ijms-logo

Journal Browser

Journal Browser

Calcium Channels and Calcium-Binding Proteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 November 2022) | Viewed by 19797

Special Issue Editor


E-Mail Website
Guest Editor
Department of Physiology, Tokyo Medical University, 1-1 Shinjuku-6-chome, Shinju-ku, Tokyo 160-8402, Japan
Interests: synaptic transmission; presynaptic terminals; neurotransmitter release; presynaptic calcium channels; presynaptic proteins; calcium-binding proteins

Special Issue Information

Dear Colleagues,

Signal of nerve impulses are transmitted to excitatory cells to induce action of organs via activation of Ca2+ entry through voltage-gated Ca2+ channels, which are classified based on their activation threshold into high- and low-voltage activated channels, expressed specifically for each organ. Ca2+ entered into excitatory cells binds to Ca2+-binding proteins which are classified into two groups of Ca2+ sensors, C2 domain and EF hand proteins. Within transient Ca2+ elevation, each Ca2+ sensor, having different affinity and binding speed to Ca2+, determines the timing of protein–protein interactions to produce the specific action of each organ. This Special Issue will focus on investigations ranging from the control of Ca2+ entry at the plasma membrane of excitatory cells to detailed studies of the intracellular mediation of Ca2+-binding proteins that catalyze the organ-specific action.

Prof. Dr. Sumiko Mochida
Guest Editor

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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • voltage-gated Ca2+ channels
  • Ca2+-binding proteins
  • Ca2+ sensors
  • C2 domain proteins
  • EF hand proteins

Published Papers (8 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Editorial

Jump to: Research, Review

8 pages, 1056 KiB  
Editorial
Calcium Channels and Calcium-Binding Proteins
by Sumiko Mochida
Int. J. Mol. Sci. 2023, 24(18), 14257; https://doi.org/10.3390/ijms241814257 - 19 Sep 2023
Viewed by 857
Abstract
Signals of nerve impulses are transmitted to excitatory cells to induce the action of organs via the activation of Ca2+ entry through voltage-gated Ca2+ channels (VGCC), which are classified based on their activation threshold into high- and low-voltage activated channels, expressed [...] Read more.
Signals of nerve impulses are transmitted to excitatory cells to induce the action of organs via the activation of Ca2+ entry through voltage-gated Ca2+ channels (VGCC), which are classified based on their activation threshold into high- and low-voltage activated channels, expressed specifically for each organ [...] Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

Research

Jump to: Editorial, Review

16 pages, 2537 KiB  
Article
Glutamate-Evoked Ca2+ Responses in the Rat Suprachiasmatic Nucleus: Involvement of Na+/K+-ATPase and Na+/Ca2+-Exchanger
by Pi-Cheng Cheng, Ruo-Ciao Cheng and Rong-Chi Huang
Int. J. Mol. Sci. 2023, 24(7), 6444; https://doi.org/10.3390/ijms24076444 - 29 Mar 2023
Cited by 3 | Viewed by 968
Abstract
Glutamate mediates photic entrainment of the central clock in the suprachiasmatic nucleus (SCN) by evoking intracellular Ca2+ signaling mechanisms. However, the detailed mechanisms of glutamate-evoked Ca2+ signals are not entirely clear. Here, we used a ratiometric Ca2+ and Na+ [...] Read more.
Glutamate mediates photic entrainment of the central clock in the suprachiasmatic nucleus (SCN) by evoking intracellular Ca2+ signaling mechanisms. However, the detailed mechanisms of glutamate-evoked Ca2+ signals are not entirely clear. Here, we used a ratiometric Ca2+ and Na+ imaging technique to investigate glutamate-evoked Ca2+ responses. The comparison of Ca2+ responses to glutamate (100 μM) and high (20 mM) K+ solution indicated slower Ca2+ clearance, along with rebound Ca2+ suppression for glutamate-evoked Ca2+ transients. Increasing the length of exposure time in glutamate, but not in 20 mM K+, slowed Ca2+ clearance and increased rebound Ca2+ suppression, a result correlated with glutamate-induced Na+ loads. The rebound Ca2+ suppression was abolished by ouabain, monensin, Na+-free solution, or nimodipine, suggesting an origin of activated Na+/K+-ATPase (NKA) by glutamate-induced Na+ loads. Ouabain or Na+-free solution also slowed Ca2+ clearance, apparently by retarding Na+/Ca2+-exchanger (NCX)-mediated Ca2+ extrusion. Together, our results indicated the involvement of glutamate-induced Na+ loads, NKA, and NCX in shaping the Ca2+ response to glutamate. Nevertheless, in the absence of external Na+ (NMDG substituted), Ca2+ clearance was still slower for the Ca2+ response to glutamate than for 20 mM K+, suggesting participation of additional Ca2+ handlers to the slower Ca2+ clearance under this condition. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

20 pages, 5862 KiB  
Article
Spatial and Functional Crosstalk between the Mitochondrial Na+-Ca2+ Exchanger NCLX and the Sarcoplasmic Reticulum Ca2+ Pump SERCA in Cardiomyocytes
by Ayako Takeuchi and Satoshi Matsuoka
Int. J. Mol. Sci. 2022, 23(14), 7948; https://doi.org/10.3390/ijms23147948 - 19 Jul 2022
Cited by 6 | Viewed by 2435
Abstract
The mitochondrial Na+-Ca2+ exchanger, NCLX, was reported to supply Ca2+ to sarcoplasmic reticulum (SR)/endoplasmic reticulum, thereby modulating various cellular functions such as the rhythmicity of cardiomyocytes, and cellular Ca2+ signaling upon antigen receptor stimulation and chemotaxis in B [...] Read more.
The mitochondrial Na+-Ca2+ exchanger, NCLX, was reported to supply Ca2+ to sarcoplasmic reticulum (SR)/endoplasmic reticulum, thereby modulating various cellular functions such as the rhythmicity of cardiomyocytes, and cellular Ca2+ signaling upon antigen receptor stimulation and chemotaxis in B lymphocytes; however, there is little information on the spatial relationships of NCLX with SR Ca2+ handling proteins, and their physiological impact. Here we examined the issue, focusing on the interaction of NCLX with an SR Ca2+ pump SERCA in cardiomyocytes. A bimolecular fluorescence complementation assay using HEK293 cells revealed that the exogenously expressed NCLX was localized in close proximity to four exogenously expressed SERCA isoforms. Immunofluorescence analyses of isolated ventricular myocytes showed that the NCLX was localized to the edges of the mitochondria, forming a striped pattern. The co-localization coefficients in the super-resolution images were higher for NCLX–SERCA2, than for NCLX–ryanodine receptor and NCLX–Na+/K+ ATPase α-1 subunit, confirming the close localization of endogenous NCLX and SERCA2 in cardiomyocytes. The mathematical model implemented with the spatial and functional coupling of NCLX and SERCA well reproduced the NCLX inhibition-mediated modulations of SR Ca2+ reuptake in HL-1 cardiomyocytes. Taken together, these results indicated that NCLX and SERCA are spatially and functionally coupled in cardiomyocytes. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

13 pages, 2516 KiB  
Article
STIM1 Controls the Focal Adhesion Dynamics and Cell Migration by Regulating SOCE in Osteosarcoma
by Yu-Shan Lin, Yi-Hsin Lin, MyHang Nguyen Thi, Shih-Chuan Hsiao and Wen-Tai Chiu
Int. J. Mol. Sci. 2022, 23(1), 162; https://doi.org/10.3390/ijms23010162 - 23 Dec 2021
Cited by 5 | Viewed by 2899
Abstract
The dysregulation of store-operated Ca2+ entry (SOCE) promotes cancer progression by changing Ca2+ levels in the cytosol or endoplasmic reticulum. Stromal interaction molecule 1 (STIM1), a component of SOCE, is upregulated in several types of cancer and responsible for cancer cell [...] Read more.
The dysregulation of store-operated Ca2+ entry (SOCE) promotes cancer progression by changing Ca2+ levels in the cytosol or endoplasmic reticulum. Stromal interaction molecule 1 (STIM1), a component of SOCE, is upregulated in several types of cancer and responsible for cancer cell migration, invasion, and metastasis. To explore the impact of STIM1-mediated SOCE on the turnover of focal adhesion (FA) and cell migration, we overexpressed the wild-type and constitutively active or dominant negative variants of STIM1 in an osteosarcoma cell line. In this study, we hypothesized that STIM1-mediated Ca2+ elevation may increase cell migration. We found that constitutively active STIM1 dramatically increased the Ca2+ influx, calpain activity, and turnover of FA proteins, such as the focal adhesion kinase (FAK), paxillin, and vinculin, which impede the cell migration ability. In contrast, dominant negative STIM1 decreased the turnover of FA proteins as its wild-type variant compared to the cells without STIM1 overexpression while promoting cell migration. These unexpected results suggest that cancer cells need an appropriate amount of Ca2+ to control the assembly and disassembly of focal adhesions by regulating calpain activity. On the other hand, overloaded Ca2+ results in excessive calpain activity, which is not beneficial for cancer metastasis. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

13 pages, 3043 KiB  
Article
Age-Dependent Contributions of NMDA Receptors and L-Type Calcium Channels to Long-Term Depression in the Piriform Cortex
by Vishaal Rajani, Aida Maziar, Kwun Nok Mimi Man, Johannes W. Hell and Qi Yuan
Int. J. Mol. Sci. 2021, 22(24), 13551; https://doi.org/10.3390/ijms222413551 - 17 Dec 2021
Cited by 8 | Viewed by 2677
Abstract
In the hippocampus, the contributions of N-methyl-D-aspartate receptors (NMDARs) and L-type calcium channels (LTCCs) to neuronal transmission and synaptic plasticity change with aging, underlying calcium dysregulation and cognitive dysfunction. However, the relative contributions of NMDARs and LTCCs in other learning encoding structures during [...] Read more.
In the hippocampus, the contributions of N-methyl-D-aspartate receptors (NMDARs) and L-type calcium channels (LTCCs) to neuronal transmission and synaptic plasticity change with aging, underlying calcium dysregulation and cognitive dysfunction. However, the relative contributions of NMDARs and LTCCs in other learning encoding structures during aging are not known. The piriform cortex (PC) plays a significant role in odor associative memories, and like the hippocampus, exhibits forms of long-term synaptic plasticity. Here, we investigated the expression and contribution of NMDARs and LTCCs in long-term depression (LTD) of the PC associational fiber pathway in three cohorts of Sprague Dawley rats: neonatal (1–2 weeks), young adult (2–3 months) and aged (20–25 months). Using a combination of slice electrophysiology, Western blotting, fluorescent immunohistochemistry and confocal imaging, we observed a shift from an NMDAR to LTCC mediation of LTD in aged rats, despite no difference in the amount of LTD expression. These changes in plasticity are related to age-dependent differential receptor expression in the PC. LTCC Cav1.2 expression relative to postsynaptic density protein 95 is increased in the associational pathway of the aged PC layer Ib. Enhanced LTCC contribution in synaptic depression in the PC may contribute to altered olfactory function and learning with aging. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Graphical abstract

Review

Jump to: Editorial, Research

28 pages, 2136 KiB  
Review
Regulation of Cardiac Cav1.2 Channels by Calmodulin
by Masaki Kameyama, Etsuko Minobe, Dongxue Shao, Jianjun Xu, Qinghua Gao and Liying Hao
Int. J. Mol. Sci. 2023, 24(7), 6409; https://doi.org/10.3390/ijms24076409 - 29 Mar 2023
Cited by 3 | Viewed by 2288
Abstract
Cav1.2 Ca2+ channels, a type of voltage-gated L-type Ca2+ channel, are ubiquitously expressed, and the predominant Ca2+ channel type, in working cardiac myocytes. Cav1.2 channels are regulated by the direct interactions with calmodulin (CaM), a Ca2+-binding protein that [...] Read more.
Cav1.2 Ca2+ channels, a type of voltage-gated L-type Ca2+ channel, are ubiquitously expressed, and the predominant Ca2+ channel type, in working cardiac myocytes. Cav1.2 channels are regulated by the direct interactions with calmodulin (CaM), a Ca2+-binding protein that causes Ca2+-dependent facilitation (CDF) and inactivation (CDI). Ca2+-free CaM (apoCaM) also contributes to the regulation of Cav1.2 channels. Furthermore, CaM indirectly affects channel activity by activating CaM-dependent enzymes, such as CaM-dependent protein kinase II and calcineurin (a CaM-dependent protein phosphatase). In this article, we review the recent progress in identifying the role of apoCaM in the channel ‘rundown’ phenomena and related repriming of channels, and CDF, as well as the role of Ca2+/CaM in CDI. In addition, the role of CaM in channel clustering is reviewed. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

15 pages, 4633 KiB  
Review
The Thermodynamically Expensive Contribution of Three Calcium Sources to Somatic Release of Serotonin
by Francisco F. De-Miguel
Int. J. Mol. Sci. 2022, 23(3), 1495; https://doi.org/10.3390/ijms23031495 - 28 Jan 2022
Cited by 1 | Viewed by 1955
Abstract
The soma, dendrites and axon of neurons may display calcium-dependent release of transmitters and peptides. Such release is named extrasynaptic for occurring in absence of synaptic structures. This review describes the cooperative actions of three calcium sources on somatic exocytosis. Emphasis is given [...] Read more.
The soma, dendrites and axon of neurons may display calcium-dependent release of transmitters and peptides. Such release is named extrasynaptic for occurring in absence of synaptic structures. This review describes the cooperative actions of three calcium sources on somatic exocytosis. Emphasis is given to the somatic release of serotonin by the classical leech Retzius neuron, which has allowed detailed studies on the fine steps from excitation to exocytosis. Trains of action potentials induce transmembrane calcium entry through L-type channels. For action potential frequencies above 5 Hz, summation of calcium transients on individual action potentials activates the second calcium source: ryanodine receptors produce calcium-induced calcium release. The resulting calcium tsunami activates mitochondrial ATP synthesis to fuel transport of vesicles to the plasma membrane. Serotonin that is released maintains a large-scale exocytosis by activating the third calcium source: serotonin autoreceptors coupled to phospholipase C promote IP3 production. Activated IP3 receptors in peripheral endoplasmic reticulum release calcium that promotes vesicle fusion. The Swiss-clock workings of the machinery for somatic exocytosis has a striking disadvantage. The essential calcium-releasing endoplasmic reticulum near the plasma membrane hinders the vesicle transport, drastically reducing the thermodynamic efficiency of the ATP expenses and elevating the energy cost of release. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

27 pages, 2384 KiB  
Review
Systematic Review of Calcium Channels and Intracellular Calcium Signaling: Relevance to Pesticide Neurotoxicity
by Carmen Costas-Ferreira and Lilian R. F. Faro
Int. J. Mol. Sci. 2021, 22(24), 13376; https://doi.org/10.3390/ijms222413376 - 13 Dec 2021
Cited by 12 | Viewed by 4909
Abstract
Pesticides of different chemical classes exert their toxic effects on the nervous system by acting on the different regulatory mechanisms of calcium (Ca2+) homeostasis. Pesticides have been shown to alter Ca2+ homeostasis, mainly by increasing its intracellular concentration above physiological [...] Read more.
Pesticides of different chemical classes exert their toxic effects on the nervous system by acting on the different regulatory mechanisms of calcium (Ca2+) homeostasis. Pesticides have been shown to alter Ca2+ homeostasis, mainly by increasing its intracellular concentration above physiological levels. The pesticide-induced Ca2+ overload occurs through two main mechanisms: the entry of Ca2+ from the extracellular medium through the different types of Ca2+ channels present in the plasma membrane or its release into the cytoplasm from intracellular stocks, mainly from the endoplasmic reticulum. It has also been observed that intracellular increases in the Ca2+ concentrations are maintained over time, because pesticides inhibit the enzymes involved in reducing its levels. Thus, the alteration of Ca2+ levels can lead to the activation of various signaling pathways that generate oxidative stress, neuroinflammation and, finally, neuronal death. In this review, we also discuss some proposed strategies to counteract the detrimental effects of pesticides on Ca2+ homeostasis. Full article
(This article belongs to the Special Issue Calcium Channels and Calcium-Binding Proteins)
Show Figures

Figure 1

Back to TopTop