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Cells
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Advances in Dissecting Calcium Signaling Pathways in Health and Diseases
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Advances in Dissecting Calcium Signaling Pathways in Health and Diseases

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

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 5956

Special Issue Editors

Prof. Dr. Yubin Zhou

E-Mail Website
Guest Editor
Institute of Biosciences and Technology, Texas A&M University, Houston, TX 77030, USA
Interests: optogenetics; synthetic biology; immunotherapy; calcium signaling; molecular and cellular engineering; epigenetics
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Youjun Wang

E-Mail Website
Guest Editor
Beijing Key Laboratory of Gene Resource and Molecular Development, College of Life Sciences, Beijing Normal University, Beijing 100875, China
Interests: Ca2+ signaling

Special Issue Information

Dear Colleagues,

Calcium is considered “a signal for life and death”, and the tightly regulated spatiotemporal dynamics of calcium ions are essential for the proper function of mammalian cells and tissues; these range from short-term responses such as synaptic transmission, the heartbeat, and muscle contraction to long-term biological events including gene expression, cell migration, the immune response, and development. Imbalanced calcium hemostasis may lead to pathological conditions and even diseases, including neurological disorders, immunodeficiencies, cancer, cardiac arrhythmia, hypertension, and stroke. This Special Issue, “Advances in Dissecting Calcium Signaling Pathways in Health and Diseases”, welcomes original findings or reviews covering calcium-related molecular tools, the dissection of calcium signaling pathways, the interrogation of calcium-modulated cellular functions, and diseases arising from aberrant calcium signaling. We encourage leading investigators across all disciplines to share their latest work on developments in calcium signaling-related topics.

Prof. Dr. Yubin Zhou
Prof. Dr. Youjun Wang
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Cells is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • calcium signaling
  • ion channel
  • signal transduction
  • organellar Ca2+ channels
  • membrane contact site
  • store-operated calcium channel (SOC)
  • voltage-gated calcium channel (VOC)
  • transient receptor potential (TRP) channel

Published Papers (6 papers)

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Research

21 pages, 4641 KiB  
Article
Agonist-Induced Ca2+ Signaling in HEK-293-Derived Cells Expressing a Single IP3 Receptor Isoform
by Ekaterina N. Kochkina, Elizaveta E. Kopylova, Olga A. Rogachevskaja, Nina P. Kovalenko, Natalia V. Kabanova, Polina D. Kotova, Marina F. Bystrova and Stanislav S. Kolesnikov
Cells 2024, 13(7), 562; https://doi.org/10.3390/cells13070562 - 22 Mar 2024
Viewed by 621
Abstract
In mammals, three genes encode IP3 receptors (IP3Rs), which are involved in agonist-induced Ca2+ signaling in cells of apparently all types. Using the CRISPR/Cas9 approach for disruption of two out of three IP3R genes in HEK-293 cells, [...] Read more.
In mammals, three genes encode IP3 receptors (IP3Rs), which are involved in agonist-induced Ca2+ signaling in cells of apparently all types. Using the CRISPR/Cas9 approach for disruption of two out of three IP3R genes in HEK-293 cells, we generated three monoclonal cell lines, IP3R1-HEK, IP3R2-HEK, and IP3R3-HEK, with the single functional isoform, IP3R1, IP3R2, and IP3R3, respectively. All engineered cells responded to ACh with Ca2+ transients in an “all-or-nothing” manner, suggesting that each IP3R isotype was capable of mediating CICR. The sensitivity of cells to ACh strongly correlated with the affinity of IP3 binding to an IP3R isoform they expressed. Based on a mathematical model of intracellular Ca2+ signals induced by thapsigargin, a SERCA inhibitor, we developed an approach for estimating relative Ca2+ permeability of Ca2+ store and showed that all three IP3R isoforms contributed to Ca2+ leakage from ER. The relative Ca2+ permeabilities of Ca2+ stores in IP3R1-HEK, IP3R2-HEK, and IP3R3-HEK cells were evaluated as 1:1.75:0.45. Using the genetically encoded sensor R-CEPIA1er for monitoring Ca2+ signals in ER, engineered cells were ranged by resting levels of stored Ca2+ as IP3R3-HEK ≥ IP3R1-HEK > IP3R2-HEK. The developed cell lines could be helpful for further assaying activity, regulation, and pharmacology of individual IP3R isoforms. Full article
(This article belongs to the Special Issue Advances in Dissecting Calcium Signaling Pathways in Health and Diseases)
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27 pages, 6529 KiB  
Article
Piezo1 Is Required for Myoblast Migration and Involves Polarized Clustering in Association with Cholesterol and GM1 Ganglioside
by Juliette Vanderroost, Thibaud Parpaite, Noémie Avalosse, Patrick Henriet, Christophe E. Pierreux, Joseph H. Lorent, Philippe Gailly and Donatienne Tyteca
Cells 2023, 12(24), 2784; https://doi.org/10.3390/cells12242784 - 07 Dec 2023
Cited by 1 | Viewed by 1174
Abstract
A specific plasma membrane distribution of the mechanosensitive ion channel Piezo1 is required for cell migration, but the mechanism remains elusive. Here, we addressed this question using WT and Piezo1-silenced C2C12 mouse myoblasts and WT and Piezo1-KO human kidney HEK293T cells. [...] Read more.
A specific plasma membrane distribution of the mechanosensitive ion channel Piezo1 is required for cell migration, but the mechanism remains elusive. Here, we addressed this question using WT and Piezo1-silenced C2C12 mouse myoblasts and WT and Piezo1-KO human kidney HEK293T cells. We showed that cell migration in a cell-free area and through a porous membrane decreased upon Piezo1 silencing or deletion, but increased upon Piezo1 activation by Yoda1, whereas migration towards a chemoattractant gradient was reduced by Yoda1. Piezo1 organized into clusters, which were preferentially enriched at the front. This polarization was stimulated by Yoda1, accompanied by Ca2+ polarization, and abrogated by partial cholesterol depletion. Piezo1 clusters partially colocalized with cholesterol- and GM1 ganglioside-enriched domains, the proportion of which was increased by Yoda1. Mechanistically, Piezo1 activation induced a differential mobile fraction of GM1 associated with domains and the bulk membrane. Conversely, cholesterol depletion abrogated the differential mobile fraction of Piezo1 associated with clusters and the bulk membrane. In conclusion, we revealed, for the first time, the differential implication of Piezo1 depending on the migration mode and the interplay between GM1/cholesterol-enriched domains at the front during migration in a cell-free area. These domains could provide the optimal biophysical properties for Piezo1 activity and/or spatial dissociation from the PMCA calcium efflux pump. Full article
(This article belongs to the Special Issue Advances in Dissecting Calcium Signaling Pathways in Health and Diseases)
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Graphical abstract

19 pages, 3262 KiB  
Article
Store-Operated Calcium Entry Increases Nuclear Calcium in Adult Rat Atrial and Ventricular Cardiomyocytes
by Julia Hermes, Vesela Borisova and Jens Kockskämper
Cells 2023, 12(23), 2690; https://doi.org/10.3390/cells12232690 - 23 Nov 2023
Viewed by 879
Abstract
Store-operated calcium entry (SOCE) in cardiomyocytes may be involved in cardiac remodeling, but the underlying mechanisms remain elusive. We hypothesized that SOCE may increase nuclear calcium, which alters gene expression via calcium/calmodulin-dependent enzyme signaling, and elucidated the underlying cellular mechanisms. An experimental protocol [...] Read more.
Store-operated calcium entry (SOCE) in cardiomyocytes may be involved in cardiac remodeling, but the underlying mechanisms remain elusive. We hypothesized that SOCE may increase nuclear calcium, which alters gene expression via calcium/calmodulin-dependent enzyme signaling, and elucidated the underlying cellular mechanisms. An experimental protocol was established in isolated adult rat cardiomyocytes to elicit SOCE by re-addition of calcium following complete depletion of sarcoplasmic reticulum (SR) calcium and to quantify SOCE in relation to the electrically stimulated calcium transient (CaT) measured in the same cell before SR depletion. Using confocal imaging, calcium changes were recorded simultaneously in the cytosol and in the nucleus of the cell. In ventricular myocytes, SOCE was observed in the cytosol and nucleus amounting to ≈15% and ≈25% of the respective CaT. There was a linear correlation between the SOCE-mediated calcium increase in the cytosol and nucleus. Inhibitors of TRPC or Orai channels reduced SOCE by ≈33–67%, whereas detubulation did not. In atrial myocytes, SOCE with similar characteristics was observed in the cytosol and nucleus. However, the SOCE amplitudes in atrial myocytes were ≈two-fold larger than in ventricular myocytes, and this was associated with ≈1.4- to 3.6-fold larger expression of putative SOCE proteins (TRPC1, 3, 6, and STIM1) in atrial tissue. The results indicated that SOCE in atrial and ventricular myocytes is able to cause robust calcium increases in the nucleus and that both TRPC and Orai channels may contribute to SOCE in adult cardiomyocytes. Full article
(This article belongs to the Special Issue Advances in Dissecting Calcium Signaling Pathways in Health and Diseases)
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19 pages, 3271 KiB  
Article
The Impact of Ca2+ on Intracellular Distribution of Hemoglobin in Human Erythrocytes
by Leonid Livshits, Sari Peretz, Anna Bogdanova, Hiba Zoabi, Harel Eitam, Gregory Barshtein, Cindy Galindo, Yuri Feldman, Ivana Pajić-Lijaković, Ariel Koren, Max Gassmann and Carina Levin
Cells 2023, 12(18), 2280; https://doi.org/10.3390/cells12182280 - 15 Sep 2023
Cited by 1 | Viewed by 882
Abstract
The membrane-bound hemoglobin (Hb) fraction impacts red blood cell (RBC) rheology and metabolism. Therefore, Hb–RBC membrane interactions are precisely controlled. For instance, the signaling function of membrane-bound deoxy-Hb and the structure of the docking sites in the cytosolic domain of the anion exchanger [...] Read more.
The membrane-bound hemoglobin (Hb) fraction impacts red blood cell (RBC) rheology and metabolism. Therefore, Hb–RBC membrane interactions are precisely controlled. For instance, the signaling function of membrane-bound deoxy-Hb and the structure of the docking sites in the cytosolic domain of the anion exchanger 1 (AE-1) protein are well documented; however, much less is known about the interaction of Hb variants with the erythrocyte’s membrane. Here, we identified factors other than O2 availability that control Hb abundance in the membrane-bound fraction and the possible variant-specific binding selectivity of Hb to the membrane. We show that depletion of extracellular Ca2+ by chelators, or its omission from the extracellular medium, leads to membrane-bound Hb release into the cytosol. The removal of extracellular Ca2+ further triggers the redistribution of HbA0 and HbA2 variants between the membrane and the cytosol in favor of membrane-bound HbA2. Both effects are reversible and are no longer observed upon reintroduction of Ca2+ into the extracellular medium. Fluctuations of cytosolic Ca2+ also impact the pre-membrane Hb pool, resulting in the massive transfer of Hb to the cellular cytosol. We hypothesize that AE-1 is the specific membrane target and discuss the physiological outcomes and possible clinical implications of the Ca2+ regulation of the intracellular Hb distribution. Full article
(This article belongs to the Special Issue Advances in Dissecting Calcium Signaling Pathways in Health and Diseases)
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17 pages, 5214 KiB  
Article
Unveiling the Role of Cholesterol in Subnanomolar Ouabain Rescue of Cortical Neurons from Calcium Overload Caused by Excitotoxic Insults
by Dmitry A. Sibarov, Zoia D. Zhuravleva, Margarita A. Ilina, Sergei I. Boikov, Yulia D. Stepanenko, Tatiana V. Karelina and Sergei M. Antonov
Cells 2023, 12(15), 2011; https://doi.org/10.3390/cells12152011 - 06 Aug 2023
Viewed by 1020
Abstract
Na/K-ATPase maintains transmembrane ionic gradients and acts as a signal transducer when bound to endogenous cardiotonic steroids. At subnanomolar concentrations, ouabain induces neuroprotection against calcium overload and apoptosis of neurons during excitotoxic stress. Here, the role of lipid rafts in interactions between Na/K-ATPase, [...] Read more.
Na/K-ATPase maintains transmembrane ionic gradients and acts as a signal transducer when bound to endogenous cardiotonic steroids. At subnanomolar concentrations, ouabain induces neuroprotection against calcium overload and apoptosis of neurons during excitotoxic stress. Here, the role of lipid rafts in interactions between Na/K-ATPase, sodium–calcium exchanger (NCX), and N-methy-D-aspartate receptors (NMDARs) was investigated. We analyzed 0.5–1-nanometer ouabain’s effects on calcium responses and miniature post-synaptic current (mEPSCs) frequencies of cortical neurons during the action of NMDA in rat primary culture and brain slices. In both objects, ouabain attenuated NMDA-evoked calcium responses and prevented an increase in mEPSC frequency, while the cholesterol extraction by methyl-β-cyclodextrin prevented the effects. The data support the conclusions that (i) ouabain-induced inhibition of NMDA-elicited calcium response involves both pre- and post-synapse, (ii) the presence of astrocytes in the tripartite synapse is not critical for the ouabain effects, which are found to be similar in cell cultures and brain slices, and (iii) ouabain action requires the integrity of cholesterol-rich membrane microdomains in which the colocalization and functional interaction of NMDAR-transferred calcium influx, calcium extrusion by NCX, and Na/K-ATPase modulation of the exchanger occur. This regulation of the molecules by cardiotonic steroids may influence synaptic transmission, prevent excitotoxic neuronal death, and interfere with the pharmacological actions of neurological medicines. Full article
(This article belongs to the Special Issue Advances in Dissecting Calcium Signaling Pathways in Health and Diseases)
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10 pages, 2786 KiB  
Communication
Ca2+-Driven Selectivity of the Effect of the Cardiotonic Steroid Marinobufagenin on Rabbit Sinoatrial Node Function
by Sofia Segal and Yael Yaniv
Cells 2023, 12(14), 1881; https://doi.org/10.3390/cells12141881 - 18 Jul 2023
Viewed by 881
Abstract
The synergy between Na+-K+ pumps, Na+-Ca2+ exchangers, membrane currents and the sarcoplasmic reticulum (SR) generates the coupled-clock system, which governs the spontaneous electrical activity of heart sinoatrial node cells (SANCs). Ca2+ mediates the degree of clock [...] Read more.
The synergy between Na+-K+ pumps, Na+-Ca2+ exchangers, membrane currents and the sarcoplasmic reticulum (SR) generates the coupled-clock system, which governs the spontaneous electrical activity of heart sinoatrial node cells (SANCs). Ca2+ mediates the degree of clock coupling via local Ca2+ release (LCR) from the SR and activation of cAMP/PKA signaling. Marinobufagenin (MBG) is a natural Na+-K+ pump inhibitor whose effect on SANCs has not been measured before. The following two hypotheses were tested to determine if and how MBG mediates between the Na+-K+ pump and spontaneous SAN activity: (i) MBG has a distinct effect on beat interval (BI) due to variable effects on LCR characteristics, and (ii) Ca2+ is an important mediator between MBG and SANC activity. Ca2+ transients were measured by confocal microscopy during application of increasing concentrations of MBG. To further support the hypothesis that Ca2+ mediates between MBG and SANC activity, Ca2+ was chelated by the addition of BAPTA. Dose response tests found that 100 nM MBG led to no change in BI in 6 SANCs (no BI change group), and to BI prolongation in 10 SANCs (BI change group). At the same concentration, the LCR period was prolonged in both groups, but more significantly in the BI change group. BAPTA-AM prolonged the BI in 12 SANCs. In the presence of BAPTA, 100 nM MBG had no effect on SANC BI or on the LCR period. In conclusion, the MBG effects on SANC function are mediated by the coupled clock system, and Ca2+ is an important regulator of these effects. Full article
(This article belongs to the Special Issue Advances in Dissecting Calcium Signaling Pathways in Health and Diseases)
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