• The Korean Journal of Physiology and Pharmacology
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• v.22 no.2
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• pp.215-223
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• 2018

Intracellular $Ca^{2+}$ mobilization is closely linked with the initiation of salivary secretion in parotid acinar cells. Reactive oxygen species (ROS) are known to be related to a variety of oxidative stress-induced cellular disorders and believed to be involved in salivary impairments. In this study, we investigated the underlying mechanism of hydrogen peroxide ($H_2O_2$) on cytosolic $Ca^{2+}$ accumulation in mouse parotid acinar cells. Intracellular $Ca^{2+}$ levels were slowly elevated when $1mM\;H_2O_2$ was perfused in the presence of normal extracellular $Ca^{2+}$. In a $Ca^{2+}-free$ medium, $1mM\;H_2O_2$ still enhanced the intracellular $Ca^{2+}$ level. $Ca^{2+}$ entry tested using manganese quenching technique was not affected by perfusion of $1mM\;H_2O_2$. On the other hand, $10mM\;H_2O_2$ induced more rapid $Ca^{2+}$ accumulation and facilitated $Ca^{2+}$ entry from extracellular fluid. $Ca^{2+}$ refill into intracellular $Ca^{2+}$ store and inositol 1,4,5-trisphosphate ($1{\mu}M$)-induced $Ca^{2+}$ release from $Ca^{2+}$ store was not affected by $1mM\;H_2O_2$ in permeabilized cells. $Ca^{2+}$ efflux through plasma membrane $Ca^{2+}-ATPase$ (PMCA) was markedly blocked by $1mM\;H_2O_2$ in thapsigargin-treated intact acinar cells. Antioxidants, either catalase or dithiothreitol, completely protected $H_2O_2-induced$ $Ca^{2+}$ accumulation through PMCA inactivation. From the above results, we suggest that excessive production of $H_2O_2$ under pathological conditions may lead to cytosolic $Ca^{2+}$ accumulation and that the primary mechanism of $H_2O_2-induced$ $Ca^{2+}$ accumulation is likely to inhibit $Ca^{2+}$ efflux through PMCA rather than mobilize $Ca^{2+}$ ions from extracellular medium or intracellular stores in mouse parotid acinar cells.

• The Zoological Society Korea : Newsletter
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• v.12 no.2
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• pp.124.2-124
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• 1995

No Abstract, See Full Text

• The Korean Journal of Zoology
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• v.38 no.1
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• pp.10-19
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• 1995

동면동물인 한국관박쥐(Korean greater horseshoe bat)와 비롱면 롱물인 토끼의 근소포체가 지니는 생리 및 근조직의 형태적 특징을 비교해 보고자 본 실험을 수행하여 다음과 같은 결론을 내렸다 Caffeine과 Mgcl2는 농도별로 처리하고, p연와 온도에 변화를 주는 등 각각의 생리조건하에서 한국관박쥐와 토끼 대흉근 근소포체 마이크로솜의 C32' 흡수정도가 다르게 나타났으며, Ca2'ATPase 활성 역시 상이함을 보였는데. 이로 미루어 보아 in vivo 상태에서 두 동물의 근소포체가 지니는 생리적 특성에 차이가 있을 것으로 추측된다. 형태학적 측면에서도 근심유의 수기와 미토콘드리아의 크기에 있어서 뚜렷한 차이를 발견할 수 있었는데. 이는 두 동물의 대흉근이 수행하는 운동의 종류와 관련이 있을 것으로 생각된다.

• The Korean Journal of Mycology
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• v.19 no.3
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• pp.220-225
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• 1991

Activities of the $F_1-ATPase$ purified from Lentinus edodes were stimulated by $Fe^{3+},\;Fe^{2+},\;Cd^{2+},\;Mg^{2+},\;K^{+}\;and\;Co^{2+}$ but were inhibited by $Zn^{2+},\;Ca^{2+},\;Cu^{2+}\;and\;Ni{2+}$ ion. The enzyme activities were increased 130, 65, 65, 68, 105% and 23% by the 5mM $Fe^{3+}$, 10 mM$Fe^{2+}$, 1mM $Cd^{2+}$, 5mM $Mg^{2+}$, 5mM $K^{+}$ and 5mM$Co^{2+}$ ion addition, respectively, as compared with those not added. The enzyme activities were decreased 18, 19, 27 and 30% by 10 mM $Zn^{2+}$, 10mM $Ca^{2+}$, 0.5 mM $Cu^{2+}$ and 10 mM $Ni^{2+}$ ion, respectively. Anion effects of 10 mM ${Co_3}^{2-}$, 20 mM,$CN^{-}$ 20 mM$CH_3COO^{-}$ and 20 mM ${NO_3}^{-}$ ion were inhibited to the enzyme activities of 98, 95, 70 and 50%, respectively. As increasing of ${SO_4}^{2-}$ ion concentration, the enzyme activity was stimulated and 20 mM ${SO_4}^{2-}$ ion was shown increased of 21%.

• Korean Journal of Plant Resources
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• v.30 no.6
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• pp.647-653
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• 2017

Hepatic ischemia-reperfusion injury (HIRI) is linked with high mortality rate. Several agents have been developed so far to reduce the risk of HIRI. In this study, we investigated the effects of Acanthopanax senticosus extract (AS) on hepatic ischemia-reperfusion. To explore the protective effects of A. senticosus extract injection (ASI) on hepatic ischemia-reperfusion injury rats animal model were used. After the development of HIRI by using clamping method rats were then randomly divided into five groups. Different doses of AS were administered in HIRI rat model. The level of ALT, AST, and MDA content in serum were detected in sham and HIRI groups. The activity of SOD, MPO and $Ca^{2+}-ATPase$, content of MDA, and cAMP in hepatic tissue were also measured. Expression of Bcl-2 and Bax protein were detected by immunohistochemical staining method. Compared with sham group, ASI has the protective effect on the HIRI model in rats. Blood levels of ALT, AST, SOD, MPO, and MDA were significantly lower in ASI group compared with HIRI. Indeed SOD and $Ca^{2+}-ATPase$ activities, MDA content, and cAMP level were improved in ASI group. Furthermore, Bcl-2 and Bax protein were improved in ASI group compared with only HIRI group. These results suggest that AS may provide potential ameliorative therapy by inhibiting the damage signaling mechanism in hepatic ischemia/reperfusion injury model.

• Journal of Aquaculture
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• v.17 no.3
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• pp.167-172
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• 2004

Chemoenzymatic method was used in this study to evaluate the quality of cultured red seabrim. Level of ATP related compounds, ATPase and Adenylate energy charge (AEC) well reflected changes in condition of fish. ATP level in the muscle of exercised cultured red seabream was decreased significantly during cultured period. In contrast, the level of ADP in the muscle was increased during the period. Level of ATP related compounds in the muscle of cultured red seabream without exercise didn't show significant difference compared to the exercised group. AEC value in muscle of cultured red seabream without exercise was 0.89$\pm$0.02, while AEC value of the exercised group was 0.88$\pm$0.04. ATP and AEC levels among different size of fish did not show any significant difference. AEC value in all sample was higher than 0.8, indicating that the condition of cultured fish was healthy. Activity of Mg2$^{＋}$ (＋Ca2$^{＋}$), Mg2$^{＋}$ (-Ca2$^{＋}$) and Ca2$^{＋}$-ATPase during culture period did not change significantly, regardless of exercise. Therefore, the AEC appears to have some validity as fish health indicator.

• Proceedings of the Zoological Society Korea Conference
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• 1995.10b
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• pp.260.2-260
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• 1995

No Abstract, See Full Text

• The Korean Journal of Pharmacology
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• v.24 no.2
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• pp.179-187
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• 1988

Verapamil, tetrodotoxin and tetraethylammonium chloride in the stated amount did not affect the $Na^{++}$ induced $Ca^{++}$ release. $Cd^{++}$ and $Zn^{++}$ significantly inhibited the $Na^{++}$ induced $Ca^{++}$ release. $Mn^{++}$ also inhibited $Na^+-Ca^{++}$ exchange. $Cd^{++}$ inhibited $Na^+-Ca^{++}$ exchange noncompetitively with an apparent inhibition constant (Ki) of $100\;{\mu}M$. $Cd^{++}$ caused loss of sulfhydryl group, whereas $Zn^{++}$ did not show any significant effect. $Cd^{++}$ and $Zn^{++}$ effectively inhibited $Na^+-Ca^{++}$ ATPase and slightly inhibited $Ca^{++}-Mg^{++}$ ATPase. Carbonyl cyanide chlorophenylhydrazone, 2,4-dinitrophenol and sodium arsenate stimulated the $Na^{++}$ induced $Ca^{++}$ release. Dibucaine and oligomycin slightly inhibited it. The results suggest that the $Na^+-Ca^{++}$ exchange on the synaptosomal plasma membrane may be not accomplished by ion channels. The $Na^+-Ca^{++}$ exchange is sensitively inhibited by $Cd^{++}$ and this transport process appears to be partially regulated by sulfhydryl groups of the synaptosomal plasma membrane. It is also postulated that $Na^+-Ca^{++}$ exchange is suppressed during the phosphorylation reaction of protein component on the neuronal membrane.

• Journal of the Korean Society of Food Science and Nutrition
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• v.14 no.1
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• pp.82-87
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• 1985

Some biological activities showed as ATPase activity of myofibril, actomyosin and myosin extracted from chicken leg and pectoral skeletal muscle were investigated. The $Mg^{+2}$-ATPase activity at 0.05 M KCl were 0.82, 0.38 and 0.11 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle while 0.71, 0.32 and 0.08 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from leg muscle. EDTA-ATPase activity at 0.6M KCl were 0.80, 0.42 and 0.40 ${\mu}mole$ Pi/mg protein/min. in actomyosin, myofibril and myosin from pectoral muscle. In case of leg muscle, that activity was noted as 0.69, 0.33 and 0.28 ${\mu}mole$e Pi/mg protein/min in proteins. ATPase activity of myosin from leg and pectoral muscle were inhibited in 10% at a higher concentration of $Mg^{+2}$ than molar concentration of EDTA, and the ATPase activity was increased to 400% compared with control at $10^{-3}M$ of $Ca^{+2}$. Actomyosin from pectoral muscle was solubilized at 0.1 M KCl above and that from leg muscle was solubilized at 0.15 M KCl above. In case of myosin, pectoral muscle was solubilized at 0.25M KCI above and leg muscle was solubilized at 0.30M KCl above.

• Development and Reproduction
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• v.1 no.1
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• pp.45-56
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• 1997

Befor fertilization, mammalian oocytes undergo meiotic maturation, which consists of nuclear and cytoplasmic differentiation. In this study, changes of $Ca^{2+}$ stores in mouse oocytes were examined during meiotic maturation and the role of $Ca^{2+}$ in the regulation of the maturation was investigated by using monoclonal antibodies against smooth endoplasmic reticulum $Ca^{2+}$-ATPase(SERCA-ATPase) and calreticulin. Observations were made under epifluorescence microscope and/or confocal laser scanning microscope. In immature oocytes which did not resume meiotic maturation, SERCA-ATPases were mostly localized in the vicinity of the germinal vesicle and calreticulins were distributed evenly throughout the cytoplasm. In mature oocytes, SERCA-ATPases were observed throughout the cytoplasm, butwere absent from the nuclear region. In contrast, calreticulins were localized mostl in the cortex of the oocyte and were absent from the cytoplasm. However, bright fluoresence stainings were wbserved in the perimeiotic spindle region of mature oocyte when labeled with antibodies against calreticulin. These results indicate that mouse oocytes undergo distinct rearrangement of the localization of $Ca^{2+}$-ATPases and calreticulins during meiotic maturation. Thus it can be suggested that redistribution of the $Ca^{2+}$ stores, as revealed by differential fluorescence stainings, is deeply involved in the regulatory mechanism of mammalian oocyte maturation.