Hexanol and lidocaine affect the oligomeric state of the Ca-ATPase of sarcoplasmic reticulum.
Hexanol and lidocaine affect the oligomeric state of the Ca-ATPase of sarcoplasmic reticulum.
复制标题
己醇和利多卡因影响肌浆网 Ca-ATP 酶的寡聚状态。
DOI：
10.1021/bi00249a007
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Thomas,DD
中科院分区：
文献类型：
--
作者：
Kutchai,H;Mahaney,JE;Geddis,LM;Thomas,DD
摘要：己醇在7℃时刺激肌浆网ca - atp酶的活性。对Ca-ATPase被异硫氰酸红素共价标记的SR的时间分辨磷光光谱研究表明，在7时，车甾醇(1)导致磷光各向异性衰变速率的浓度依赖性增加，(2)导致Ca-ATPase的较大低聚物解离成较小的低聚物，(3)增加Ca-ATPase在所有低聚物状态下的旋转迁移率。SR中自旋标记硬脂酸（SASL）的电子顺磁共振（EPR）谱表明，在7℃时，己醇降低了SR脂质在边界脂质域的比例，并使边界脂质域和无限制脂质域紊乱和流化。在提取的SR脂质无蛋白脂质体中，己醇在脂质双分子层中心附近比在极性头基团附近更大程度地增加流动性和降低有序度。在25℃时，己醇对ca - atp酶活性有双相影响：在10和20 mM时，己醇增加活性，但在30 mM，特别是在40 mM时，ca - atp酶活性受到抑制。25℃下己醇对ca - atp酶低聚态的影响也是双相的。在10和20 mM的浓度下，己醇促进较大的低聚物解离成较小的低聚物，而在30和40 mM的浓度下，己醇使较小的低聚物形成较大的低聚物。利多卡因在25℃时抑制Ca-ATPase活性，通过使Ca-ATPase小聚物形成较大的低聚物，显著减缓了eritc标记的SR的磷光各向异性的衰减。在25℃的SR脂质无蛋白脂质体中，利多卡因紊乱并流化双分子层中心附近的酰基链（与己醇一样），但在极性头基附近有相反的作用。己醇和利多卡因对SR ca - atp酶低聚态的相反作用为己醇和利多卡因对ca - atp酶活性的相反作用提供了新的分子解释。我们得出结论，己醇对ca - atp酶活性的双相效应可以通过己醇对ca - atp酶低聚态的双相效应来解释。这项研究支持了麻醉药可以改变膜蛋白之间相互作用的观点。
Revised Manuscript Received August 9, 1994s abstract: Hexanol at 7 C stimulates the activity of the Ca-ATPase of sarcoplasmic reticulum (SR). Time-resolved phosphorescence spectroscopystudies of SR whose Ca-ATPase is covalently labeled with erythrosin isothiocyanate (ERITC) indicate that at 7 Chexanol (1) causes a concentration-dependent increase in the rate of decay of phosphorescence anisotropy,(2) causes larger oligomers of Ca-ATPase to dissociate into smaller oligomers, and (3) increases the rotationalmobility of Ca-ATPase in all its oligomeric states. Electron paramagnetic resonance(EPR) spectroscopy of spin-labeled stearic acid (SASL) in SR suggests that at 7 C hexanol diminishes the fraction of SR lipids in the boundary lipid domain and disorders and fluidizes both the boundary lipid and the unrestricted lipid domain. In protein-free liposomes of extracted SR lipids hexanol increases fluidity and decreases order to a greater extent near the center of the lipid bilayer than near the polar head groups. At 25 C hexanol has biphasic effects on Ca-ATPase activity: at 10 and 20 mM hexanol increases activity, but at 30 mM and especially at 40 mM there is inhibition of Ca-ATPase activity. The influence of hexanol at 25 C on the oligomeric state of Ca-ATPase is also biphasic. At 10 and20 mM, hexanol promotes the dissociation of larger oligomers into smaller ones, whereas at higher concentrations, 30 and 40 mM, hexanol causes larger oligomers to be formed from smaller ones. Lidocaine at 25 C inhibits Ca-ATPase activity and causes dramatic slowing of the decay of phosphorescence anisotropy of ERITC-labeled SR by causing the formation of larger oligomers of Ca-ATPase from smaller ones. In protein-free liposomes of SR lipids at 25 C, lidocaine disorders and fluidizes the acyl chains near the center of the bilayer (as did hexanol), but has opposite effects near the polar head groups. The opposite effects of hexanol and lidocaine on the oligomeric state of the SR Ca-ATPase provide a new molecular explanation for the opposite effects of hexanol and lidocaine on the activity of the Ca-ATPase. We conclude that the biphasic effects of hexanol on the activity of Ca-ATPase can be accounted for by biphasic effects of hexanol on the oligomeric state of the Ca-ATPase. This study supports the view that anesthetics can alter interactions between membrane proteins.
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DOI：
--
发表时间：
1976
期刊：
Biochimica et Biophysica Acta
影响因子：
--
作者：
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影响因子：
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作者：
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