• Biomedical Science Letters
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• v.4 no.1
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• pp.27-33
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• 1998

This study has been designed in order to examine a physiological role of $Ca^{2+}$ which has been known as an essential factor for capacitation, to confirm whether the enzyme activity of $Ca^{2+}$-ATPase on capacitation is important or not, and to clarify relationship between various levels of the $Ca^{2+}$ concentration and $Ca^{2+}$-ATPase which has been known to be an important factor of the plasma membranes. In the present study applying quercetin, a $Ca^{2+}$-ATPase inhibitor, the enzymatic effect of $Ca^{2+}$-ATPase on capacitation was found to be remarkable: a significant increase of the transition from the original type (type A) to the type B and the type AR of the spermatozoa. This finding suggests that $Ca^{2+}$-ATPase plays an important role in the efflux and the influx of the $Ca^{2+}$ which has been known to be an essential factor the capacitation and acrosome reaction, and that the inhibitory action of the $Ca^{2+}$-ATPase might be a prerequsite step toward the acrosome reaction. The conclusion reached can be deduced as follows: increment of the intracelluar $Ca^{2+}$ concentration occurred by controlling the slope of $Ca^{2+}$ concentration through $Ca^{2+}$-ATPase activities in both the intra- and extracelluar fluid may be an important procedure for capacitation and acrosome reaction, and ultimately for fertilization of the spermatozoa and the ova.

• The Journal of Korean Medicine
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• v.18 no.1
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• pp.198-207
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• 1997

To explore the action mechanism of Ijintang in the brain, the authors investigated the effects of Ijintang fractions on MgNaK ATPase and MgCa ATPase in rat brain synaptosomes prepared from cerebral cortex. The activities of MgNaK ATPase and MgCa ATPase were assayed by the level of inorganic phosphate liberated from the hydrolysis of ATP. Fraction WH-95-7 at the concentration of $10^{-2}%$ decreased the activity of MgNaK ATPase about 34.1% and also reduced the activity of MgCa ATPase about 49.3% But, other fractions (WB-95-7, WC-95-7, MB-95-7, MC-95-7, MH-95-7) did not significantly changed the activities of the MgNaK ATPase and MgCa ATPase The decreased activity of MgNaK ATPase by WH-95-7 will decrease the rate of $Ca^{2+}$ efflux, probably via an Na-Ca exchange mechanism and will increase the rate of $Ca^{2+}$ entry by the depolarization of nerve terminals. The reduced activity of MgCa ATPase by WH-95-7 will result in the decreased efflux of $Ca^{2+}$. As a conclusion, it can be speculated that lithium elevates the intrasynaptosomal $Ca^{2+}$ concentration via inhibition of the activities of MgNaK ATPase and MgCa ATPase. and this increased $[Ca^{2+}]i$ will cause the release of neurotransmitters.

• Clinical and Experimental Reproductive Medicine
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• v.25 no.3
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• pp.269-275
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• 1998

It has been reported that the $Ca^{2+}$-ATPase and the $Ca^{2+}-Na^+$ exchanger play an important role for the regulation of intracellular $Ca^{2+}$ in somatic cells, the $Ca^{2+}$-ATPase located in the plasma membrane helps the $Ca^{2+}$ concentration in maintain low $[Ca^{2+}]_i$. Roldan & Fleming reported that the spermatozoan $Ca^{2+}$-ATPase plays an important role in the capacitation and acrosome reaction. We used to assess $Ca^{2+}$ changes by chlortetracycline (CTC) patterns in the capacitation and acrosome reaction of human and hamster spermatozoa. In the present study applying quercetin which has been known as an ATPase antagonist, the enzymatic effect of $Ca^{2+}$-ATPase on capacitation and acrosome reaction was found to be remarkable: a significant increase of the transformation from the original type to the B type and the AR type of spermatozoa. This finding suggests that $Ca^{2+}$-ATPase play an important role in the efflux and the influx of the $Ca^{2+}$ which have been known to be an essential factor for the capacitation and acrosome reaction, and that the inhibitory action of the $Ca^{2+}$-ATPase might be a prerequsit step toward the capacitation and acrosome reaction. In conclusion, this study suggest the considerable evidence as follows: the increment of the intracellular $Ca^{2+}$ concentration occurred by controlling the slope of $Ca^{2+}$ concentration through $Ca^{2+}$-ATPase activites in both the intracellular and extracellulr fluid may be important procedures for the capacitation and the acrosome reaction, and finally for fertilization of the sperm and ovum.

• The Korean Journal of Zoology
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• v.17 no.2
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• pp.93-102
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• 1974

Fragmente dsarcoplasmic reticulum of rabbit skeletal muscle was prepared and biochemical properties of its ATPase activity were studied. The ATPase of the fragments could be distinguished as $Mg^++ - ATPase and (Mg^++ - Ca^++)$-ATPase. The activity of $(Mg^++ - Ca^++)$-ATPase was predominant over that of $Mg^++$-ATPase in the temperature range of $0 \\sim 40^\\circ C$ and in the pH 6.4$\\sim$7.6. At higher temperatures the predominance of $(Mg^++ - Ca^++)$-ATpase was far greater. The apparent energies of activation were 14 kcal/mole for $Mg^++$-ATPase, 21kcal/mole for $(Mg^++ - Ca^++)$-ATPase, and 18kcal/mole for total ATPase. Changes in pH and Mg concentration did not alter the energies of activation of these ATPases. The Km values of these ATPases were found to be 0.36 mM for $Mg^++$-ATPase, 2.20 mM for $(Mg^++ - Ca^++)$-ATpase, and 0.86 mM for total ATPase.

• Journal of the korean academy of Pediatric Dentistry
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• v.10 no.1
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• pp.139-147
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• 1983

This study was undertaken to evaluate the physiological roles & mechanism of $Ca^{++}$-ATPase & $Mg^{++}$-ATPase in human dental pulp. Each specimen of dental pulp was obtained from the freshly extracted, freeze-dried 242 teeth. $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were measured by the release of inorganic phosphate & protein with Spectrophotometer. The results were as follows; 1. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significantly increased in developing teeth. 2. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significantly decreased in nonvital teeth. 3. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity were significant decreased in deciduous teeth. 4. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase activity didn't have relation with dental caries. 5. The $Ca^{++}$-ATPase & $Mg^{++}$-ATPase were activated by either $Ca^{++}$ alone or $Mg^{++}$ alone.

• KSBB Journal
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• v.11 no.5
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• pp.518-523
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• 1996

The sensor to determine ATPase activities was consisted of an immobilized enzyme membrane(purine nucloside phosphoryrase and xanthine oxidase) and an oxygen electrode. The proposed sensor was used for the determination of $K^+-, Ca^{2}+- and Mg^{2+}-$ATPase activities in several fish muscle proteins such as Thunnus albacares(Yellowfin tuna), Tetrapturus audax(Striped marlin), Prognichthys agoo(Japanese flyingfish), and Cypvinus carpio(Carp). $K^+-, Ca^{2}-$ATPase activities measured by the proposed sensor system were in good agreement with the results obtained by a conventional colorimetric assay. One cycle of assay could be completed within 3mlnutes.

• The Korean Journal of Physiology
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• v.20 no.2
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• pp.157-164
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• 1986

Since it has been reported that vanadate inhibits $Ca^{++}-ATPase$ activity without affecting $Ca^{++}$ uptake, this study was undertaken to investigate the effects of vanadate on $Ca^{++}-ATPase$ activity and $Ca^{++}$ uptake in the sarcoplasmic reticulum of rat skeletal muscle. The following results were obtained. 1) $Ca^{++}$ activated ATPase activity of the intact sarcoplasmic reticulum was significantly inhibited when vanadate was added to the incubation medium at concentration greater than $10^{-6}\;M$. However $Mg^{++}$-ATPase activity of the intact SR was not affected by vanadate at concentrations ranging from $10^{-7}\;to\;10^{-4}\;M.$ Similarly, $Ca^{++}-ATPase$ activity in sonicated sarcoplasmic reticulum was significantly reduced by vanadate at a concentration $10^{-7}$ M or higher. 2) The uptake of $Ca^{++}$ by isolated sarcoplasmic reticulum was also inhibited by vanadate under the conditions where the turnover rate of $Ca^{++}-ATPase$ was made to increase. These results suggest that the inhibition of $Ca^{++}$ uptake by vanadate may be correlated with that of $Ca^{++}-ATPase$ if experimental conditions are properly set.

• 한국유가공학회:학술대회논문집
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• 1997.05a
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• pp.23-34
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• 1997

Calcium-stimulated ATPase ($Ca^{2+}$-ATPase) which has optimal pH value at 7.0 was found in the membrane fraction of human milk, and its enzymatic properties were studied. The purified $Ca^{2+}$-ATPase required 0.45 mM Ca ion for maximal activity. Among the nucleosides, $Ca^{2+}$-ATPase showed a higher substrate specificity to ATP and UTP than to CTP and GTP. $Ca^{2+}$-ATPase had apparent Km value of 0.065, and V max of 7.63 mol ATP hydrolyzed/mg pro-tein per min, respectively. $Ca^{2+}$-ATPase was potently inhibited by lanthanide, vanadate, and p-chloromercuribenzoate, and inactivated by EDTA, and CDTA and EGTA, but were unaffected by N-ethylmaleimide, $NaN_3$, ouabain, or oligomycin, and was completely inactivated by heating at $60^{\circ}C$ for 10 min. This enzyme activity was concentrated in the membrane fraction of the cream and skim milk membrane, but not founded in bovine milk.

• Journal of Life Science
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• v.21 no.5
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• pp.671-677
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• 2011

We previously reported the isolation and characterization of a gene, SCA1 (for soybean $Ca^{2+}$-ATPase 1), encoding a calmodulin-regulated $Ca^{2+}$-ATPase that is located in the plasma membrane in soybean. Here, a $Ca^{2+}$-ATPase designated as SCA2 was isolated from soybean. The two $Ca^{2+}$-ATPases, SCA1 and SCA2, share a remarkably high degree of similarity (78%). Ten transmemebrane domains were predicted by hydropathy analysis. Using gel overlay assays, CaM was found to bind to SCA2 in a $Ca^{2+}$-dependent manner. Southern blot analysis revealed the presence of two copies of the $Ca^{2+}$-ATPase gene in the soybean genome. An N-terminal truncation mutant that deletes sequence through the putative calmodulin binding site was able to complement a yeast mutant (K616) that was deficient in two endogenous $Ca^{2+}$ pumps. Our results indicate that SCA2 is structurally highly conserved with type IIB $Ca^{2+}$ pumps in plants.

• BMB Reports
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• v.29 no.1
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• pp.22-26
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• 1996

Agents that activate or inhibit the $Ca^{2+}$ release channel in cardiac sarcoplasmic reticulum (SR) were tested for their abilities to affect the activity of the SR $Ca^{2+}$-ATPase. Vesicles of junctional SR (heavy SR, HSR) from terminal cisternae were prepared from porcine cardiac muscle by density gradient centrifugation. The steady-state activity of $Ca^{2+}$-ATPases in intact HSR vesicles was/$347{\pm}5\;nmol/min{\cdot}mg$ protein (${\pm}$ SD). When the HSR vesicles were made leaky, the activity was increased to $415{\pm}5\;nmol/min{\cdot}mg$ protein. This increase is probably due to the uncoupling of HSR vesicles. Caffeine (10 mM), an agonist of the SR $Ca^{2+}$ release channel, increased $Ca^{2+}$-ATPase activity in the intact HSR vesicle preparation to $394{\pm}30\;nmol/min{\cdot}mg$ protein. However, caffeine had no significant effect in the leaky vesicle preparation and in the purified $Ca^{2+}$-ATPase preparation. The effect of caffeine on SR $Ca^{2+}$-ATPase was investigated at various concentrations of $Ca^{2+}$. Caffeine increased the pump activity over the whole range of $Ca^{2+}$ concentrations, from $1\;{\mu}M$ to $250\;{\mu}M$, in the intact HSR vesicles. When the SR $Ca^{2+}$-ATPase was inhibited by thapsigargin, no caffeine effect was observed. These results imply that the caffeine effect requires the intact vesicles and that the increase in $Ca^{2+}$-ATPase activity is not due to a direct interaction of caffeine with the enzyme. We propose that the activity of SR $Ca^{2+}$-ATPase is linked indirectly to the activity of the $Ca^{2+}$ release channel (ryanodine receptor) and may depend upon the amount of $Ca^{2+}$ released by the channels.