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      The Different Facets of Extracellular Calcium Sensors: Old and New Concepts in Calcium-Sensing Receptor Signalling and Pharmacology

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          Abstract

          The current interest of the scientific community for research in the field of calcium sensing in general and on the calcium-sensing Receptor (CaR) in particular is demonstrated by the still increasing number of papers published on this topic. The extracellular calcium-sensing receptor is the best-known G-protein-coupled receptor (GPCR) able to sense external Ca 2+ changes. Widely recognized as a fundamental player in systemic Ca 2+ homeostasis, the CaR is ubiquitously expressed in the human body where it activates multiple signalling pathways. In this review, old and new notions regarding the mechanisms by which extracellular Ca 2+ microdomains are created and the tools available to measure them are analyzed. After a survey of the main signalling pathways triggered by the CaR, a special attention is reserved for the emerging concepts regarding CaR function in the heart, CaR trafficking and pharmacology. Finally, an overview on other Ca 2+ sensors is provided.

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          Cloning and characterization of an extracellular Ca(2+)-sensing receptor from bovine parathyroid.

          E M Brown, G Gamba, D. Riccardi … (1993)
          Maintenance of a stable internal environment within complex organisms requires specialized cells that sense changes in the extracellular concentration of specific ions (such as Ca2+). Although the molecular nature of such ion sensors is unknown, parathyroid cells possess a cell surface Ca(2+)-sensing mechanism that also recognizes trivalent and polyvalent cations (such as neomycin) and couples by changes in phosphoinositide turnover and cytosolic Ca2+ to regulation of parathyroid hormone secretion. The latter restores normocalcaemia by acting on kidney and bone. We now report the cloning of complementary DNA encoding an extracellular Ca(2+)-sensing receptor from bovine parathyroid with pharmacological and functional properties nearly identical to those of the native receptor. The novel approximately 120K receptor shares limited similarity with the metabotropic glutamate receptors and features a large extracellular domain, containing clusters of acidic amino-acid residues possibly involved in calcium binding, coupled to a seven-membrane-spanning domain like those in the G-protein-coupled receptor superfamily.
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            Cadherins in development: cell adhesion, sorting, and tissue morphogenesis.

            Jennifer Halbleib, W Nelson (2006)
            Tissue morphogenesis during development is dependent on activities of the cadherin family of cell-cell adhesion proteins that includes classical cadherins, protocadherins, and atypical cadherins (Fat, Dachsous, and Flamingo). The extracellular domain of cadherins contains characteristic repeats that regulate homophilic and heterophilic interactions during adhesion and cell sorting. Although cadherins may have originated to facilitate mechanical cell-cell adhesion, they have evolved to function in many other aspects of morphogenesis. These additional roles rely on cadherin interactions with a wide range of binding partners that modify their expression and adhesion activity by local regulation of the actin cytoskeleton and diverse signaling pathways. Here we examine how different members of the cadherin family act in different developmental contexts, and discuss the mechanisms involved.
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              Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor.

              N Kunishima, Y Shimada, Y Tsuji … (2000)
              The metabotropic glutamate receptors (mGluRs) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. Here we have determined three different crystal structures of the extracellular ligand-binding region of mGluR1--in a complex with glutamate and in two unliganded forms. They all showed disulphide-linked homodimers, whose 'active' and 'resting' conformations are modulated through the dimeric interface by a packed alpha-helical structure. The bi-lobed protomer architectures flexibly change their domain arrangements to form an 'open' or 'closed' conformation. The structures imply that glutamate binding stabilizes both the 'active' dimer and the 'closed' protomer in dynamic equilibrium. Movements of the four domains in the dimer are likely to affect the separation of the transmembrane and intracellular regions, and thereby activate the receptor. This scheme in the initial receptor activation could be applied generally to G-protein-coupled neurotransmitter receptors that possess extracellular ligand-binding sites.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Int J Mol Sci
                Journal ID (iso-abbrev): Int J Mol Sci
                Journal ID (publisher-id): ijms
                Title: International Journal of Molecular Sciences
                Publisher: MDPI
                ISSN (Electronic): 1422-0067
                Publication date (Electronic): 27 March 2018
                Publication date Collection: April 2018
                Volume: 19
                Issue: 4
                Electronic Location Identifier: 999
                Affiliations
                Department of Biosciences, Biotechnology and Biopharmaceutics, University of Bari, 70121 Bari, Italy
                Author notes
                [* ]Correspondence: andrea.gerbino@ 123456uniba.it (A.G.); matilde.colella@ 123456uniba.it (M.C.); Tel.: +39-080-544-3334 (A.G.); +39-080-544-3028 (M.C.)
                Author information
                https://orcid.org/0000-0002-2839-0130
                https://orcid.org/0000-0002-9584-7030
                Article
                Publisher ID: ijms-19-00999
                DOI: 10.3390/ijms19040999
                PMC ID: 5979557
                PubMed ID: 29584660
                SO-VID: b7b428b5-d39b-4fb5-94d0-2e8f275afc9f
                Copyright © © 2018 by the authors.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 02 March 2018
                Date accepted : 25 March 2018
                Categories
                Subject: Review

                ScienceOpen disciplines: Molecular biology
                Keywords: ca2+-signalling,microelectrode,fluorophore,exocytosis,camp signalling,parathyroid extracellular-ca2+-sensing receptor (car),cancer,apoptosis,ischemia/reperfusion,hypertrophy,heart,cardiomyocytes
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: ca2+-signalling, microelectrode, fluorophore, exocytosis, camp signalling, parathyroid extracellular-ca2+-sensing receptor (car), cancer, apoptosis, ischemia/reperfusion, hypertrophy, heart, cardiomyocytes

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