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  • S. Karger AG  (19)
  • 2015-2019  (19)
  • 1
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    Online Resource
    LEFTY2 Controls Migration of Human Endometrial Cancer Cells via Focal Adhesion Kinase Activity (FAK) and miRNA-200a
    S. Karger AG ; 2016
    In:  Cellular Physiology and Biochemistry Vol. 39, No. 3 ( 2016), p. 815-826
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 39, No. 3 ( 2016), p. 815-826
    Abstract: Background: LEFTY2, a suppressor of cell proliferation, tumor growth, regulator of stemness and embryonic differentiation, is a negative regulator of cancer cell reprogramming. Malignant transformation may lead to migration requiring loss of adhesion and gain of migratory activity. Signaling involved in the orchestration of migration, proliferation and spreading of cells include focal adhesion kinase (FAK) and adhesion molecule E-cadherin. Aims: The present study explored whether LEFTY2 influences the proliferation marker MKi67, FAK activity, E-cadherin abundance and migration of Ishikawa human endometrial carcinoma cells. Moreover, the study explored the involvement of microRNA-200a (miR-200a), which is known to regulate cellular adhesion by targeting E-Cadherin. Methods: FAK activity was estimated from FAK phosphorylation quantified by Western blotting, migration utilizing a wound healing assay, miR-200a and MKi67 expression levels utilizing qRT-PCR, cell proliferation and apoptosis using BrdU and Annexin V staining, respectively, and E-Cadherin (E-Cad) abundance, using confocal microscopy. Results: LEFTY2 (25 ng/ml, 48 hours) treatment was followed by decrease of MKi67 expression, FAK activity and migration. LEFTY2 upregulated miRNA-200a and E-Cad protein level in Ishikawa cells. The effect of LEFTY2 on migration was mimicked by FAK inhibitor PF 573228 (50 µM). Addition of LEFTY2 in the presence of PF-573228 did not result in a further significant decline of migration. Conclusion: In conclusion, LEFTY2 down-regulates MKi67 expression and FAK activity, up-regulates miR-200a and E-cadherin, and is thus a powerful negative regulator of endometrial cell proliferation and migration.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000447792
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2016
    detail.hit.zdb_id: 1482056-0
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  • 2
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    Pomona Large Vessel Occlusion Screening Tool for Prehospital and Emergency Room Settings
    S. Karger AG ; 2018
    In:  Interventional Neurology Vol. 7, No. 3-4 ( 2018), p. 196-203
    Details
    In: Interventional Neurology, S. Karger AG, Vol. 7, No. 3-4 ( 2018), p. 196-203
    Abstract: 〈 b 〉 〈 i 〉 Background: 〈 /i 〉 〈 /b 〉 Early identification of patients with acute ischemic strokes due to large vessel occlusions (LVO) is critical. We propose a simple risk score model to predict LVO. 〈 b 〉 〈 i 〉 Method: 〈 /i 〉 〈 /b 〉 The proposed scale (Pomona Scale) ranges from 0 to 3 and includes 3 items: gaze deviation, expressive aphasia, and neglect. We reviewed a cohort of all acute stroke activation patients between February 2014 and January 2016. The predictive performance of the Pomona Scale was determined and compared with several National Institutes of Health Stroke Scale (NIHSS) cutoffs (≥4, ≥6, ≥8, and ≥10), the Los Angeles Motor Scale (LAMS), the Cincinnati Prehospital Stroke Severity (CPSS) scale, the Vision Aphasia and Neglect Scale (VAN), and the Prehospital Acute Stroke Severity Scale (PASS). 〈 b 〉 〈 i 〉 Results: 〈 /i 〉 〈 /b 〉 LVO was detected in 94 of 776 acute stroke activations (12%). A Pomona Scale ≥2 had comparable accuracy to predict LVO as the VAN and CPSS scales and higher accuracy than Pomona Scale ≥1, LAMS, PASS, and NIHSS. A Pomona Scale ≥2 had an accuracy (area under the curve) of 0.79, a sensitivity of 0.86, a specificity of 0.70, a positive predictive value of 0.71, and a negative predictive value of 0.97 for the detection of LVO. We also found that the presence of either neglect or gaze deviation alone had comparable accuracy of 0.79 as Pomona Scale ≥2 to detect LVO. 〈 b 〉 〈 i 〉 Conclusion: 〈 /i 〉 〈 /b 〉 The Pomona Scale is a simple and accurate scale to predict LVO. In addition, the presence of either gaze deviation or neglect also suggests the possibility of LVO.
    Type of Medium: Online Resource
    ISSN: 1664-9737 , 1664-5545
    URL: Article
    DOI: 10.1159/000486515
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2018
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  • 3
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    Negative Effect of Ellagic Acid on Cytosolic pH Regulation and Glycolytic Flux in Human Endometrial Cancer Cells
    S. Karger AG ; 2017
    In:  Cellular Physiology and Biochemistry Vol. 41, No. 6 ( 2017), p. 2374-2382
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 41, No. 6 ( 2017), p. 2374-2382
    Abstract: Background/Aims: Key properties of tumor cells include enhanced glycolytic flux with excessive consumption of glucose and formation of lactate. As glycolysis is highly sensitive to cytosolic pH, maintenance of glycolysis requires export of H+ ions, which is in part accomplished by Na+/H+ exchangers, such as NHE1. The carrier is sensitive to oxidative stress. Growth of tumor cells could be suppressed by the polyphenol Ellagic acid, which is found in various fruits and vegetables. An effect of Ellagic acid on transport processes has, however, never been reported. The present study thus elucidated an effect of Ellagic acid on cytosolic pH (pHi), NHE1 transcript levels, NHE1 protein abundance, Na+/H+ exchanger activity, and lactate release. Methods: Experiments were performed in Ishikawa cells without or with prior Ellagic acid (20 µM) treatment. NHE1 transcript levels were determined by qRT-PCR, NHE1 protein abundance by Western blotting, pHi utilizing (2',7'-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein [BCECF] fluorescence, Na+/H+ exchanger activity from Na+ dependent realkalinization after an ammonium pulse, cell volume from forward scatter in flow cytometry, reactive oxygen species (ROS) from 2’,7’-dichlorodihydrofluorescein fluorescence, glucose uptake utilizing 2-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-2-deoxyglucose, and lactate concentration in the supernatant utilizing a colorimetric (570 nm)/ fluorometric enzymatic assay. Results: A 48 hour treatment with Ellagic acid (20 µM) significantly decreased NHE1 transcript levels by 75%, NHE1 protein abundance by 95%, pHi from 7.24 ± 0.01 to 7.02 ± 0.01, Na+/H+ exchanger activity by 77%, forward scatter by 10%, ROS by 82%, glucose uptake by 58%, and lactate release by 15%. Conclusion: Ellagic acid (20µM) markedly down-regulates ROS formation and NHE1 expression leading to decreased Na+/H+ exchanger activity, pHi, glucose uptake and lactate release in endometrial cancer cells. Those effects presumably contribute to reprogramming and growth inhibition of tumor cells.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000475655
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2017
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  • 4
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    Regulation of Large Conductance Voltage-and Ca2+-Activated K+ Channels by the Janus Kinase JAK3
    S. Karger AG ; 2015
    In:  Cellular Physiology and Biochemistry Vol. 37, No. 1 ( 2015), p. 297-305
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 37, No. 1 ( 2015), p. 297-305
    Abstract: Background/Aims: Janus kinase 3 (JAK3), a tyrosine kinase contributing to the regulation of cell proliferation and apoptosis of lymphocytes and tumour cells, has been shown to modify the expression and function of several ion channels and transport proteins. Channels involved in the regulation of cell proliferation include the large conductance voltage- and Ca2+-activated K+ channel BK. The present study explored whether JAK3 modifies BK channel protein abundance and current. Methods: cRNA encoding Ca2+-insensitive BK channel (BKM513I+Δ899-903) was injected into Xenopus oocytes with or without additional injection of cRNA encoding wild-type JAK3, constitutively active A568VJAK3, or inactive K851AJAK3. Voltage gated K+ channel activity was measured utilizing dual electrode voltage clamp. Moreover, BK channel protein abundance was determined utilizing flow cytometry in CD19+ B lymphocyte cell membranes from mice lacking functional JAK3 (jak3-/-) and corresponding wild-type mice (jak3+/+). Results: BK activity in BKM513I+Δ899-903 expressing oocytes was slightly but significantly decreased by coexpression of wild-type JAK3 and of A568VJAK3, but not by coexpression of K851AJAK3. The BK channel protein abundance in the cell membrane was significantly higher in jak3-/- than in jak3+/+ B lymphocytes. The decline of conductance in BK and JAK3 coexpressing oocytes following inhibition of channel protein insertion by brefeldin A (5 µM) was similar in oocytes expressing BK with JAK3 and oocytes expressing BK alone, indicating that JAK3 might slow channel protein insertion into rather than accelerating channel protein retrieval from the cell membrane. Conclusion: JAK3 is a weak negative regulator of membrane BK protein abundance and activity.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000430354
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2015
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  • 5
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    The Role of Janus Kinase 3 in the Regulation of Na+/K+ ATPase under Energy Depletion
    S. Karger AG ; 2015
    In:  Cellular Physiology and Biochemistry Vol. 36, No. 2 ( 2015), p. 727-740
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 36, No. 2 ( 2015), p. 727-740
    Abstract: Background/Aims: Janus kinase-3 (JAK3) is activated during energy depletion. Energy-consuming pumps include the Na+/K+-ATPase. The present study explored whether JAK3 regulates Na+/K+-ATPase in dendritic cells (DCs). Methods: Ouabain (100 µM)-sensitive (Iouabain) and K+-induced (Ipump) outward currents were determined by utilizing whole cell patch-clamp, Na+/K+-ATPase α1-subunit mRNA levels by RT-PCR, Na+/K+-ATPase protein abundance by flow cytometry or immunofluorescence, and cellular ATP by luciferase-assay in DCs from bone marrow of JAK3-knockout (jak3-/-) or wild-type mice (jak3+/+). Ipump was further determined by voltage clamp in Xenopus oocytes expressing JAK3, active A568VJAK3 or inactive K851AJAK3. Results: Na+/K+-ATPase α1-subunit mRNA and protein levels, as well as Ipump and Iouabain were significantly higher in jak3-/-DCs than in jak3+/+DCs. Energy depletion by 4h pre-treatment with 2,4-dinitro-phenol significantly decreased Ipump in jak3+/+ DCs but not in jak3-/-DCs. Cellular ATP was significantly lower in jak3-/-DCs than in jak3+/+DCs and decreased in both genotypes by 2,4-dinitro-phenol, an effect significantly more pronounced in jak3-/-DCs than in jak3+/+DCs and strongly blunted by ouabain in both jak3+/+ and jak3-/-DCs. Ipump and Iouabain in oocytes were decreased by expression of JAK3 and of A568VJAK3 but not of K851AJAK3. JAK3 inhibitor WHI-P154 (4-[(3'-bromo-4'-hydroxyphenyl)amino]-6,7-dimethoxyquinazoline, 22 μM) enhanced Ipump and Iouabain in JAK3 expressing oocytes. The difference between A568VJAK3 and K851AJAK3 expressing oocytes was virtually abrogated by actinomycin D (50 nM). Conclusions: JAK3 down-regulates Na+/K+-ATPase activity, an effect involving gene expression and profoundly curtailing ATP consumption.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000430133
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2015
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  • 6
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    Regulation of Na+/H+ Exchanger in Dendritic Cells by Akt1
    S. Karger AG ; 2015
    In:  Cellular Physiology and Biochemistry Vol. 36, No. 3 ( 2015), p. 1237-1249
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 36, No. 3 ( 2015), p. 1237-1249
    Abstract: Background/Aims: Dendritic cells (DCs), antigen-presenting cells critically important for primary immune response and establishment of immunological memory, are activated by bacterial lipopolysaccharides (LPS) resulting in stimulation of Na+/H+ exchanger, ROS formation and migration. The effects are dependent on phosphoinositide 3 (PI3) kinase and paralleled by Akt phosphorylation. The present study explored the contribution of the Akt isoform Akt1. Methods: Cytosolic pH (pHi) (2',7'-bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein [BCECF] fluorescence), Na+/H+ exchanger activity (Na+ dependent realkalinization after an ammonium pulse), cell volume (forward scatter in FACS analysis), and ROS production (2′,7′-dichlorodihydrofluorescein diacetate [DCFDA] fluorescence) were determined in DCs isolated from bone marrow of mice lacking functional Akt1/PKBα (akt1-/-) and their wild type littermates (akt1+/+). Results: Forward scatter was lower in akt1-/- than in akt1+/+ DCs, whereas pHi, Na+/H+ exchanger activity and ROS formation were less in untreated akt1-/- and akt1+/+ DCs. Exposure of DCs to LPS was followed by increase of forward scatter and ROS formation to a similar extent in akt1-/- and in akt1+/+ DCs. A 4 hours treatment with either LPS (1µg/ml) or tert-butylhydroperoxide (tBOOH, 5 µM) significantly stimulated Na+/H+ exchanger activity in both genotypes, effects, however, significantly blunted in akt1-/- DCs. Conclusion: The present observations demonstrate that Akt1 is required for the full stimulation of Na+/H+ exchanger activity by LPS or oxidative stress in dendritic cells.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000430293
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2015
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  • 7
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    OSR1 and SPAK Sensitivity of Large-Conductance Ca2+ Activated K+ Channel
    S. Karger AG ; 2016
    In:  Cellular Physiology and Biochemistry Vol. 38, No. 4 ( 2016), p. 1652-1662
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 38, No. 4 ( 2016), p. 1652-1662
    Abstract: Background/Aims: The oxidative stress-responsive kinase 1 (OSR1) and the serine/threonine kinases SPAK (SPS1-related proline/alanine-rich kinase) are under the control of WNK (with-no-K [Lys]) kinases. OSR1 and SPAK participate in diverse functions including cell volume regulation and neuronal excitability. Cell volume and neuronal excitation are further modified by the large conductance Ca2+-activated K+ channels (maxi K+ channel or BK channels). An influence of OSR1 and/or SPAK on BK channel activity has, however, never been shown. The present study thus explored whether OSR1 and/or SPAK modify the activity of BK channels. Methods: cRNA encoding the Ca2+ insensitive BK channel mutant BKM513I+Δ899-903 was injected into Xenopus laevis oocytes without or with additional injection of cRNA encoding wild-type OSR1 or wild-type SPAK, constitutively active T185EOSR1, catalytically inactive D164AOSR1, constitutively active T233ESPAK or catalytically inactive D212ASPAK. K+ channel activity was measured utilizing dual electrode voltage clamp. Results: BK channel activity in BKM513I+Δ899-903 expressing oocytes was significantly decreased by co-expression of OSR1 or SPAK. The effect of wild-type OSR1/SPAK was mimicked by T185EOSR1 and T233ESPAK, but not by D164AOSR1 or D212ASPAK. Conclusions: OSR1 and SPAK suppress BK channels, an effect possibly contributing to cell volume regulation and neuroexcitability.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000443105
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2016
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  • 8
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    Lithium Sensitivity of Store Operated Ca2+ Entry and Survival of Fibroblasts Isolated from Chorea-Acanthocytosis Patients
    S. Karger AG ; 2017
    In:  Cellular Physiology and Biochemistry Vol. 42, No. 5 ( 2017), p. 2066-2077
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 42, No. 5 ( 2017), p. 2066-2077
    Abstract: Background: The widely expressed protein chorein fosters activation of the phosphoinositide 3 kinase (PI3K) pathway thus supporting cell survival. Loss of function mutations of the chorein encoding gene VPS13A (vacuolar protein sorting-associated protein 13A) causes chorea-acanthocytosis (ChAc), a neurodegenerative disorder paralleled by deformations of erythrocytes. In mice, genetic knockout of chorein leads to enhanced neuronal apoptosis. PI3K dependent signalling upregulates Orai1, a pore forming channel protein accomplishing store operated Ca2+ entry (SOCE). Increased Orai1 expression and SOCE have been shown to confer survival of tumor cells. SOCE could be up-regulated by lithium. The present study explored, whether SOCE and/or apoptosis are altered in ChAc fibroblasts and could be modified by lithium treatment. Methods: Fibroblasts were isolated from ChAc patients and age-matched healthy volunteers. Cytosolic Ca2+ activity ([Ca2+]i) was estimated from Fura-2-fluorescence, SOCE from increase of [Ca2+] i following Ca2+ re-addition after Ca2+-store depletion with sarcoendoplasmatic Ca2+-ATPase (SERCA) inhibitor thapsigargin (1 µM), and apoptosis from annexin-V/propidium iodide staining quantified in flow cytometry. Results: SOCE was significantly smaller in ChAc fibroblasts than in control fibroblasts. Lithium (2 mM, 24 hours) significantly increased and Orai1 blocker 2-Aminoethoxydiphenyl Borate (2-APB, 50 µM, 24 hours) significantly decreased SOCE. Annexin-V-binding and propidium iodide staining were significantly higher in ChAc fibroblasts than in control fibroblasts. In ChAc fibroblasts annexin-V-binding and propidium iodide staining were significantly decreased by lithium treatment, significantly increased by 2-APB and virtually lithium insensitive in the presence of 2-APB. Conclusions: In ChAc fibroblasts, downregulation of SOCE contributes to enhanced susceptibility to apoptosis. Both, decreased SOCE and enhanced apoptosis of ChAc fibroblasts can be reversed by lithium treatment.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000479901
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2017
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  • 9
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    Enhanced Reactive Oxygen Species Production, Acidic Cytosolic pH and Upregulated Na+/H+ Exchanger (NHE) in Dicer Deficient CD4+ T Cells
    S. Karger AG ; 2017
    In:  Cellular Physiology and Biochemistry Vol. 42, No. 4 ( 2017), p. 1377-1389
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 42, No. 4 ( 2017), p. 1377-1389
    Abstract: Background: MicroRNAs (miRNAs) negatively regulate gene expression at a post-transcriptional level. Dicer, a cytoplasmic RNase III enzyme, is required for the maturation of miRNAs from precursor miRNAs. Dicer, therefore, is a critical enzyme involved in the biogenesis and processing of miRNAs. Several biological processes are controlled by miRNAs, including the regulation of T cell development and function. T cells generate reactive oxygen species (ROS) with parallel H+ extrusion accomplished by the Na+/H+-exchanger 1 (NHE1). The present study explored whether ROS production, as well as NHE1 expression and function are sensitive to the lack of Dicer (miRNAs deficient) and could be modified by individual miRNAs. Methods: CD4+ T cells were isolated from CD4 specific Dicer deficient (DicerΔ/Δ) mice and the respective control mice (Dicerfl/fl). Transcript and protein levels were quantified with RT-PCR and Western blotting, respectively. For determination of intracellular pH (pHi) cells were incubated with the pH sensitive dye bis-(2-carboxyethyl)-5-(and-6)-carboxyfluorescein (BCECF) and Na+/H+ exchanger (NHE) activity was calculated from re-alkalinization after an ammonium pulse. Changes in cell volume were measured using the forward scatter in flow cytometry, and ROS production utilizing 2',7' -dichlorofluorescin diacetate (DCFDA) fluorescence. Transfection of miRNA-control and mimics in T cells was performed using DharmaFECT3 reagent. Results: ROS production, cytosolic H+ concentration, NHE1 transcript and protein levels, NHE activity, and cell volume were all significantly higher in CD4+ T cells from DicerΔ/Δ mice than in CD4+ T cells from Dicerfl/fl mice. Furthermore, individual miR-200b and miR-15b modify pHi and NHE activity in Dicerfl/fl and DicerΔ/Δ CD4+ T cells, respectively. Conclusions: Lack of Dicer leads to oxidative stress, cytosolic acidification, upregulated NHE1 expression and activity as well as swelling of CD4+ T cells, functions all reversed by miR-15b or miR-200b.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000479201
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2017
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  • 10
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    Small Heat Shock Protein16.3 of Mycobacterium tuberculosis: After Two Decades of Functional Characterization
    S. Karger AG ; 2018
    In:  Cellular Physiology and Biochemistry Vol. 49, No. 1 ( 2018), p. 368-380
    Details
    In: Cellular Physiology and Biochemistry, S. Karger AG, Vol. 49, No. 1 ( 2018), p. 368-380
    Abstract: Small heat shock proteins (sHSPs) are one of the five families of proteins acting as molecular chaperone. sHSPs possess a universally conserved alpha-crystallin domain, hence, also known as alpha-crystallin family. Mycobacterium tuberculosis (MTB) is an etiological agent of tuberculosis, a disease claiming million of lives every year across the world. MTB has two sHSPs: sHSP16.3 (a 16.3 kDa protein) and Acr2 (a 17.8 kDa protein). Of these, sHSP16.3 has been reported to be crucial for survival of MTB during prolonged period of dormancy, in addition to indispensable role in its growth, virulence and cell wall thickening. Additionally, this mycobacterial protein is also beneficial for host as well. Due to strong immunogenic properties and consistent presence in patients sera, sHSP16.3 has largely been implicated in vaccine development and diagnosis of latent and active infections of MTB in the clinical cases of TB. Recently, our study provided the substantial evidence to exploit this mycobacterial protein as a good drug target for developing novel therapeutic intervention. In the present review, a comprehensive analysis of various attributes of sHSP16.3 has been done and major gaps in area have been highlighted for future course of action.
    Type of Medium: Online Resource
    ISSN: 1015-8987 , 1421-9778
    URL: Article
    DOI: 10.1159/000492887
    Language: English
    Publisher: S. Karger AG
    Publication Date: 2018
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