hives. Thus, α-terpineol could be used as the potential compound to control two major honeybee ectoparasitic mites, T. mercedesae and Varroa destructor, in the apiculture industry

    DIP/WISH deficiency enhances synaptic function and performance in the Barnes maze

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    <p>Abstract</p> <p>Background</p> <p>DIP (diaphanous interacting protein)/WISH (WASP interacting SH3 protein) is a protein involved in cytoskeletal signaling which regulates actin cytoskeleton dynamics and/or microtubules mainly through the activity of Rho-related proteins. Although it is well established that: 1) spine-head volumes change dynamically and reflect the strength of the synapse accompanying long-term functional plasticity of glutamatergic synaptic transmission and 2) actin organization is critically involved in spine formation, the involvement of DIP/WISH in these processes is unknown.</p> <p>Results</p> <p>We found that DIP/WISH-deficient hippocampal CA1 neurons exhibit enhanced long-term potentiation via modulation of both pre- and post-synaptic events. Consistent with these electrophysiological findings, DIP/WISH-deficient mice, particularly at a relatively young age, found the escape hole more rapidly in the Barnes maze test.</p> <p>Conclusions</p> <p>We conclude that DIP/WISH deletion improves performance in the Barnes maze test in mice probably through increased hippocampal long-term potentiation.</p

    TRPA1 Channels in Drosophila and Honey Bee Ectoparasitic Mites Share Heat Sensitivity and Temperature-Related Physiological Functions

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    The transient receptor potential cation channel, subfamily A, member 1 (TRPA1) is conserved between many arthropods, and in some has been shown to function as a chemosensor for noxious compounds. Activation of arthropod TRPA1 channels by temperature fluctuations has been tested in only a few insect species, and all of them were shown to be activated by heat. The recent identification of chemosensitive TRPA1 channels from two honey bee ectoparasitic mite species (VdTRPA1 and TmTRPA1) have provided an opportunity to study the temperature-dependent activation and the temperature-associated physiological functions of TRPA1 channels in non-insect arthropods. We found that both mite TRPA1 channels are heat sensitive and capable of rescuing the temperature-related behavioral defects of a Drosophila melanogaster trpA1 mutant. These results suggest that heat-sensitivity of TRPA1 could be conserved between many arthropods despite its amino acid sequence diversity. Nevertheless, the ankyrin repeats (ARs) 6 and 7 are well-conserved between six heat-sensitive arthropod TRPA1 channels and have critical roles for the heat activation of VdTRPA1

    Embryonic thermosensitive TRPA1 determines transgenerational diapause phenotype of the silkworm, Bombyx mori

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    In the bivoltine strain of the silkworm, Bombyx mori, embryonic diapause is induced transgenerationally as a maternal effect. Progeny diapause is determined by the environmental temperature during embryonic development of the mother; however, its molecular mechanisms are largely unknown. Here, we show that the Bombyx TRPA1 ortholog (BmTrpA1) acts as a thermosensitive transient receptor potential (TRP) channel that is activated at temperatures above similar to 21 degrees C and affects the induction of diapause in progeny. In addition, we show that embryonic RNAi of BmTrpA1 affects diapause hormone release during pupal-adult development. This study identifying a thermosensitive TRP channel that acts as a molecular switch for a relatively long-term predictive adaptive response by inducing an alternative phenotype to seasonal polyphenism is unique.ArticlePROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 111(13):E1249-E1255 (2014)journal articl
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