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Vats, Yu. A.; Fedirko, N. V.; Klevets, M. Yu.; Voitenko, Nana

doi:10.1023/a:1020257722880

Cited by 8 publications

(1 citation statement)

References 15 publications

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“…In this sense ROS, such as H 2 O 2 , can affect the activity of SERCA, however the mechanisms that underlie this process remain unclear. Several authors have described that metal-catalyzed oxidation result in SERCA inhibition by direct disulfide bonds oxidation, this is the case in platelets [26,85], but in other cell types, such as skeletal-muscle cells [86] or myocardic H9c2 [83], SERCA inhibition is induced by an independent oxidative mechanism. Other ROS like hydroxyl radicals and peroxynitrite can also reduce the activity of SERCA [86,87].…”

Section: (C) Removal Of Cytosolic Calciummentioning

confidence: 99%

Calcium Signalling and Reactive Oxygen Species in Non-Excitable Cells

Rosado¹,

Redondo²,

Salido³

et al. 2006

MRMC

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Section: (C) Removal Of Cytosolic Calciummentioning

confidence: 99%

Calcium Signalling and Reactive Oxygen Species in Non-Excitable Cells

Rosado¹,

Redondo²,

Salido³

et al. 2006

MRMC

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Selectivity of plasma membrane calcium ATPase (PMCA)-mediated extrusion of toxic divalent cations in vitro and in cultured cells

et al. 2017

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In the recent years, the toxicity of certain divalent cations has been associated with the alteration of intracellular Ca homeostasis. Among other mechanisms, these cations may affect the functionality of certain Ca-binding proteins and/or Ca pumps. The plasma membrane calcium pump (PMCA) maintains Ca homeostasis in eukaryotic cells by mediating the efflux of this cation in a process coupled to ATP hydrolysis. The aim of this work was to investigate both in vitro and in cultured cells if other divalent cations (Sr, Ba, Co, Cd, Pb or Be) could be transported by PMCA. Current results indicate that both purified and intact cell PMCA transported Sr with kinetic parameters close to those of Ca transport. The transport of Pb and Co by purified PMCA was, respectively, 50 and 75% lower than that of Ca, but only Co was extruded by intact cells and to a very low extent. In contrast, purified PMCA-but not intact cell PMCA-transported Ba at low rates and only when activated by limited proteolysis or by phosphatidylserine addition. Finally, purified PMCA did not transport Cd or Be, although minor Be transport was measured in intact cells. Moreover, Cd impaired the transport of Ca through various mechanisms, suggesting that PMCA may be a potential target of Cd-mediated toxicity. The differential capacity of PMCA to transport these divalent cations may have a key role in their detoxification, limiting their noxious effects on cell homeostasis.

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Mechanisms Underlying Leakage of Calcium from the Endoplasmic Reticulum of Acinar Cells of the Submandibular Salivary Gland

et al. 2005

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In the resting state, the Са 2+ concentration in agonist-sensitive intracellular stores reflects the balance between active uptake of Са 2+ , which is mediated by Са 2+ -ATPase (SERCA), and passive leakage of Са 2+ . The mechanisms underlying such a leakage in cells of the submaxillary salivary gland were not studied. In our experiments, we examined possible pathways of passive leakage of Са 2+ from the endoplasmic reticulum (ER) of acinar cells obtained from the rat submaxillary salivary gland; direct measurements of the concentration of Са 2+ in the ER ([Ca 2+ ] ER ) using a low-affinity calcium-sensitive dye, mag-fura 2/AM, were performed. The cellular membrane was permeabilized with the help of β-escin (40 μg/ml); the Са 2+ concentration in the cytoplasm ([Ca 2+ ] і ) was clamped at its level typical of the resting state (~100 nM) using an EGTA/Ca 2+ buffer. Incubation of permeabilized acinar cells in a calcium-free intracellular milieu, as well as application of thapsigargin, resulted in complete inhibition of the uptake of Ca 2+ with the involvement of SERCA. This effect was observed 1 min after the beginning of superfusion of the cells with the corresponding solutions and was accompanied by the leakage of Са 2+ from the ER; this is confirmed by a gradual drop in the [Ca 2+ ] ER . Such a leakage of Са 2+ remained unchanged in the presence of thapsigargin, heparin, and ruthenium red; therefore, it is not mediated by SERCA, inositol 1,4,5-trisphosphate-sensitive receptors (InsP 3 R), or ryanodine receptors (RyRs). At the same time, an antibiotic, puromycin (0.1 to 1.0 mM), which disconnects polypeptides from the ER-ribosome translocon complex, caused intensification of passive leakage of Са 2+ from the ER. This effect did not depend on the functioning of SERCA, InsP 3 R, or RyR. Therefore, passive leakage of Са 2+ from the ER in acinar cells of the submaxillary salivary gland is realized through pores of the translocon complex of the ER membrane.

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Untitled

Cited by 8 publications

References 15 publications

Calcium Signalling and Reactive Oxygen Species in Non-Excitable Cells

Calcium Signalling and Reactive Oxygen Species in Non-Excitable Cells

Selectivity of plasma membrane calcium ATPase (PMCA)-mediated extrusion of toxic divalent cations in vitro and in cultured cells

Mechanisms Underlying Leakage of Calcium from the Endoplasmic Reticulum of Acinar Cells of the Submandibular Salivary Gland

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