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Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to...
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Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Signaling".

Deadline for manuscript submissions: closed (15 June 2023) | Viewed by 22589

Special Issue Editor

Dr. Dmitry Lim

E-Mail Website
Guest Editor
Department of Pharmaceutical Science, University of Piemonte Orientale, 28100 Novara, Italy
Interests: calcium signaling; astrocytes; calcineurin; Alzheimer’s disease
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The calcium ion (Ca2+) is the most versatile and the most evolutionarily conserved signaling molecule, from bacteria and algae to invertebrates and mammals. The unique repertoire of receptors, channels, pumps, transporters and proteins that are involved in creating, sensing and decoding intracellular Ca2+ signals across the phylogenetic tree has been largely exploited to understand their crucial role in human physiology and pathology. Spatio-temporal Ca2+ signals regulate virtually all cellular functions, ranging from fertilization and proliferation to exocytosis, contraction, metabolism, gene expression, and motility. Moreover, the modelling of human diseases in model species such as S. cerevisiae, C. elegans, D. melanogaster, Danio rerio, and a variety of transgenic mice allowed the elucidation of the pathogenic role of deranged Ca2+-handling machinery in human pathology. Finally, advances in molecular biology and protein chemistry led to the creation of chimeric molecular probes and organisms which made possible the detection and visualization of Ca2+ signaling processes in living plants and animals. The brightest example is the Nobel-Prize-winning green fluorescent protein from the jellyfish Aequorea victoria, and its analogues from coral Dictyostelium, which revolutionized the field of cell signaling including Ca2+.

This Special Issue is organized to provide a forum for all researchers and scholars whose activity is linked to the study of Ca2+ signaling and Ca2+-regulated processes in all organisms across the phylogenetic tree. We welcome original research articles, reviews, commentaries, opinions and experimental protocols on the physiology and pathology of Ca2+ signals, components of the Ca2+ signaling toolkit, Ca2+-regulated proteins and processes studied in the species populating the Earth. These include comparative studies and contributions regarding molecular and functional evolution of Ca2+ signaling components and Ca2+-binding proteins. We also welcome contributions which exploit the molecules from diverse species to the study of Ca2+ signaling in health and disease.

Dr. Dmitry Lim
Guest Editor

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Keywords

  • calcium signals
  • calcium homeostasis
  • calcium signaling
  • calcium-binding proteins
  • phylogenetic tree
  • animal models
  • calcium probes
  • calcium reporters
  • calcium in health and disease

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Published Papers (6 papers)

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Research

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22 pages, 3969 KiB  
Article
GABAA and GABAB Receptors Mediate GABA-Induced Intracellular Ca2+ Signals in Human Brain Microvascular Endothelial Cells
by Sharon Negri, Francesca Scolari, Mauro Vismara, Valentina Brunetti, Pawan Faris, Giulia Terribile, Giulio Sancini, Roberto Berra-Romani and Francesco Moccia
Cells 2022, 11(23), 3860; https://doi.org/10.3390/cells11233860 - 30 Nov 2022
Cited by 14 | Viewed by 4147
Abstract
Numerous studies recently showed that the inhibitory neurotransmitter, γ-aminobutyric acid (GABA), can stimulate cerebral angiogenesis and promote neurovascular coupling by activating the ionotropic GABAA receptors on cerebrovascular endothelial cells, whereas the endothelial role of the metabotropic GABAB receptors is still unknown. [...] Read more.
Numerous studies recently showed that the inhibitory neurotransmitter, γ-aminobutyric acid (GABA), can stimulate cerebral angiogenesis and promote neurovascular coupling by activating the ionotropic GABAA receptors on cerebrovascular endothelial cells, whereas the endothelial role of the metabotropic GABAB receptors is still unknown. Preliminary evidence showed that GABAA receptor stimulation can induce an increase in endothelial Ca2+ levels, but the underlying signaling pathway remains to be fully unraveled. In the present investigation, we found that GABA evoked a biphasic elevation in [Ca2+]i that was initiated by inositol-1,4,5-trisphosphate- and nicotinic acid adenine dinucleotide phosphate-dependent Ca2+ release from neutral and acidic Ca2+ stores, respectively, and sustained by store-operated Ca2+ entry. GABAA and GABAB receptors were both required to trigger the endothelial Ca2+ response. Unexpectedly, we found that the GABAA receptors signal in a flux-independent manner via the metabotropic GABAB receptors. Likewise, the full Ca2+ response to GABAB receptors requires functional GABAA receptors. This study, therefore, sheds novel light on the molecular mechanisms by which GABA controls endothelial signaling at the neurovascular unit. Full article
(This article belongs to the Special Issue Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms)
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19 pages, 2069 KiB  
Article
Platelet-Derived Extracellular Vesicles Stimulate Migration through Partial Remodelling of the Ca2+ Handling Machinery in MDA-MB-231 Breast Cancer Cells
by Mauro Vismara, Sharon Negri, Francesca Scolari, Valentina Brunetti, Silvia Maria Grazia Trivigno, Pawan Faris, Luca Galgano, Teresa Soda, Roberto Berra-Romani, Ilaria Canobbio, Mauro Torti, Gianni Francesco Guidetti and Francesco Moccia
Cells 2022, 11(19), 3120; https://doi.org/10.3390/cells11193120 - 4 Oct 2022
Cited by 10 | Viewed by 2845
Abstract
Background: Platelets can support cancer progression via the release of microparticles and microvesicles that enhance the migratory behaviour of recipient cancer cells. We recently showed that platelet-derived extracellular vesicles (PEVs) stimulate migration and invasiveness in highly metastatic MDA-MB-231 cells by stimulating the phosphorylation [...] Read more.
Background: Platelets can support cancer progression via the release of microparticles and microvesicles that enhance the migratory behaviour of recipient cancer cells. We recently showed that platelet-derived extracellular vesicles (PEVs) stimulate migration and invasiveness in highly metastatic MDA-MB-231 cells by stimulating the phosphorylation of p38 MAPK and the myosin light chain 2 (MLC2). Herein, we assessed whether the pro-migratory effect of PEVs involves the remodelling of the Ca2+ handling machinery, which drives MDA-MB-231 cell motility. Methods: PEVs were isolated from human blood platelets, and Fura-2/AM Ca2+ imaging, RT-qPCR, and immunoblotting were exploited to assess their effect on intracellular Ca2+ dynamics and Ca2+-dependent migratory processes in MDA-MB-231 cells. Results: Pretreating MDA-MB-231 cells with PEVs for 24 h caused an increase in Ca2+ release from the endoplasmic reticulum (ER) due to the up-regulation of SERCA2B and InsP3R1/InsP3R2 mRNAs and proteins. The consequent enhancement of ER Ca2+ depletion led to a significant increase in store-operated Ca2+ entry. The larger Ca2+ mobilization from the ER was required to potentiate serum-induced migration by recruiting p38 MAPK and MLC2. Conclusions: PEVs stimulate migration in the highly metastatic MDA-MB-231 breast cancer cell line by inducing a partial remodelling of the Ca2+ handling machinery. Full article
(This article belongs to the Special Issue Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms)
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19 pages, 7079 KiB  
Article
Species-Specific Gamete Interaction during Sea Urchin Fertilization: Roles of the Egg Jelly and Vitelline Layer
by Nunzia Limatola, Jong Tai Chun and Luigia Santella
Cells 2022, 11(19), 2984; https://doi.org/10.3390/cells11192984 - 24 Sep 2022
Cited by 5 | Viewed by 3513
Abstract
In sea urchins, the sequence of the cellular and molecular events characterizing the fertilization process has been intensively studied. We have learned that to activate the egg, the fertilizing sperm must undergo morphological modifications (the acrosome reaction, AR) upon reaching the outer gelatinous [...] Read more.
In sea urchins, the sequence of the cellular and molecular events characterizing the fertilization process has been intensively studied. We have learned that to activate the egg, the fertilizing sperm must undergo morphological modifications (the acrosome reaction, AR) upon reaching the outer gelatinous layer enveloping the egg (egg jelly), which triggers the polymerization of F-actin on the sperm head to form the acrosomal process. The AR exposes bindin, an adhesive sperm protein essential for the species-specific interaction with the cognate receptor on the egg vitelline layer. To investigate the specific roles of the egg jelly and vitelline layer at fertilization of sea urchin eggs, Paracentrotus lividus eggs were incubated in acidic seawater, which removes the egg jelly, i.e., experimental conditions that should prevent the occurrence of the AR, and inseminated in the same medium. At variance with the prevailing view, our results have shown that these dejellied P. lividus eggs can still interact with sperm in acidic seawater, albeit with altered fertilization responses. In particular, the eggs deprived of the vitelline layer reacted with multiple sperm but with altered Ca2+ signals. The results have provided experimental evidence that the plasma membrane, and not the vitelline layer, is where the specific recognition between gametes occurs. The vitelline layer works in unfertilized eggs to prevent polyspermy. Full article
(This article belongs to the Special Issue Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms)
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19 pages, 2880 KiB  
Article
Calcineurin Controls Cellular Prion Protein Expression in Mouse Astrocytes
by Giulia Dematteis, Elena Restelli, Virginia Vita Vanella, Marcello Manfredi, Emilio Marengo, Marco Corazzari, Armando A. Genazzani, Roberto Chiesa, Dmitry Lim and Laura Tapella
Cells 2022, 11(4), 609; https://doi.org/10.3390/cells11040609 - 10 Feb 2022
Cited by 5 | Viewed by 3467
Abstract
Prion diseases arise from the conformational conversion of the cellular prion protein (PrPC) into a self-replicating prion isoform (PrPSc). Although this process has been studied mostly in neurons, a growing body of evidence suggests that astrocytes express PrPC [...] Read more.
Prion diseases arise from the conformational conversion of the cellular prion protein (PrPC) into a self-replicating prion isoform (PrPSc). Although this process has been studied mostly in neurons, a growing body of evidence suggests that astrocytes express PrPC and are able to replicate and accumulate PrPSc. Currently, prion diseases remain incurable, while downregulation of PrPC represents the most promising therapy due to the reduction of the substrate for prion conversion. Here we show that the astrocyte-specific genetic ablation or pharmacological inhibition of the calcium-activated phosphatase calcineurin (CaN) reduces PrPC expression in astrocytes. Immunocytochemical analysis of cultured CaN-KO astrocytes and isolation of synaptosomal compartments from the hippocampi of astrocyte-specific CaN-KO (ACN-KO) mice suggest that PrPC is downregulated both in vitro and in vivo. The downregulation occurs without affecting the glycosylation of PrPC and without alteration of its proteasomal or lysosomal degradation. Direct assessment of the protein synthesis rate and shotgun mass spectrometry proteomics analysis suggest that the reduction of PrPC is related to the impairment of global protein synthesis in CaN-KO astrocytes. When WT-PrP and PrP-D177N, a mouse homologue of a human mutation associated with the inherited prion disease fatal familial insomnia, were expressed in astrocytes, CaN-KO astrocytes showed an aberrant localization of both WT-PrP and PrP-D177N variants with predominant localization to the Golgi apparatus, suggesting that ablation of CaN affects both WT and mutant PrP proteins. These results provide new mechanistic details in relation to the regulation of PrP expression in astrocytes, suggesting the therapeutic potential of astroglial cells. Full article
(This article belongs to the Special Issue Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms)
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16 pages, 4195 KiB  
Review
Calnexin, More Than Just a Molecular Chaperone
by Tautvydas Paskevicius, Rabih Abou Farraj, Marek Michalak and Luis B. Agellon
Cells 2023, 12(3), 403; https://doi.org/10.3390/cells12030403 - 24 Jan 2023
Cited by 17 | Viewed by 5023
Abstract
Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone involved in [...] Read more.
Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone involved in the folding and quality control of membrane-associated and secreted proteins, a function that is attributed to its ER- localized domain with a structure that bears a strong resemblance to another luminal ER chaperone and Ca2+-binding protein known as calreticulin. Studies have discovered that the cytosolic C-terminal domain of calnexin undergoes distinct post-translational modifications and interacts with a variety of proteins. Here, we discuss recent findings and hypothesize that the post-translational modifications of the calnexin C-terminal domain and its interaction with specific cytosolic proteins play a role in coordinating ER functions with events taking place in the cytosol and other cellular compartments. Full article
(This article belongs to the Special Issue Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms)
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12 pages, 1584 KiB  
Review
The Complex Journey of the Calcium Regulation Downstream of TAS2R Activation
by Maria Talmon, Federica Pollastro and Luigia Grazia Fresu
Cells 2022, 11(22), 3638; https://doi.org/10.3390/cells11223638 - 16 Nov 2022
Cited by 8 | Viewed by 2609
Abstract
Bitter taste receptors (TAS2Rs) have recently arisen as a potential drug target for asthma due to their localization in airway cells. These receptors are expressed in all cell types of the respiratory system comprising epithelial, smooth muscle and immune cells; however, the expression [...] Read more.
Bitter taste receptors (TAS2Rs) have recently arisen as a potential drug target for asthma due to their localization in airway cells. These receptors are expressed in all cell types of the respiratory system comprising epithelial, smooth muscle and immune cells; however, the expression pattern of the subtypes is different in each cell type and, accordingly, so is their role, for example, anti-inflammatory or bronchodilator. The most challenging aspect in studying TAS2Rs has been the identification of the downstream signaling cascades. Indeed, TAS2R activation leads to canonical IP3-dependent calcium release from the ER, but, alongside, there are other mechanisms that differ according to the histological localization. In this review, we summarize the current knowledge on the cytosolic calcium modulation downstream of TAS2R activation in the epithelial, smooth muscle and immune cells of the airway system. Full article
(This article belongs to the Special Issue Cell Calcium across the Phylogenetic Tree: From Physiological Signaling to Pathogenic Mechanisms)
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