• Journal of Biosystems Engineering
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• 제32권1호
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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.

• BMB Reports
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• 제44권10호
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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.

• 한국응용과학기술학회지
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• 제30권2호
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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.

• 한국식품과학회지
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• 제53권2호
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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.

• Molecules and Cells
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• 제44권2호
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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.

• 한국발생생물학회지:발생과생식
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• 제24권4호
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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.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2003년도 정기총회 및 학술발표회
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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.

• 생명과학회지
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• 제24권6호
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• pp.642-647
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• 2014

치아과민증은 치아의 병적인 증세는 아니지만 치아뿌리가 잇몸밖으로 노출되어 외부의 자극에 대한 민감한 반응으로 환자가 통증을 느끼는 것을 말한다. 칫솔질이나 잇몸질환 등의 다양한 원인이 있으며 치료를 위해서는 자극을 줄여 주는 방법으로 치아과민치료활성이 있는 물질을 이용하거나 레진으로 들어난 치주를 도포하는 방법이 있다. 본 연구에서 수산화인회석과 인산삼칼슘을 혼합하여 만든 치약과 시중에 판매하고 있는 불소함유치약을 4주간 사용하면서 치주과민성 치료효과를 비교 조사하였다. 첨가한 수산화인회석과 인산삼칼슘의 순도는 XRD분석결과 99% 이상으로 나타났으며, 제조한 치약(Hap-TCP)에는 각각 10%와 19%(W/W) 되게 첨가하였다. 치아과민성 치료효과를 VRS값으로 조사한 결과 사용직후에는 대조군과 차이가 없었으나, 1주후에는 대조군에 비해 8% 통증감소효과가 나타났고, 2주와 4주 후에는 각각 30%와 60%정도 통증감소효과가 나타났다. 그리고 냉자극에 대한 지각과민증을 VAS값으로 조사한 결과도 초기에는 차이가 없었으나, 1주, 2주, 4주 후에 측정한 결과 기간에 따라 유의적으로 감소하였다. 4주후에는 VAS값이 3배이상 차이를 보였다. 이 결과는 현미경관찰에서도 확인이 되어진 것과 같이 수산화인회석이 확장된 상아세관들을 메우고, 구강내의 칼슘, 인 등 이온평형을 인산삼칼슘이 조절하여 메워진 상아세관을 안정적으로 자리를 잡도록 도와주는 재석회화현상으로 치아과민증상을 완화하는 것으로 확인되었다.

• Journal of Chest Surgery
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• 제43권4호
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• pp.345-355
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• 2010

산성화를 초래하는 Hypoxia 등 여러 가지 조건에서 변화하는 세포외 pH 변화는 궁극적으로 세포내 pH 변화를 유발하며 세포 내외 pH 변화는 혈관평활근 수축성 변화를 유발한다. 이러한 세포 내외 pH 변화에 의한 혈관 수축성 변화 기전을 규명하고자, pH 변화가 혈관수축인자들에 의한 혈관평활근 수축, 혈관평활근세포내 $Ca^{2+}$ 농도, 그리고 혈관평활근의 $Ca^{2+}$에 대한 민감도에 미치는 영향을 알아보고자 하였다. 대상 및 방법: 쥐에서 분리한 상장간막동맥과 그 분지에서 등장성 수축을 기록하였으며 배양한 상장간막동맥 세포에서 세포내 $Ca^{2+}$ 변화를 측정하였다. 세포외 pH는 정상인 7.4에서 6.4, 6.9 혹은 7.8로 변화시켰으며, 세포내 pH 변화는 propionic acid나 $NH_4$를 투여하거나 ${\beta}$-escin으로 세포막의 투과성을 증가시켜 세포외 용액의 pH 변화로 유발시켰다. 결과: 세포외 pH를 7.4에서 6.9, 6.4로 감소시키면 노에피네프린과 세로토닌에 의한 용량-반응 곡선이 우측 이동하였으며 최대 수축력의 50% 수축력을 유발하는 농도(half maximal effective concentration)가 증가하였고, pH를 7.8로 증가시키면 그 반대 현상이 일어났다. 노에피네프린은 배양한 혈관평활근세포에서 세포내 $Ca^{2+}$ 농도를 증가시켰으며, 이 세포내 $Ca^{2+}$ 증가는 세포외 pH 감소에 의하여 억제되었으며 세포외 pH 증가에 의하여 증가하였다. 노에피네프린에 의한 수축은 세포내 pH를 감소시키는 $NH_4$에 의하여 억제된 반면, 안정 장력은 $NH_4$과 propionic acid에 의하여 증가하였다. ${\beta}$-escin으로 세포막의 투과도를 증가시킨 후 세포외 용액의 $Ca^{2+}$ 농도를 증가시켜 수축을 유발시킨 후 세포외 용액의 pH를 변화시키면 pH 감소에 의하여 수축력이 감소하였으며 증가에 의하여 수축력이 증가하였다. 결론: 세포외 pH의 감소는 혈관평활근의 수축성을 감소시키는데 이는 세포외 pH 감소에 의한 혈관평활근의 혈관수축물질에 대한 반응성 감소, 혈관평활근 세포내 $Ca^{2+}$ 유입 억제 그리고 $Ca^{2+}$에 대한 혈관평활근의 민감성 감소에 의하여 일어난 것으로 추정할 수 있었다.