• Title/Summary/Keyword: calcium ion sensitivity

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Application of Ion-Selective Electrodes to Measure Ionic Concentrations of Macronutrients in Hydroponics (수경재배 시 다량 이온 농도 측정을 위한 이온 선택성 전극의 응용)

  • Kim, Min-Su;Park, Tu-San;Cho, Seong-In
    • Journal of Biosystems Engineering
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    • v.32 no.1 s.120
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    • pp.37-43
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    • 2007
  • This study was carried out to investigate the applicability of PVC membrane-based ion-selective electrodes for macronutrients (K, Ca, and N) by measuring of potassium, calcium, nitrate ions in hydroponic nutrient solution. The capabilities of two ion-selective membranes with varying chemical compositions for each ion were evaluated in terms of sensitivity, selectivity, and lifetime to choose sensing elements suitable for measuring typical ranges of nutrient concentrations in hydroponic solutions. The selected calcium and nitrate ion-selective membranes showed effectively sensitive responses to calcium and nitrate ions with lifetimes of 25 and 15 days, respectively. The addition of a cation additive to the potassium membrane cocktail allowed its sensitivity to be increased whereas its lifetime was reduced from 30 days to 10 days.

Ca2+-regulated ion channels

  • Cox, Daniel H.
    • BMB Reports
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    • v.44 no.10
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    • pp.635-646
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    • 2011
  • Due to its high external and low internal concentration the $Ca^{2+}$ ion is used ubiquitously as an intracellular signaling molecule, and a great many $Ca^{2+}$-sensing proteins have evolved to receive and propagate $Ca^{2+}$ signals. Among them are ion channel proteins, whose $Ca^{2+}$ sensitivity allows internal $Ca^{2+}$ to influence the electrical activity of cell membranes and to feedback-inhibit further $Ca^{2+}$ entry into the cytoplasm. In this review I will describe what is understood about the $Ca^{2+}$ sensing mechanisms of the three best studied classes of $Ca^{2+}$-sensitive ion channels: Large-conductance $Ca^{2+}$-activated $K^+$ channels, small-conductance $Ca^{2+}$-activated $K^+$ channels, and voltage-gated $Ca^{2+}$ channels. Great strides in mechanistic understanding have be made for each of these channel types in just the past few years.

Diagnostic Calculation of Trace Calcium Ions in Food Using a DNA doped Sensor

  • Yang, Young-Kyun;Ly, Suw-Young
    • Journal of the Korean Applied Science and Technology
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    • v.30 no.2
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    • pp.197-203
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    • 2013
  • The diagnostic assay of calcium ion was sought using a modified sensor with square-wave stripping voltammetry (SWSV) and cyclic voltammetry (CV). In this study, simple graphite pencil was used as working, reference, and auxiliary electrodes. By coating the working electrodes with DNA, their sensitivity was very much improved, and good results were yielded. Moreover, clean seawater was used as an electrolyte solution instead of acid and base electrolytes to lessen the expenses involved in the experiment. The analytical optimum conditions were also examined. These conditions were attained at the low detection limit of $0.6ugL^1$. After that, the results were applied to drinking water of milk contain.

Structural and gelling properties of very low methoxyl pectin produced by an alkali-treatment

  • Lee, Byung-Hoo;Jung, Ho-Tak;Kim, Hyun-Seok;Yoo, Sang-Ho
    • Korean Journal of Food Science and Technology
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    • v.53 no.2
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    • pp.121-125
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    • 2021
  • Very low methoxyl pectin (VLMP) has different physical and rheological properties compared to high and low methoxyl pectins (HMP and LMP). In this study, we produced LMP and VLMP by alkaline de-esterification, and investigated the structural and textural properties. Apple peel pectin was kept at pH 12 using 5.0 M NaOH solution for 3 and 24 h to produce LMP and VLMP, respectively. The molecular weight was decreased due to the removal of an esterified group in the pectin backbones by the alkali treatment, and the VLMP showed a higher calcium ion sensitivity which leads to the production of the gel with increased hardness. The result clearly showed that VLMP has the potential to improve the texture and stability in food products depending on their degree of esterification, and this result can be applied as a functional ingredient in food industrial area application to enhance the current commercial pectins.

Ca2+ Sensitivity of Anoctamin 6/TMEM16F Is Regulated by the Putative Ca2+-Binding Reservoir at the N-Terminal Domain

  • Roh, Jae Won;Hwang, Ga Eun;Kim, Woo Kyung;Nam, Joo Hyun
    • Molecules and Cells
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    • v.44 no.2
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    • pp.88-100
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    • 2021
  • Anoctamin 6/TMEM16F (ANO6) is a dual-function protein with Ca2+-activated ion channel and Ca2+-activated phospholipid scramblase activities, requiring a high intracellular Ca2+ concentration (e.g., half-maximal effective Ca2+ concentration [EC50] of [Ca2+]i > 10 μM), and strong and sustained depolarization above 0 mV. Structural comparison with Anoctamin 1/TMEM16A (ANO1), a canonical Ca2+-activated chloride channel exhibiting higher Ca2+ sensitivity (EC50 of 1 μM) than ANO6, suggested that a homologous Ca2+-transferring site in the N-terminal domain (Nt) might be responsible for the differential Ca2+ sensitivity and kinetics of activation between ANO6 and ANO1. To elucidate the role of the putative Ca2+-transferring reservoir in the Nt (Nt-CaRes), we constructed an ANO6-1-6 chimera in which Nt-CaRes was replaced with the corresponding domain of ANO1. ANO6-1-6 showed higher sensitivity to Ca2+ than ANO6. However, neither the speed of activation nor the voltage-dependence differed between ANO6 and ANO6-1-6. Molecular dynamics simulation revealed a reduced Ca2+ interaction with Nt-CaRes in ANO6 than ANO6-1-6. Moreover, mutations on potentially Ca2+-interacting acidic amino acids in ANO6 Nt-CaRes resulted in reduced Ca2+ sensitivity, implying direct interactions of Ca2+ with these residues. Based on these results, we cautiously suggest that the net charge of Nt-CaRes is responsible for the difference in Ca2+ sensitivity between ANO1 and ANO6.

Voltage Dependent N Type Calcium Channel in Mouse Egg Fertilization

  • Eum, Jin Hee;Park, Miseon;Yoon, Jung Ah;Yoon, Sook Young
    • Development and Reproduction
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    • v.24 no.4
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    • pp.297-306
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    • 2020
  • Repetitive changes in the intracellular calcium concentration ([Ca2+]i) triggers egg activation, including cortical granule exocytosis, resumption of second meiosis, block to polyspermy, and initiating embryonic development. [Ca2+]i oscillations that continue for several hours, are required for the early events of egg activation and possibly connected to further development to the blastocyst stage. The sources of Ca2+ ion elevation during [Ca2+]i oscillations are Ca2+ release from endoplasmic reticulum through inositol 1,4,5 tri-phosphate receptor and Ca2+ ion influx through Ca2+ channel on the plasma membrane. Ca2+ channels have been characterized into voltage-dependent Ca2+ channels (VDCCs), ligand-gated Ca2+ channel, and leak-channel. VDCCs expressed on muscle cell or neuron is specified into L, T, N, P, Q, and R type VDCs by their activation threshold or their sensitivity to peptide toxins isolated from cone snails and spiders. The present study was aimed to investigate the localization pattern of N and P/Q type voltage-dependent calcium channels in mouse eggs and the role in fertilization. [Ca2+]i oscillation was observed in a Ca2+ contained medium with sperm factor or adenophostin A injection but disappeared in Ca2+ free medium. Ca2+ influx was decreased by Lat A. N-VDCC specific inhibitor, ω-Conotoxin CVIIA induced abnormal [Ca2+]i oscillation profiles in SrCl2 treatment. N or P/Q type VDC were distributed on the plasma membrane in cortical cluster form, not in the cytoplasm. Ca2+ influx is essential for [Ca2+]i oscillation during mammalian fertilization. This Ca2+ influx might be controlled through the N or P/Q type VDCCs. Abnormal VDCCs expression of eggs could be tested in fertilization failure or low fertilization eggs in subfertility women.

Presenilin Modulates Calcium-permeant, Magnesium-Nucleotide regulated channel, I(MgNUM)

  • Shin, Sun-Young;Jeong, Soon-Youn;Uhm, Dae-Yong;Sungkwon Chung
    • Proceedings of the Korean Biophysical Society Conference
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    • 2003.06a
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    • pp.47-47
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    • 2003
  • The presenilin 1 (PS1) or PS2 is an essential component of the ${\gamma}$-secretase complex, which mediates the intramembrane proteolysis of selected type-I membrane, including the ${\beta}$-amyloid precursor protein (APP) to yield A${\beta}$. Familial Alzheimer's disease (FAD)-associated mutations in presenilins give rise to an increased production of a highly amyloidogenic A${\beta}$42. In addition to their well-documented proteolytic function, the presenilins play a role in calcium signaling. We have previously reported that presenilin FAD mutations cause highly consistent alterations in intracellular calcium signaling pathways, which include deficits in capacitative calcium entry (CCE), the refilling mechanism for depleted internal calcium stores. However, molecular basis for the presenilin-mediated modulation of CCE remains to be elucidated. In the present study, whole-cell patch clamp method was used to identify a specific calcium-permeable ion channel current(s) that is responsible for the CCE deficits associated with FAD-linked PS1 mutants. Unexpectedly, both voltage-activated and conventional store depletion-activated calcium currents I(CRAC), were absent in HEK293 cells, which were stably transfected either with wild-type or FAD mutant (L286V, M146L, and delta E9) forms of PS1. Recently, magnesium-nucleotide-regulated metal cation current, or I(MagNum), has been described and appears to share many common properties with I(CRAC) including calcium permeability and inhibitor sensitivity (e.g. 2-APB). We have detected I(MagNum) in all 293 cells tested. Interestingly, FAD mutant 293 cells developed only about half of currents compared to PS1 wild type cells.

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Therapeutic Effect of Toothpaste Containing Hydroxyapatite and Tribasic Calcium Phosphate on Dentinal Hypersensitivity (치아 과민증에 Hydroxyapatite와 Tricalcium phosphate을 함유한 치약의 치료효과)

  • Choi, Yea Hun;Park, Hyean Cheal;Lee, Sang Mong;Son, Hong Joo;Choi, Eun Bi;Ha, Jun Young;Lee, Jun Young;Kim, Keun Ki
    • Journal of Life Science
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    • v.24 no.6
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    • pp.642-647
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    • 2014
  • Although it is not a pathological symptom, Dentinal Hypersensitivity (DH) describes pain felt by patients whose tooth roots are exposed outside of the gums and are therefore sensitive to external stimuli. DH is caused by tooth brushing or gum diseases and treatment to reduce the sensitivity can include use of materials having stimulation activity for DH or a resin material applied periodontally. This study examined the hypersensitivity treatment effects of a four-week treatment with a toothpaste containing hydroxyapatite and tricalcium phosphate (Hap-TCP toothpaste). The Hap-TCP toothpaste was made by mixing a commercially available fluorine-containing toothpaste with 10% (W/W) hydroxyapatite and 19% (W/W) tricalcium phosphate (both 99% purity based on XRD analysis). The tooth hypersensitivity treatment effect was surveyed by scoring VRS values, and showed no significant initial difference compared with the control. However, after 1 week of use, the pain reduction value was 8% in the treatment group compared to the control group. This value increased to 30% and 60% after 2 and 4 weeks, respectively. Hypersensitivity to cold stimulation, which was used as a VAS value, showed no initial significant differences compared with the control, but was significantly decreased after 1, 2, and 4 weeks in the experimental group, with more than a 3-fold difference after 4 weeks. These findings confirmed that remineralization can alleviate DH as hydroxyapatite fills dentinal tubules and calcium, phosphorus, and tricalcium phosphate ion equilibrium is established.

Effect of pH Change on Vascular Smooth Muscle Contractility in Rat Superior Mesenteric Artery and Its Branches (쥐 상장간막 동맥과 그 분지에서 pH 변화가 혈관평활근 수축성에 미치는 영향)

  • Choi, Soo-Seung
    • Journal of Chest Surgery
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    • v.43 no.4
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    • pp.345-355
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    • 2010
  • Background: Extracellular and intracellular pH ($pH_o$ and $pH_i$), which can be changed in various pathological conditions such as hypoxia, affects vascular contractility. To elucidate the mechanism to alter vascular contractility by pH, the effects of pH on reactivity to vasocontracting agents, intracellular $Ca^{2+}$ influx, and $Ca^{2+}$ sensitivity in vascular smooth muscle were examined. Material and Method: Isometric contractions in rat superior mesenteric arteries (SMA) were observed. Intracellular $Ca^{2+}$ concentration ($[Ca^{2+}]_i$) was recorded by microfluorometer using Fura-2/acetoxylmethyl ester in muscle cells. $pH_o$ was increased from 7.4 to 7.8 or decreased to 6.9 or 6.4. $pH_i$ was decreased by applying $NH_4^+$ or propionic acid or modulated by changing $pH_o$ after increasing membrane permeability using $\beta$-escin. Result: Decreases in $pH_o$ from 7.4 to 6.9 or 6.4 shifted concentration-response curve by norepinephrine (NE) or serotonin (SE) to the right and significantly increased half maximal effective concentration (EC50) to NE or SE. Increase in $pH_o$ from 7.4 to 7.8 shifted concentration-response curve by norepinephrine (NE) or serotonin (SE) to the left and significantly reduced EC50 to NE or SE. NE increased $[Ca^{2+}]_i$ in cultured smooth muscle cells from SMA and the increased $[Ca^{2+}]_i$ was reduced by decreases in $pH_o$. NE-induced contraction was inhibited by $NH_4^+$, whereas the resting tension was increased by $NH_4^+$ or propionic acid. When the cell membrane of SMA was permeabilized using ${\beta}$-escin, SMA was contracted by increasing extracellular $Ca^{2+}$ concentration from 0 to $10{\mu}M$ and the magnitude of contraction was decreased by a decrease in $pH_o$ and vice versa. Conclusion: From these results, it can be concluded that a decrease in $pH_o$ might inhibit vascular contraction by reducing the reactivity of vascular smooth muscle to vasoactive agents, $Ca^{2+}$ influx and the sensitivity of vascular smooth muscle to $Ca^{2+}$.