Role of store-operated Ca2+ entry in cardiovascular disease

Lu, Ting; Zhang, Yihua; Su, Yong; Zhou, Dayan; Xu, Qiang

doi:10.1186/s12964-022-00829-z

Cited by 16 publications

(16 citation statements)

References 105 publications

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“…Using the methods of molecular genetics and electrophysiology, it has been shown that many nervous and muscular disorders, including myopathies and periodic paralysis, are caused by dysfunctions of ion channels in the membrane. A study published in 2022 demonstrated the important role of the channel (So Cs) associated with several physiological roles in endothelial dysfunction and vascular smooth muscle proliferation, which contribute to the progression of cardiovascular diseases [22], diseases of the blood system [23]. The authors revealed a disturbed regulation of the main mechanosensory ion channel Piezo 1 in several blood lineages in the patients with type 2 diabetes mellitus (DM2).…”

Section: Electron Transport and Ion Channelsmentioning

confidence: 99%

Application of fluorescent potential-sensitive probes for the study of living blood and marrow cells

Parkhomenko¹,

Galibin²,

Tomson³

2023

CTT

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Usage of membrane potential-sensitive probes is of great importance for assessing both the viability and functional integrity of the cells and their structural components (mitochondria, nuclei, cytoplasmic membranes, ion channels). Potential advantage of this approach includes studies of native viable cells in order to assess functional state of donor hematopoietic cells before transplantation as well as upon their storage and cultivation. These staining tools allow to assess the state of cellular bioenergetics, i.e., the balance between production and consumption of energy in living cells. The production of energy in mitochondrial structures ensures the cell viability, whereas its impairment leads to the development of different disorders and aging. The purpose of this literature review is to demonstrate the opportunities of using potential-sensitive probes to assess the viability of blood system cells and to study the state of their energy potential.

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Section: Electron Transport and Ion Channelsmentioning

confidence: 99%

Application of fluorescent potential-sensitive probes for the study of living blood and marrow cells

Parkhomenko¹,

Galibin²,

Tomson³

2023

CTT

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“…In contrast, STIM1 and Orai1 gain-of-function mutations were found in patients with tubular aggregate myopathy and Stormorken syndrome (STRMK) ( Böhm et al, 2013 ; Misceo et al, 2014 ; Morin et al, 2014 ; Nesin et al, 2014 ; Morin et al, 2020 ). In addition, SOCE plays important roles in the pathophysiology of cardiovascular diseases, thrombus formation, tumor cell metastasis, and the pathogenesis of acute pancreatitis ( Varga-Szabo et al, 2008 ; Braun et al, 2009 ; Yang et al, 2009 ; Zhu et al, 2018 ; Lee & Papachristou, 2019 ; Lu et al, 2022 ), etc.…”

Section: Introductionmentioning

confidence: 99%

S417 in the CC3 region of STIM1 is critical for STIM1-Orai1 binding and CRAC channel activation

Luo

et al. 2023

Life Sci. Alliance

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Store-operated Ca2+entry (SOCE) is a universal Ca2+influx pathway that is important for the function of many cell types. SOCE is controlled by the interaction of the ER Ca2+sensor STIM1 with the plasma membrane Ca2+channel Orai1. S417 is located in the third coiled-coil (CC3) domain of the C-terminus of STIM1. We found that single-point mutation of this residue (S417G) abolished STIM1 C-terminus interactions with Orai1. Mutation of S417 also abolished CAD-Orai1 binding and Orai1 channel activation, eliminated STIM1 puncta formation, and co-localization with Orai1 and SOCE. 2-APB was found to restore the binding of the STIM1 C-terminus mutant (S417G) to Orai1 and dose-dependently activate Orai1 channel. Both CBD and NBD of Orai1 are required for 2-APB–induced coupling between the Orai1 and STIM1 C-terminus mutant (S417G) and CRAC channel activation. We also demonstrated that 2-APB led to delayed activation of Orai1-K85E channel, although Orai1-K85E obviously impairs 2-APB–induced STIM1 C-terminus mutant (S417G)–Orai1 coupling. Our results suggest S417 in the CC3 domain of STIM1 is essential for STIM1–Orai1 binding and CRAC channel activation.

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“…ECCE causes Ca 2+ influx in response to physiological triggers [ 17 , 18 ]. In addition, a mechanism triggered by depletion of intracellular Ca 2+ stores (endoplasmic/sarcoplasmic reticulum, ER and SR), known as store-operated Ca 2+ entry (SOCE) [ 19 , 20 , 21 , 22 ], was also reported in skeletal muscle [ 23 ]. SOCE is a pathway mainly mediated by the interaction between (a) stromal interaction molecule-1 (STIM1), a protein placed in the ER/SR membrane, which has an intra-luminal domain that acts as Ca 2+ sensor; and (b) Orai1, a protein that mediates Ca 2+ release-activated (CRAC) current and is placed in external membranes or TTs [ 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 ].…”

Section: Introductionmentioning

confidence: 99%

Searching for Mechanisms Underlying the Assembly of Calcium Entry Units: The Role of Temperature and pH

Girolami

Serano

Fonso

et al. 2023

IJMS

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Store-operated Ca2+ entry (SOCE) is a mechanism that allows muscle fibers to recover external Ca2+, which first enters the cytoplasm andthen, via SERCA pump, also refills the depleted intracellular stores (i.e., the sarcoplasmic reticulum, SR). We recently discovered that SOCE is mediated by Calcium Entry Units (CEUs), intracellular junctions formed by: (i) SR stacks containing STIM1; and (ii) I-band extensions of the transverse tubule (TT) containing Orai1. The number and size of CEUs increase during prolonged muscle activity, though the mechanisms underlying exercise-dependent formation of new CEUs remain to be elucidated. Here, we first subjected isolated extensor digitorum longus (EDL) muscles from wild type mice to an exvivo exercise protocol and verified that functional CEUs can assemble alsoin the absence of blood supply and innervation. Then, we evaluated whetherparameters that are influenced by exercise, such as temperature and pH, may influence the assembly of CEUs. Results collected indicate that higher temperature (36 °C vs. 25 °C) and lower pH (7.2 vs. 7.4) increase the percentage of fibers containing SR stacks, the n. of SR stacks/area, and the elongation of TTs at the I band. Functionally, assembly of CEUs at higher temperature (36 °C) or at lower pH (7.2) correlates with increased fatigue resistance of EDL muscles in the presence of extracellular Ca2+. Taken together, these results indicate that CEUs can assemble in isolated EDL muscles and that temperature and pH are two of the possible regulators of CEU formation.

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Role of store-operated Ca2+ entry in cardiovascular disease

Cited by 16 publications

References 105 publications

Application of fluorescent potential-sensitive probes for the study of living blood and marrow cells

Application of fluorescent potential-sensitive probes for the study of living blood and marrow cells

S417 in the CC3 region of STIM1 is critical for STIM1-Orai1 binding and CRAC channel activation

Searching for Mechanisms Underlying the Assembly of Calcium Entry Units: The Role of Temperature and pH

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