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  • American Physiological Society  (10)
  • Shumilina, Ekaterina  (10)
  • 1
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    Decreased cation channel activity and blunted channel-dependent eryptosis in neonatal erythrocytes
    American Physiological Society ; 2006
    In:  American Journal of Physiology-Cell Physiology Vol. 291, No. 4 ( 2006-10), p. C710-C717
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 291, No. 4 ( 2006-10), p. C710-C717
    Abstract: Eryptosis or apoptosis-like death of erythrocytes is characterized by phosphatidylserine exposure and erythrocyte shrinkage, both typical features of nucleated apoptotic cells. Eryptosis is triggered by activation of nonselective Ca 2+ -permeable cation channels with subsequent entry of Ca 2+ and stimulation of Ca 2+ -sensitive scrambling of the cell membrane. The channels are activated and thus eryptosis is triggered by Cl − removal, osmotic shock, oxidative stress, or glucose deprivation. The present study has been performed to compare cation channel activity and susceptibility to eryptosis in neonatal and adult erythrocytes. Channel activity was determined by patch-clamp analysis, cytosolic Ca 2+ activity by fluo-3 fluorescence, phosphatidylserine exposure by FITC-labeled annexin V binding, and cell shrinkage by decrease in forward scatter in fluorescence-activated cell sorting analysis. Prostaglandin E 2 (PGE 2 ) formation, cation channel activity, Ca 2+ entry, annexin V binding, and decreased forward scatter were triggered by removal of Cl − in both adult and neonatal erythrocytes. The effects were, however, significantly blunted in neonatal erythrocytes. Osmotic shock, PGE 2, and platelet-activating factor similarly increased annexin V binding and decreased forward scatter, effects again significantly reduced in neonatal erythrocytes. On the other hand, spontaneous and oxidative (addition of tert-butylperoxide) stress-induced eryptosis was significantly larger in neonatal erythrocytes. In conclusion, cation channel activity, Ca 2+ leakage, and thus channel-dependent triggering of eryptosis are blunted, whereas spontaneous and oxidative stress-induced eryptosis is more pronounced in neonatal erythrocytes.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00631.2005
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2006
    detail.hit.zdb_id: 1477334-X
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  • 2
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    Ca 2+ signaling in the regulation of dendritic cell functions
    American Physiological Society ; 2011
    In:  American Journal of Physiology-Cell Physiology Vol. 300, No. 6 ( 2011-06), p. C1205-C1214
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 300, No. 6 ( 2011-06), p. C1205-C1214
    Abstract: Dendritic cells (DCs) are highly versatile antigen-presenting cells critically involved in both innate and adaptive immunity as well as maintenance of self-tolerance. DC function is governed by Ca 2+ signaling, which directs the DC responses to diverse antigens, including Toll-like receptor ligands, intact bacteria, and microbial toxins. Ca 2+ -sensitive DC functions include DC activation, maturation, migration, and formation of immunological synapses with T cells. Moreover, alterations of cytosolic Ca 2+ trigger immune suppression or switch off DC activity. Ca 2+ signals are generated by the orchestration of Ca 2+ transport processes across plasma, endoplasmic reticulum, and inner mitochondrial membrane. These processes include active pumping of Ca 2+ , Ca 2+ /Na + antiport, and electrodiffusion through Ca 2+ -permeable channels or uniporters. Ca 2+ channels in the plasma membrane such as Ca 2+ release-activated Ca 2+ or L-type Ca 2+ channels are tightly regulated by the membrane potential which in turn depends on the activity of voltage-gated K + or Ca 2+ -activated nonselective cation channels. The rapidly growing knowledge on the function and regulation of these membrane transport proteins provides novel insight into pathophysiological mechanisms underlying dysfunction of the immune system and opens novel therapeutic opportunity to favorably influence the function of the immune system.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00039.2011
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2011
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  • 3
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    Serum- and glucocorticoid-inducible kinase SGK1 regulates reorganization of actin cytoskeleton in mast cells upon degranulation
    American Physiological Society ; 2013
    In:  American Journal of Physiology-Cell Physiology Vol. 304, No. 1 ( 2013-01-01), p. C49-C55
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 304, No. 1 ( 2013-01-01), p. C49-C55
    Abstract: Aggregation of the high-affinity IgE receptor (FcεRI) on mast cells (MCs) causes MC degranulation, a process that involves cortical F-actin disassembly. Actin depolymerization may be triggered by increase of cytosolic Ca 2+ . Entry of Ca 2+ through the Ca 2+ release-activated Ca 2+ (CRAC) channels is under powerful regulation by the serum- and glucocorticoid-inducible kinase SGK1. Moreover, FcεRI-dependent degranulation is decreased in SGK1-deficient ( sgk1 −/− ) MCs. The present study addressed whether SGK1 is required for actin cytoskeleton rearrangement in MCs and whether modulation of actin architecture could underlie decreased degranulation of sgk1 −/− MCs. Confirming previous results, release of β-hexosaminidase reflecting FcεRI-dependent degranulation was impaired in sgk1 −/− MCs compared with sgk1 +/+ MCs. When CRAC channels were inhibited by 2-aminoethoxydiphenyl borate (2-APB; 50 μM), MC degranulation was strongly decreased in both sgk1 +/+ and sgk1 −/− MCs and the difference between genotypes was abolished. Moreover, degranulation was impaired by actin-stabilizing (phallacidin) and enhanced by actin-disrupting (cytochalasin B) agents to a similar extent in sgk1 +/+ MCs and sgk1 −/− MCs, implying a regulatory role of actin reorganization in this event. In line with this, measurements of monomeric (G) and filamentous (F) actin content by FACS analysis and Western blotting of detergent-soluble and -insoluble cell fractions indicated an increase of the G/F-actin ratio in sgk1 +/+ MCs but not in sgk1 −/− MCs upon FcεRI ligation, an observation reflecting actin depolymerization. In sgk1 +/+ MCs, FcεRI-induced actin depolymerization was abolished by 2-APB. The observed actin reorganization was confirmed by confocal laser microscopic analysis. Our observations uncover SGK1-dependent Ca 2+ entry in mast cells as a novel mechanism regulating actin cytoskeleton.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00179.2012
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2013
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  • 4
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    Energy-sensitive regulation of Na + /K + -ATPase by Janus kinase 2
    American Physiological Society ; 2014
    In:  American Journal of Physiology-Cell Physiology Vol. 306, No. 4 ( 2014-02-15), p. C374-C384
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 306, No. 4 ( 2014-02-15), p. C374-C384
    Abstract: Janus kinase 2 (JAK2) contributes to intracellular signaling of leptin and erythropoietin, hormones protecting cells during energy depletion. The present study explores whether JAK2 is activated by energy depletion and regulates Na + /K + -ATPase, the major energy-consuming pump. In Jurkat cells, JAK2 activity was determined by radioactive kinase assay, phosphorylated JAK2 detected by Western blotting, ATP levels measured by luciferase assay, as well as Na + /K + -ATPase α1-subunit transcript and protein abundance determined by real-time PCR and Western blotting, respectively. Ouabain-sensitive K + -induced currents ( I pump ) were measured by whole cell patch clamp. I pump was further determined by dual-electrode voltage clamp in Xenopus oocytes injected with cRNA-encoding JAK2, active V617F JAK2, or inactive K882E JAK2. As a result, in Jurkat T cells, JAK2 activity significantly increased following energy depletion by sodium azide (NaN 3 ) or 2,4- dinitro phenol (DNP). DNP- and NaN 3 -induced decrease of cellular ATP was significantly augmented by JAK2 inhibitor AG490 and blunted by Na + /K + -ATPase inhibitor ouabain. DNP decreased and AG490 enhanced I pump as well as Na + /K + -ATPase α1-subunit transcript and protein abundance. The α1-subunit transcript levels were also enhanced by signal transducer and activator of transcription-5 inhibitor CAS 285986-31-4. In Xenopus oocytes, I pump was significantly decreased by expression of JAK2 and V617F JAK2 but not of K882E JAK2, effects again reversed by AG490. In V617F JAK2-expressing Xenopus oocytes, neither DNP nor NaN 3 resulted in further decline of I pump . In Xenopus oocytes, the effect of V617F JAK2 on I pump was not prevented by inhibition of transcription with actinomycin. In conclusion, JAK2 is a novel energy-sensing kinase that curtails energy consumption by downregulating Na + /K + -ATPase expression and activity.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00320.2013
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2014
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  • 5
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    Inhibition of voltage-gated K + channels in dendritic cells by rapamycin
    American Physiological Society ; 2010
    In:  American Journal of Physiology-Cell Physiology Vol. 299, No. 6 ( 2010-12), p. C1379-C1385
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 299, No. 6 ( 2010-12), p. C1379-C1385
    Abstract: Rapamycin, an inhibitor of the serine/threonine kinase mammalian target of rapamycin (mTOR), is a widely used immunosuppressive drug. Rapamycin affects the function of dendritic cells (DCs), antigen-presenting cells participating in the initiation of primary immune responses and the establishment of immunological memory. Voltage-gated K + (Kv) channels are expressed in and impact on the function of DCs. The present study explored whether rapamycin influences Kv channels in DCs. To this end, DCs were isolated from murine bone marrow and ion channel activity was determined by whole cell patch clamp. To more directly analyze an effect of mTOR on Kv channel activity, Kv1.3 and Kv1.5 were expressed in Xenopus oocytes with or without the additional expression of mTOR and voltage-gated currents were determined by dual-electrode voltage clamp. As a result, preincubation with rapamycin (0–50 nM) led to a gradual decline of Kv currents in DCs, reaching statistical significance within 6 h and 50 nM of rapamycin. Rapamycin accelerated Kv channel inactivation. Coexpression of mTOR upregulated Kv1.3 and Kv1.5 currents in Xenopus oocytes. Furthermore, mTOR accelerated Kv1.3 channel activation and slowed down Kv1.3 channel inactivation. In conclusion, mTOR stimulates Kv channels, an effect contributing to the immunomodulating properties of rapamycin in DCs.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00367.2010
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2010
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  • 6
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    Effect of dexamethasone on Na + /Ca 2+ exchanger in dendritic cells
    American Physiological Society ; 2011
    In:  American Journal of Physiology-Cell Physiology Vol. 300, No. 6 ( 2011-06), p. C1306-C1313
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 300, No. 6 ( 2011-06), p. C1306-C1313
    Abstract: Ca + -dependent signaling regulates the function of dendritic cells (DCs), antigen-presenting cells linking innate and adaptive immunity. The activity of DCs is suppressed by glucocorticoids, potent immunosuppressive hormones. The present study explored whether the glucocorticoid dexamethasone influences the cytosolic Ca 2+ concentration ([Ca 2+ ] i ) in DCs. To this end, DCs were isolated from mouse bone marrow. According to fura-2 fluorescence, exposure of DCs to lipopolysaccharide (LPS, 100 ng/ml) increased [Ca 2+ ] i , an effect significantly blunted by overnight incubation with 10 nM dexamethasone before LPS treatment. Dexamethasone did not affect the Ca 2+ content of intracellular stores, sarco(endo)plasmic reticulum Ca 2+ -ATPase (SERCA)2 and SERCA3 expression, ryanodine receptor (RyR)1 expression, or Ca 2+ entry through store-operated Ca 2+ channels. In contrast, dexamethasone increased the transcript level and the membrane protein abundance of the Na + /Ca 2+ exchanger NCX3. The activity of Na + /Ca 2+ exchangers was assessed by removal of extracellular Na + in the presence of external Ca 2+ , a maneuver triggering the Ca 2+ influx mode. Indeed, Na + removal resulted in a rapid transient increase of [Ca 2+ ] i and induced an outwardly directed current as measured in whole cell patch-clamp experiments. Dexamethasone significantly augmented the increase of [Ca 2+ ] i and the outward current following removal of extracellular Na + . The NCX blocker KB-R7943 reversed the inhibitory effect of dexamethasone on LPS-induced increase in [Ca 2+ ] i . Dexamethasone blunted LPS-induced stimulation of CD86 expression and TNF-α production, an effect significantly less pronounced in the presence of NCX blocker KB-R7943. In conclusion, our results show that glucocorticoid treatment blunts LPS-induced increase in [Ca 2+ ] i in DCs by increasing expression and activity of Na + /Ca 2+ exchanger NCX3. The effect contributes to the inhibitory effect of the glucocorticoid on DC maturation.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00396.2010
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2011
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  • 7
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    Upregulation of the large conductance voltage- and Ca 2+ -activated K + channels by Janus kinase 2
    American Physiological Society ; 2014
    In:  American Journal of Physiology-Cell Physiology Vol. 306, No. 11 ( 2014-06-01), p. C1041-C1049
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 306, No. 11 ( 2014-06-01), p. C1041-C1049
    Abstract: The iberiotoxin-sensitive large conductance voltage- and Ca 2+ -activated potassium (BK) channels (maxi-K + -channels) hyperpolarize the cell membrane thus supporting Ca 2+ entry through Ca 2+ -release activated Ca 2+ channels. Janus kinase-2 (JAK2) has been identified as novel regulator of ion transport. To explore whether JAK2 participates in the regulation of BK channels, cRNA encoding Ca 2+ -insensitive BK channels (BK M513I+Δ899–903 ) was injected into Xenopus oocytes with or without cRNA encoding wild-type JAK2, gain-of-function V617F JAK2, or inactive K882E JAK2. K + conductance was determined by dual electrode voltage clamp and BK-channel protein abundance by confocal microscopy. In A204 alveolar rhabdomyosarcoma cells, iberiotoxin-sensitive K + current was determined utilizing whole cell patch clamp. A204 cells were further transfected with JAK2 and BK-channel transcript, and protein abundance was quantified by RT-PCR and Western blotting, respectively. As a result, the K + current in BK M513I+Δ899–903 -expressing oocytes was significantly increased following coexpression of JAK2 or V617F JAK2 but not K882E JAK2. Coexpression of the BK channel with V617F JAK2 but not K882E JAK2 enhanced BK-channel protein abundance in the oocyte cell membrane. Exposure of BK-channel and V617F JAK2-expressing oocytes to the JAK2 inhibitor AG490 (40 μM) significantly decreased K + current. Inhibition of channel insertion by brefeldin A (5 μM) decreased the K + current to a similar extent in oocytes expressing the BK channel alone and in oocytes expressing the BK channel and V617F JAK2. The iberiotoxin (50 nM)-sensitive K + current in rhabdomyosarcoma cells was significantly decreased by AG490 pretreatment (40 μM, 12 h). Moreover, overexpression of JAK2 in A204 cells significantly enhanced BK channel mRNA and protein abundance. In conclusion, JAK2 upregulates BK channels by increasing channel protein abundance in the cell membrane.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00209.2013
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2014
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  • 8
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    Lipopolysaccharide-sensitive H + current in dendritic cells
    American Physiological Society ; 2012
    In:  American Journal of Physiology-Cell Physiology Vol. 303, No. 2 ( 2012-07-15), p. C204-C212
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 303, No. 2 ( 2012-07-15), p. C204-C212
    Abstract: Dendritic cells (DCs) are the most potent antigen-presenting cells equipped to transport antigens from the periphery to lymphoid tissues and to present them to T cells. Ligation of Toll-like receptor 4 (TLR4), expressed on the DC surface, by lipopolysaccharides (LPS), elements of the Gram-negative bacteria outer wall, induces DC maturation. Initial steps of maturation include stimulation of antigen endocytosis and enhanced reactive oxygen species (ROS) production with eventual downregulation of endocytic capacity in fully matured DCs. ROS production depends on NADPH oxidase (NOX2), the activity of which requires continuous pH and charge compensation. The present study demonstrates, for the first time, the functional expression of voltage-gated proton (Hv1) channels in mouse bone marrow-derived DCs. In whole cell patch-clamp experiments, we recorded Zn 2+ (50 μM)-sensitive outwardly rectifying currents activated upon depolarization, which were highly selective for H + , with the reversal potential shift of 38 mV per pH unit. The threshold voltage of activation ( V threshold ) was dependent on the pH gradient and was close to the empirically predicted V threshold for the Hv1 currents. LPS (1 μg/ml) had bimodal effects on Hv1 channels: acute LPS treatment increased Hv1 channel activity, whereas 24 h of LPS incubation significantly inhibited Hv1 currents and decreased ROS production. Activation of H + currents by acute application of LPS was abolished by PKC inhibitor GFX (10 nM). According to electron current measurements, acute LPS application was associated with increased NOX2 activity.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00059.2012
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2012
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  • 9
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    Blunted IgE-mediated activation of mast cells in mice lacking the serum- and glucocorticoid-inducible kinase SGK3
    American Physiological Society ; 2010
    In:  American Journal of Physiology-Cell Physiology Vol. 299, No. 5 ( 2010-11), p. C1007-C1014
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 299, No. 5 ( 2010-11), p. C1007-C1014
    Abstract: Previous studies have shown that pharmacological inhibition of the phosphoinositol-3 (PI3) kinase disrupts the activation of mast cells. Through phosphoinositide-dependent kinase PDK1, PI3 kinase activates the serum- and glucocorticoid-inducible kinase 3 (SGK3). The present study explored the role of SGK3 in mast cell function. Mast cells were isolated and cultured from bone marrow (BMMCs) of gene-targeted mice lacking SGK3 ( sgk3 −/− ) and their wild-type littermates ( sgk3 +/+ ). BMMC numbers in the ear conch were similar in both genotypes. Stimulation with IgE and cognate antigen triggered the release of intracellular Ca 2+ and entry of extracellular Ca 2+ . Influx of extracellular Ca 2+ but not Ca 2+ release from intracellular stores was significantly blunted in sgk3 −/− BMMCs compared with sgk3 +/+ BMMCs. Antigen stimulation further led to a rapid increase of a K + -selective conductance in sgk3 +/+ BMMCs, an effect again blunted in sgk3 −/− BMMCs. In contrast, the Ca 2+ ionophore ionomycin activated K + currents to a similar extent in sgk3 −/− and in sgk3 +/+ BMMCs. β-Hexosaminidase release, triggered by antigen stimulation, was also significantly decreased in sgk3 −/− BMMCs. IgE-dependent anaphylaxis measured as a sharp decrease in body temperature upon injection of DNP-HSA antigen was again significantly blunted in sgk3 −/− compared with sgk3 +/+ mice. Serum histamine levels measured 30 min after induction of an anaphylactic reaction were significantly lower in sgk3 −/− than in sgk3 +/+ mice. In conclusion, both in vitro and in vivo function of BMMCs are impaired in gene targeted mice lacking SGK3. Thus SGK3 is critical for proper mast cell function.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00539.2009
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2010
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  • 10
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    Altered regulation of cytosolic Ca 2+ concentration in dendritic cells from klotho hypomorphic mice
    American Physiological Society ; 2013
    In:  American Journal of Physiology-Cell Physiology Vol. 305, No. 1 ( 2013-07-01), p. C70-C77
    Details
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 305, No. 1 ( 2013-07-01), p. C70-C77
    Abstract: The function of dendritic cells (DCs), antigen-presenting cells regulating naïve T-cells, is regulated by cytosolic Ca 2+ concentration ([Ca 2+ ] i ). [Ca 2+ ] i is increased by store-operated Ca 2+ entry and decreased by K + -independent (NCX) and K + -dependent (NCKX) Na + /Ca 2+ exchangers. NCKX exchangers are stimulated by immunosuppressive 1,25-dihydroxyvitamin D3 [1,25(OH) 2 D 3 ], the biologically active form of vitamin D. Formation of 1,25(OH) 2 D 3 is inhibited by the antiaging protein Klotho. Thus 1,25(OH) 2 D 3 plasma levels are excessive in Klotho-deficient mice ( klotho hm ). The present study explored whether Klotho deficiency modifies [Ca 2+ ] i regulation in DCs. DCs were isolated from the bone marrow of klotho hm mice and wild-type mice ( klotho +/+ ) and cultured for 7–9 days with granulocyte-macrophage colony-stimulating factor. According to major histocompatibility complex II (MHC II) and CD86 expression, differentiation and lipopolysaccharide (LPS)-induced maturation were similar in klotho hm DCs and klotho +/+ DCs. However, NCKX1 membrane abundance and NCX/NCKX-activity were significantly enhanced in klotho hm DCs. The [Ca 2+ ] i increase upon acute application of LPS (1 μg/ml) was significantly lower in klotho hm DCs than in klotho +/+ DCs, a difference reversed by the NCKX blocker 3′,4′-dichlorobenzamyl (DBZ; 10 μM). CCL21-dependent migration was significantly less in klotho hm DCs than in klotho +/+ DCs but could be restored by DBZ. NCKX activity was enhanced by pretreatment of klotho +/+ DC precursors with 1,25(OH) 2 D 3 the first 2 days after isolation from bone marrow. Feeding klotho hm mice a vitamin D-deficient diet decreased NCKX activity, augmented LPS-induced increase of [Ca 2+ ] i , and enhanced migration of klotho hm DCs, thus dissipating the differences between klotho hm DCs and klotho +/+ DCs. In conclusion, Klotho deficiency upregulates NCKX1 membrane abundance and Na + /Ca 2+ -exchange activity, thus blunting the increase of [Ca 2+ ] i following LPS exposure and CCL21-mediated migration. The effects are in large part due to excessive 1,25(OH) 2 D 3 formation.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    URL: Article
    DOI: 10.1152/ajpcell.00355.2012
    Language: English
    Publisher: American Physiological Society
    Publication Date: 2013
    detail.hit.zdb_id: 1477334-X
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