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      Calcium signalling and related ion channels in neutrophil recruitment and function

      1 , 2 , 1
      European Journal of Clinical Investigation
      Wiley

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          Abstract

          <p class="first" id="P1">The recruitment of neutrophils to sites of inflammation, their battle against invading microorganisms through phagocytosis and the release of antimicrobial agents is a highly coordinated and tightly regulated process that involves the interplay of many different receptors, ion channels, and signaling pathways. Changes in intracellular calcium levels, caused by cytosolic Ca <sup>2+</sup> store depletion and the influx of extracellular Ca <sup>2+</sup> via ion channels play a critical role in synchronizing neutrophil activation and function. In this review, we provide an overview of how Ca <sup>2+</sup> signaling is initiated in neutrophils and how changes in intracellular Ca <sup>2+</sup> levels modulate neutrophil function. </p>

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          Most cited references75

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          How leukocytes cross the vascular endothelium.

          Immune responses depend on the ability of leukocytes to move from the circulation into tissue. This is enabled by mechanisms that guide leukocytes to the right exit sites and allow them to cross the barrier of the blood vessel wall. This process is regulated by a concerted action between endothelial cells and leukocytes, whereby endothelial cells activate leukocytes and direct them to extravasation sites, and leukocytes in turn instruct endothelial cells to open a path for transmigration. This Review focuses on recently described mechanisms that control and open exit routes for leukocytes through the endothelial barrier.
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            STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane.

            As the sole Ca2+ entry mechanism in a variety of non-excitable cells, store-operated calcium (SOC) influx is important in Ca2+ signalling and many other cellular processes. A calcium-release-activated calcium (CRAC) channel in T lymphocytes is the best-characterized SOC influx channel and is essential to the immune response, sustained activity of CRAC channels being required for gene expression and proliferation. The molecular identity and the gating mechanism of SOC and CRAC channels have remained elusive. Previously we identified Stim and the mammalian homologue STIM1 as essential components of CRAC channel activation in Drosophila S2 cells and human T lymphocytes. Here we show that the expression of EF-hand mutants of Stim or STIM1 activates CRAC channels constitutively without changing Ca2+ store content. By immunofluorescence, EM localization and surface biotinylation we show that STIM1 migrates from endoplasmic-reticulum-like sites to the plasma membrane upon depletion of the Ca2+ store. We propose that STIM1 functions as the missing link between Ca2+ store depletion and SOC influx, serving as a Ca2+ sensor that translocates upon store depletion to the plasma membrane to activate CRAC channels.
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              Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol.

              Eukaryotic cells respond to many hormones and neurotransmitters with increased activity of the enzyme phospholipase C and a subsequent rise in the concentration of intracellular free calcium ([Ca2+]i). The increase in [Ca2+]i occurs as a result of the release of Ca2+ from intracellular stores and an influx of Ca2+ through the plasma membrane; this influx of Ca2+ may or may not be store-dependent. Drosophila transient receptor potential (TRP) proteins and some mammalian homologues (TRPC proteins) are thought to mediate capacitative Ca2+ entry. Here we describe the molecular mechanism of store-depletion-independent activation of a subfamily of mammalian TRPC channels. We find that hTRPC6 is a non-selective cation channel that is activated by diacylglycerol in a membrane-delimited fashion, independently of protein kinases C activated by diacylglycerol. Although hTRPC3, the closest structural relative of hTRPC6, is activated in the same way, TRPCs 1, 4 and 5 and the vanilloid receptor subtype 1 are unresponsive to the lipid mediator. Thus, hTRPC3 and hTRPC6 represent the first members of a new functional family of second-messenger-operated cation channels, which are activated by diacylglycerol.
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                Author and article information

                Journal
                European Journal of Clinical Investigation
                Eur J Clin Invest
                Wiley
                00142972
                November 2018
                November 2018
                June 22 2018
                : 48
                : e12964
                Affiliations
                [1 ]Walter Brendel Centre of Experimental Medicine; Biomedical Center; Ludwig-Maximilians-Universität München; Munich Germany
                [2 ]Department of Biomedical Engineering; Graduate Group in Immunology; University of California; Davis CA USA
                Article
                10.1111/eci.12964
                6221920
                29873837
                2ba63190-39ba-47cb-a062-831568e99a40
                © 2018

                http://doi.wiley.com/10.1002/tdm_license_1.1

                http://onlinelibrary.wiley.com/termsAndConditions#vor

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