• The Plant Pathology Journal
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• 제32권3호
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• pp.242-250
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• 2016

The aim of this study was to investigate antifungal activity of a range of different molecular weight (MW) chitosan against Penicillium italicum. Our results demonstrate that the antifungal activity was dependent both the MW and concentration of the chitosan. Among a series of chitosan derived from the hydrolysis of high MW chitosan, the fractions containing various sizes of chitosan ranging from 3 to 15 glucosamine units named as chitooligomers-F2 (CO-F2) was found to show the highest antifungal activity against P. italicum. Furthermore, the effect of CO-F2 toward this fungus was significantly reduced in the presence of $Ca^{2+}$, whereas its effect was recovered by ethylenediaminetetraacetic acid, suggesting that the CO-F2 acts via disruption of $Ca^{2+}$ gradient required for survival of the fungus. Our results suggest that CO-F2 may serve as potential compounds to develop alternatives to synthetic fungicides for the control of the postharvest diseases.

• 한국식품영양과학회지
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• 제18권1호
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• pp.123-130
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• 1989

방어로부터 추출한 근원섬유 현탁액을 $0^{\circ}C$(빙장), $-3.5^{\circ}C$(PF저장), $-20^{\circ}C$(동결저장)에 저장하면서 Ca-과 Mg-ATPase활성을 측정하여 근육단백질의 변성을 조사하였으며 일부는 생선을 각 온도에 일정기간 저장한 후 근원섬유를 추출하여 단백질 변성정도를 비교한 결과 추출한 근원섬유를 저장하였을 때 빙장 및 PF저장한 시료의 ATPase활성은 비슷한 수준이었으나 동결 저장한 시료에서는 현저히 낮았다. 생선을 각 온도에 1주일간 저장한 후 추출한 근원섬유의 소활성은 근원섬유를 미리 추출하여 같은 기간동안 저장한 경우에 비하여 빙장과 PF저장에서는 1.2-1.8배, 동결저장에서는 2.5-3배 정도 높은 수준을 유지하고 있었다. 근원섬유를 각 온도에 저장하였을 때의 변성속도는 Ca-의 경우가 Mg-ATPase에 비 해 2-3배 빨랐으나 생선으로 저장한 경우에는 Ca-과 Mg-ATPase간에 큰 차이를 나타내지 않았다.

• Molecules and Cells
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• 제39권2호
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• pp.149-155
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• 2016

In the heart, excitation-contraction (E-C) coupling is mediated by $Ca^{2+}$ release from sarcoplasmic reticulum (SR) through the interactions of proteins forming the $Ca^{2+}$ release unit (CRU). Among them, calsequestrin (CSQ) and histidine-rich $Ca^{2+}$ binding protein (HRC) are known to bind the charged luminal region of triadin (TRN) and thus directly or indirectly regulate ryanodine receptor 2 (RyR2) activity. However, the mechanisms of CSQ and HRC mediated regulation of RyR2 activity through TRN have remained unclear. We first examined the minimal KEKE motif of TRN involved in the interactions with CSQ2, HRC and RyR2 using TRN deletion mutants and in vitro binding assays. The results showed that CSQ2, HRC and RyR2 share the same KEKE motif region on the distal part of TRN (aa 202-231). Second, in vitro binding assays were conducted to examine the $Ca^{2+}$ dependence of protein-protein interactions (PPI). The results showed that TRN-HRC interaction had a bell-shaped $Ca^{2+}$ dependence, which peaked at pCa4, whereas TRN-CSQ2 or TRN-RyR2 interaction did not show such $Ca^{2+}$ dependence pattern. Third, competitive binding was conducted to examine whether CSQ2, HRC, or RyR2 affects the TRN-HRC or TRN-CSQ2 binding at pCa4. Among them, only CSQ2 or RyR2 competitively inhibited TRN-HRC binding, suggesting that HRC can confer functional refractoriness to CRU, which could be beneficial for reloading of $Ca^{2+}$ into SR at intermediate $Ca^{2+}$ concentrations.

• The Korean Journal of Physiology and Pharmacology
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• 제24권3호
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• pp.277-286
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• 2020

Polycystic kidney disease 2-like-1 (PKD2L1), also known as polycystin-L or TRPP3, is a non-selective cation channel that regulates intracellular calcium concentration. Calmodulin (CaM) is a calcium binding protein, consisting of N-lobe and C-lobe with two calcium binding EF-hands in each lobe. In previous study, we confirmed that CaM is associated with desensitization of PKD2L1 and that CaM N-lobe and PKD2L1 EF-hand specifically are involved. However, the CaM-binding domain (CaMBD) and its inhibitory mechanism of PKD2L1 have not been identified. In order to identify CaM-binding anchor residue of PKD2L1, single mutants of putative CaMBD and EF-hand deletion mutants were generated. The current changes of the mutants were recorded with whole-cell patch clamp. The calmidazolium (CMZ), a calmodulin inhibitor, was used under different concentrations of intracellular. Among the mutants that showed similar or higher basal currents with that of the PKD2L1 wild type, L593A showed little change in current induced by CMZ. Co-expression of L593A with CaM attenuated the inhibitory effect of PKD2L1 by CaM. In the previous study it was inferred that CaM C-lobe inhibits channels by binding to PKD2L1 at 16 nM calcium concentration and CaM N-lobe at 100 nM. Based on the results at 16 nM calcium concentration condition, this study suggests that CaM C-lobe binds to Leu-593, which can be a CaM C-lobe anchor residue, to regulate channel activity. Taken together, our results provide a model for the regulation of PKD2L1 channel activity by CaM.

• 한국세라믹학회지
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• 제37권5호
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• pp.453-458
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• 2000

Glasses showing the composition of blast furnace slag were made in the laboratory, and the effect of the chemical composition on the latent hydraulic activity of the slags was examined. The latent hydraulicity was greatly influenced by the composition change, the optimal characteristic of the hydraulicity was achieved at the slag composition of 47CaO:20Al2O3:33SiO2. The content of CaO and Al2O3 were not equivalent to the hydraulic activity of the slags as the b-formula (KS L 5210) indicates. Good latent hydraulicity was shown when Al2O3 was richly contained at the high (CaO＋Al2O3):SiO ratio, while the more the MgO content was, the more negative the result turned out.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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• pp.61-62
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• 1999

;The mechanisms inducing hypertension are actively investigated and are still challenging topics. Basically hypertension must be caused by the disorder of $Ca^{2+}$ metabolism in vascular smooth muscle, such as the increase of $Ca^{2+}$ influx, the decrease of ci+ efflux, or the change of sensitivity of contractile protein etc. The one of cause of the increase of ci+ influx may be the change of ci+ channel activity. Even though the relationships of ci+ channel activity and hypertension were studied using various hypertension models, still it is not clear how much change of $Ca^{2+}$ channel activity in diabetes mellitus (DM) induced hypertension is occurred. We induced DM hypertension in SD rat and compared the $Ca^{2+}$ channel activity with age-matched normotensive SD rat. For inducing DM hypertension, left kidney was removed with 200 gm rat and, after 1 month, 60 mg/kg of streptozotocin was injected into peritoneal space to induce diabetes mellitus. Usually after 4-6 weeks, hypertension was fully induced. For isolating vascular smooth muscle cells (VSMC), we used mesenteric arteriole (3rd - 4th branch of mesenteric artery) of which diameter is below 150 urn. VSMCs were isolated enzymatically. $Ca^{2+}$ current was measured using whole cell patch clamp technique. All experiments were performed at $37^{\circ}C$. The cell membrane area of VSMC of DM hypertensive rat is larger than that of control VSMC($36.6{\pm}3.64{\;}pF{\;}vs{\;}22.4{\pm}1.29{\;}pF, {\;}mean{\pm}S.E.$) When we compared the current amplitude, the $Ca^{2+}$ current amplitude in VSMC of DM hypertensive rat is much larger than that in VSMC of normotensive age-matched rat. After $Ca^{2+}$ current amplitude was normalized by cell membrane area, the current amplitude in DM hypertension is increased to $249.1{\pm}15.9{\;}%{\;}(mean{\pm}S.E.M)$, which means the ;absolute current amplitude is about 4 times larger in DM hypertension. When we compared the steady state activation and inactivation. there were no noticeable differences. From these results. one of cause of the DM hypertension is due to the increase of $Ca^{2+}$ current amplitude. But it need further study why the $Ca^{2+}$ current is so large in VSMC of DM hypertension and how much $Ca^{2+}$ influx through $Ca^{2+}$ channel contribute to the increase of intracellular $Ca^{2+}$ and eventually contribute to development of hypertension.ypertension.

• Archives of Pharmacal Research
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• 제18권6호
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• pp.391-395
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• 1995

Several lines of evidence indicate that physiological activity of N-methyl-D-aspartate (NMDA) receptor was blocked by physiological concentration of $Mg^{2+}$ (1.2 mM). However, the activity of NMDA receptor may not be blocked totally with this concentration of $Mg^{2+}$ under elevated membrane potential by kainate. Here, we described the effect of $Mg^{2+}$ on NMDA receptor and how much of NMDA receptor functions could be activated by kainate. Effects of NMDA receptor antagonist on kainate-induced elevation of intracellualr $Ca^{2+}$ levels $([Ca^{2+}]_i)$ and extracellular glutamate level were examined in cultured rat cerebellar granule neurons. kainate-induced elevation of $([Ca^{2+}]_i)$ was not affected by physiological concentration of $Mg^{2+}$. Kainate-induced NMDA-induced elevation was blocked by the same concentration of $MG^{2+}$Kainate-induced elevation of [$([Ca^{2+}]_i)$ was decreased by 32% in the presence of NMDA antagonists, MK-801 and CPP (3-[2-carboxypiperazine-4-yl]propyl-1-phosphonic acid), in $Mg^{2+}$ free buffer. Kainate receptor-activated gluamate release was also decreased (30%) by MK-801 or CPP. These resuts show that certain extent of elevations of intracellular $Ca^{2+}$ and extracellular glutamate by kainate is due to coativation of NMDA receptors.

• 한국동물학회지
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• 제14권2호
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• pp.43-56
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• 1971

筋小胞體의 Ca 吸收能과 ATPase 活性을 各種 濃度의 K, Mg, caffeine, procaine, 및 quinine 존재하에서 측정하였다. ATP不在下에서 Ca吸收能은 K 또는 Mg의 농도가 증가함에 따라 低下된다. 그러나 ATP 존재하에서의 Ca吸收能은 K의 농도에는 거의 영향을 받지 않고, Mg의 농도가 증가함에 따라 현저히 증가한다. Caffeine과 procaine은 ATP 존재하의 Ca吸收能을 阻害하지만 quinine은 阻害하지 않는다. ATPase 活性은 K의 농도에는 영향을 받지 않으나 Mg의 존재에 의하여 증가된다. Caffeine, procaine 및 quinine은 이 活性에 거의 영향을 미치지 않는다.

• The Korean Journal of Physiology and Pharmacology
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• 제3권2호
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• pp.199-205
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• 1999

Vibrio vulnificus cytolysin caused platelet cytolysis and increased intracellular calcium concentration $([Ca^{2+}]_i)$ of rat platelets in a concentration-dependent manner. In the presence of V. vulnificus cytolysin (3 HU/ml), lactate dehydrogenase (LDH) activity was increased from $1.3{\pm}0.4%$ of control to $64.3{\pm}3.4%$ in platelet suspension buffer. In $Ca^{2+}-free$ platelet suspension buffer, however, V. vulnificus cytolysin did not induce $[Ca^{2+}]_i$ increase and LDH release. Addition of EGTA (2 mM) to suspension buffer after the initial $Ca^{2+}$ influx reversed $[Ca^{2+}]_i$ to the control level. However, a $Ca^{2+}$ channel blocker verapamil $(20\;{\mu}M)$ or mefenamic acid $(20\;{\mu}M)$ did not inhibit V. vulnificus cytolysin-induced $[Ca^{2+}]_i$ increase and LDH release. Divalent cations such as $Co^{2+},\;Cd^{2+}\;or\;Mn^{2+}$ (2 mM each) also did not alter V. vulnificus cytolysin-induced $[Ca^{2+}]_i$ increase and LDH release. V. vulnificus cytolysin (3 HU/ml)-induced calcium influx was completely blocked by lanthanum (2 mM). Lanthanum (2 mM) also completely blocked V. vulnificus cytolysin (3 HU/ml)-induced LDH release. Osmotic protectants such as, raffinose, sucrose or PEG600 (50 mM each) did not inhibit the lytic activity of V. vulnificus cytolysin. In conclusion, lanthanum sensitive $Ca^{2+}$ influx plays a significant role in Vibrio vulnificus cytolysin-induced platelet cytolysis and thrombocytopenia in V. vulnificus infection.

• Journal of Photoscience
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• 제3권3호
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• pp.133-136
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• 1996

Calcium modulates the activity of guanylate cyclase and plays a key role in dark and light adaptation in the visual system. We have measured the Ca$^{2+}$, K$^+$ and Na$^+$ concentration in dark and light adapted bullfrog's (Rana catesbeiana) vitreous humor by using the atomic absorption spectrophotometer. The calcium concentration of the light adapted bullfrog's vitreous humor was higher than that of the dark adapted bullfrog's vitreous humor. This means that ion activity between the photoreceptor and vitreous humor side is light dependent and we have found that a Ca$^{2+}$ channel and Na$^+$ - Ca$^{2+}$ exchanger exist in the vitreous humor.