• 제목/요약/키워드: Ca-ATPase

검색결과 233건 처리시간 0.035초

Protective effect of green tea extract on doxorubicin induced cardiotoxicity in rats

  • Patil, Leena;Balaraman, R.
    • Advances in Traditional Medicine
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    • 제5권2호
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    • pp.137-143
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    • 2005
  • Doxorubicin induces oxidative stress leading to cardiotoxicity causing electrocardiogram abnormalities and increases in biomarkers associated with toxicity. Green tea extract (GTE) is reported to possess antioxidant activity mainly via its polyphenolic constituent, catechins. This study was intended to determine the effect of various doses of GTE (25, 50 and 100 mg/kg/day p.o. for 30 days) on doxorubicin-induced electrocardiographic and biochemical changes in rat heart. The latter included lactate dehydrogenase, creatine kinase, and glutamic oxaloacetate transaminase in serum and superoxide dismutase, catalase, and reduced glutathione, as well as membrane bound enzymes like $Na^+K^+ATPase,\;Ca^{2+}ATPase,\;Mg^{2+}ATPase$ and decreased lipid peroxidation in heart tissue Results demonstrated that rats which received GTE were less susceptible to such changes indicating protection afforded by GTE.

Freeze Denaturation of Squid Actomyosin

  • Lee Kang-Ho;Ryu Hong-Soo;Cho Young-Je;Jung Byung-Chun;Hong Byung-Il;Je Yoi-Kwon;Lee Goon-Ja
    • Fisheries and Aquatic Sciences
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    • 제2권1호
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    • pp.12-16
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    • 1999
  • Denaturation of actomyosin from the obliquely striated mantle muscle of squids (Todarodes pacificus) was studied by measuring the changes in $Ca^{2+}$-ATPase activity, relative viscosity, and solubility during frozen storage at three different temperature zones of maximum ice crystal formation $(-3^{\circ}C,\;-\;-5^{\circ}C)$, the eutectic point $(-11^{\circ}C)$, and $-20^{\circ}C$. The logarithms of $Ca^{2+}$-ATPase activity, relative viscosity and solubility of the actomyosin solutions (0.6 M KCl) and suspensions (0.05 M KCl) tended to decrease during frozen storage. The denaturation of squid actomyosin at the zone of maximum ice crystal formation significantly differed by only two degree of temperature difference between $-3^{\circ}C$ and $-5^{\circ}C$, and it (0.05 M KCl) at $-3^{\circ}C$ was less than those of other temperature. The denaturation at $-11^{\circ}C$ was more rapid than at $-5^{\circ}C$. The logarithms of $Ca^{2+}$ -ATPase activity, relative viscosity, and solubility were changed slower in the suspensions (0.05 M KCl) than the solutions (0.6 M KCl) at all experimental temperatures.

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Identification of Phospholipase C Activated by $GTP{\gamma}S$ in Plasma Membrane of Oat Cell

  • Kim, Hyae-Kyeong;Park, Moon-Hwan;Chae, Quae
    • BMB Reports
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    • 제28권5호
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    • pp.387-391
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    • 1995
  • In order to investigate whether phospholipase C (PLC) activity in oat celIs is regulated by Gprotein, we have characterized PLC in plasma membranes of oat tissues. To identify the purified plasma membrane, $K^+$-stimulated, $Mg^{2+}$-dependent ATPase activity was measured. The activity of ATPase was shown to be proportional to the concentration of membrane protein. To examine the PLC activity regulated by G-protein, we used the inside-out and outside-out plasma membrane mixture isolated from the oat cells. The plasma membrane mixture showed higher PLC activity than the one of the outside-out plasma membrane. This suggests that PLC activity is located at the cytoplasmic surface of plasma membrane. PLC activity in plasma membrane mixture was dependent on $Ca^{2+}$ with maximum activity at 100 ${\mu}m$ $Ca^{2+}$ and it was inhibited by 1 mM EGTA. Using Sep-pak $Accell^{TM}$ Plus QMA chromatography, we found that inositol 1,4,5-trisphosphate ($IP_3$) was produced in the presence of 10 ${\mu}m$ $Ca^{2+}$. The PLC activity in the membrane was enhanced by an activator of G-protein ($GTP{\gamma}S$) and not by an inhibitor ($GDP{\beta}S$). This indicates that a G-protein is involved in the activation of PLC in the plasma membrane of oat cells.

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Effect of t-butylhydroperoxide on $Na^+-dependent$ Glutamate Uptake in Rabbit Brain Synaptosome

  • Lee, Hyun-Je;Kim, Yong-Keun
    • The Korean Journal of Physiology and Pharmacology
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    • 제1권4호
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    • pp.367-376
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    • 1997
  • The effect of an organic peroxide, t-butylhydroperoxide (t-BHP), on glutamate uptake was studied in synaptosomes prepared from cerebral cortex. t-BHP inhibited the $Na^+-dependent$ glutamate uptake with no change in the $Na^+-independent$ uptake. This effect of t-BHP was not altered by addition of $Ca^{2+}$ channel blockers (verapamil, diltiazem and nifedipine) or $PLA_2$ inhibitors (dibucaine, butacaine and quinacrine). However, the effect was prevented by iron chelators (deferoxamine and phenanthroline) and phenolic antioxidants (N,N'-diphenyl-phenylenediamine, butylated hydroxyanisole, and butylated hydroxytoluene). At low concentrations (<1.0 mM), t-BHP inhibited glutamate uptake without altering lipid peroxidation. Moreover, a large increase in lipid peroxidation by $ascorbate/Fe^{2+}$ was not accompanied by an inhibition of glutamate uptake. The impairment of glutamate uptake by t-BHP was not intimately related to the change in $Na^+-K+-ATPase$ activity. These results suggest that inhibition of glutamate uptake by t-BHP is not totally mediated by peroxidation of membrane lipid, but is associated with direct interactions of glutamate transport proteins with t-BHP metabolites. The $Ca^{2+}$ influx through $Ca^{2+}$ channel or $PLA_2$ activation may not be involved in the t-BHP inhibition of glutamate transport.

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인유 및 우유의 획분에 존재하는 표지효소들의 효소활성과 분포 (Enzymatic Activity and Distribution of Marker Enzymes between Human Milk and Bovine Milk with Their Separated Milk Fractions)

  • 조진국;무전안홍;김천제;김창한
    • 한국축산식품학회지
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    • 제18권2호
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    • pp.185-191
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    • 1998
  • Human milk and bovine milk in normal stage were fractionated four parts : whey, skimmilk membrane, and casein pellet. The specific activity (nmole / mim / mg protein) and distribution ratio(%) of suborganella marker enzymes in each separated milk fraction were determined. Especially, neutral $Ca^{2+}$-ATPase, acid $Ca^{2+}$-ATPase, NADH-cytochrome C reductase, and acid phosphatase were higher in human milk. However, both $Ca^{2+}$-ATPases were not detected in all fractions of bovine milk. On the other hand, 5'-nucleotidase, phosphodiesterase I, alkaline phosphatase, and $\gamma$-glutamyl transpeptidase activities in bovine milk were higher than in human milk. Most of the marker enzymes were highly distributed in cream fraction of either human milk or bovine milk, and their specific activities were high to 24 fold from 3 fold when compared with that of whole milk. These results suggest that marker enzymes in mammary epitherial cell are transfered into cream fraction by the membrane rearrangement, and different biochemical reaction between human and bovine exists for milk secretion in mammary gland.

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Calcium and bioenergetics: from endoplasmic reticulum to mitochondria

  • Lee, Duk-Gyu;Michalak, Marek
    • Animal cells and systems
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    • 제16권4호
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    • pp.269-273
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    • 2012
  • Controlling metabolism throughout life is a necessity for living creatures, and perturbation of energy balance elicits disorders such as type-2 diabetes mellitus and cardiovascular disease. $Ca^{2+}$ plays a key role in regulating energy generation. $Ca^{2+}$ homeostasis of the endoplasmic reticulum (ER) lumen is maintained through the action of $Ca^{2+}$ channels and the $Ca^{2+}$ ATPase pump. Once released from the ER, $Ca^{2+}$ is taken up by mitochondria where it facilitates energy metabolism. Mitochondrial $Ca^{2+}$ serves as a key metabolic regulator and determinant of cell fate, necrosis, and/or apoptosis. Here, we focus on $Ca^{2+}$ transport from the ER to mitochondria, and $Ca^{2+}$-dependent regulation of mitochondrial energy metabolism.

Antifungal Mechanism of Antifungal Peptide Derived from Cecropin A(1-8)- Melittin(1-12) Hybrid against Aspergillus fumigatus

  • Lee, Dong-Gun;Jin, Zhe-Zhu;Maeng, Cheol-Young;Shin, Song-Yub;Seo, Moo-Yeol;Kim, Kil-Lyong;Hahm, Kyung-Soo
    • Journal of Microbiology and Biotechnology
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    • 제9권2호
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    • pp.168-172
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    • 1999
  • The antifungal mechanism of the antifungal peptide against Aspergillus fumigatus, $K^{18,19}$-CA(l-8)-ME(l-12), derived from cecropin A(l-8)-melittin(l-12) was investigated by confocal laser scanning microscopy, cell wall regeneration, ATPase activity inhibition, and released potassium ion. By confocal laser scanning microscopy, $K^{18,19}$-CA(l-8)-ME(l-12) was detected on the surface of A. fumigatus, while cecropin A used as a negative control peptide was not detected. The protoplast of A. fumigatus treated with$K^{18,19}$-CA(1-8)-ME(1-12) failed to regenerate the fungal cell walls. Compared with cecropin A, the amount of potassium ion released by $K^{18,19}$-CA(l-8)-ME(l-12) was increased. Furthermore, $K^{18,19}$-CA(l-8)-ME(l-12) inhibited the ATPase activity on the plasma membrane. These results suggested that $K^{18,19}$-CA(l-8)-ME(1-12) acts on the plasma membrane of A. fumigatus and its antifungal action is due to the ion channel or pore formation on the plasma membrane.

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Porcine Myofibrillar Protein에 대한 비교생화학적 연구 (Comparative Biochemical Study on the Myofibrillar Proteins from Porcine Muscle)

  • 양융;박현주;김영호;진홍승;신완철
    • 한국식품과학회지
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    • 제18권6호
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    • pp.443-449
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    • 1986
  • 근원섬유구성단백질의 SDS-polyacrylamide gel 전기 영동상으로 부터 돼지근육의 red muscle과 while muscle의 근원섬유단백질사이에는 30K성분함량의 특징적 차이가 나타났으며, 생물활성에서도 red muscle쪽이 white muscle쪽보다 높은 ATPase 활성을 나타내었다. 근원섬유단핵질의 열안정성은 D값에서 확실한 차이를 보여 white muscle쪽이 red muscle쪽보다 높은 열안정성을 나타냈고, 열역학량에서도 근섬유 type간의 차이를 보였다. 한편 근원섬유단백질의 열안정성은 생체조직에 가까운 형태일수륵 안정하다는 사실도 확인되었다.

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Hydrogen peroxide attenuates refilling of intracellular calcium store in mouse pancreatic acinar cells

  • Yoon, Mi Na;Kim, Dong Kwan;Kim, Se Hoon;Park, Hyung Seo
    • The Korean Journal of Physiology and Pharmacology
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    • 제21권2호
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    • pp.233-239
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    • 2017
  • Intracellular calcium ($Ca^{2+}$) oscillation is an initial event in digestive enzyme secretion of pancreatic acinar cells. Reactive oxygen species are known to be associated with a variety of oxidative stress-induced cellular disorders including pancreatitis. In this study, we investigated the effect of hydrogen peroxide ($H_2O_2$) on intracellular $Ca^{2+}$ accumulation in mouse pancreatic acinar cells. Perfusion of $H_2O_2$ at $300{\mu}M$ resulted in additional elevation of intracellular $Ca^{2+}$ levels and termination of oscillatory $Ca^{2+}$ signals induced by carbamylcholine (CCh) in the presence of normal extracellular $Ca^{2+}$. Antioxidants, catalase or DTT, completely prevented $H_2O_2$-induced additional $Ca^{2+}$ increase and termination of $Ca^{2+}$ oscillation. In $Ca^{2+}$-free medium, $H_2O_2$ still enhanced CCh-induced intracellular $Ca^{2+}$ levels and thapsigargin (TG) mimicked $H_2O_2$-induced cytosolic $Ca^{2+}$ increase. Furthermore, $H_2O_2$-induced elevation of intracellular $Ca^{2+}$ levels was abolished under sarco/endoplasmic reticulum $Ca^{2+}$ ATPase-inactivated condition by TG pretreatment with CCh. $H_2O_2$ at $300{\mu}M$ failed to affect store-operated $Ca^{2+}$ entry or $Ca^{2+}$ extrusion through plasma membrane. Additionally, ruthenium red, a mitochondrial $Ca^{2+}$ uniporter blocker, failed to attenuate $H_2O_2$-induced intracellular $Ca^{2+}$ elevation. These results provide evidence that excessive generation of $H_2O_2$ in pathological conditions could accumulate intracellular $Ca^{2+}$ by attenuating refilling of internal $Ca^{2+}$ stores rather than by inhibiting $Ca^{2+}$ extrusion to extracellular fluid or enhancing $Ca^{2+}$ mobilization from extracellular medium in mouse pancreatic acinar cells.

저장온도에 따른 쇠고기 근원섬유의 형태적, 효소적 성질 변화 (Changes in Morphologic and Enzymatic Properties of Beef Myofibrillar Protein by Storage Tmeperature)

  • 정인철
    • 한국식품영양학회지
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    • 제10권4호
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    • pp.468-474
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    • 1997
  • 쇠고기의 사태, 갈비 및 등심부위를 8$^{\circ}C$에 저장하면서 육질의 변화를 검토하기 위해 전단력가, 근원섬유의 소편화, actomyosin의 추출성 및 ATPase 활성을 측정하였다. 사태 및 등심부위의 전단력가는 저장 6일째 현저하게 낮아졌고, 갈비부위는 저장기간 동안 현저한 차이가 없었다. 저장초기 부위별 전단력가는 갈비, 등심 및 사태부위의 순으로 현저한 차이가 있었으나 저장기간이 경과하면서 갈비 및 등심부위는 비슷하였다. 근원 섬유 소편화도의 경우 사태부위는 저장 6일째 현저한 증가를 보였지만 갈비와 등심부위는 저장기간동안 계속 증가하였다. 근원섬유의 소편화율도 소편화도와 비슷한 양상이었으며, 갈비와 등심부위는 사태부위와 다른 변화를 보였다. Actomyosin의 추출성은 저장초기 갈비, 등심 및 사태부위의 순으로 높게 나타났으며 3일째 모든 부위가 증가하다가 등심부위는 저장 6일째 감소하였다. Acomyosin의 Mg2+-ATPase 활성의 경우, 사태부위는 저장 3일째 증가하다가 6일째 저장 0일의 수준으로 회복되었고, 갈비 및 등심부위는 비슷한 변화를 나타내었지만 0일째는 등심부위가 갈비부위보다 높게 나타났다. 그리고 사태부위의 Ca2+-ATPase 활성도 저장 3일째 증가하다가 6일째 감소하였으며, 갈비부위는 저장 중 변화가 없었고, 등심부위는 저장기간 동안 완만하게 감소하였다.

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