Rabbit myocardial membrane Ca2+-adenosine triphosphatase activity: stimulation in vitro by thyroid hormone.
Rabbit myocardial membrane Ca2+-adenosine triphosphatase activity: stimulation in vitro by thyroid hormone.
复制标题
兔心肌膜Ca2-腺苷三磷酸酶活性：甲状腺激素体外刺激。
DOI：
10.1016/0003-9861(84)90165-6
复制
发表时间：
1984
影响因子：
3.9
通讯作者：
S. D. Blas
中科院分区：
文献类型：
--
作者：
A. Rudinger;K. Mylotte;P. Davis;F. B. Davis;S. D. Blas
最近报道了生理浓度的甲状腺激素对人和兔红细胞膜Ca ~（2+）-ATP酶活性的体外刺激作用。为了将这些观察结果扩展到有核细胞模型，研究了从兔心肌获得的膜制剂中的Ca 2 +-ATP酶活性。5′-核苷酸酶的活性比心肌匀浆增加了26倍，与肌膜富集一致。9只动物膜中的平均基础酶活性为20.8 ± 3.3 μmolPimg膜蛋白−190 min−1，约为兔红细胞膜中所述活性的20倍。心肌细胞膜暴露于甲状腺素（T4）（10 - 10 μ m）后，Ca ~（2+）-ATP酶活性增加到29.2 ± 3.8 μmolPi（P< 0.001）。用T4进行的剂量反应研究表明，在10 - 10米处获得最大刺激反应。对于l-T4和三碘甲腺原氨酸（T3）（10− 10 m），激素刺激相当。四碘甲状腺乙酸没有生物活性，而三碘甲状腺乙酸和d-T4，在10− 10米处，与对照（基础）水平相比，显着降低酶活性。三氟拉嗪（100 μm）和萘磺酰胺W-7（50-100 μm）可阻断钙调素（Ca 2 +-ATP酶的蛋白激活剂）的作用。放射免疫分析显示，心肌膜部分中存在钙调素（1.4 μg mg膜蛋白−1），胞浆中存在0.35 μg mg− 1。心肌Ca ~（2+）-ATP酶活性，显然是肌膜来源的，因此是甲状腺激素刺激的。这种钙泵相关酶的激素反应需要钙调蛋白。
Thein vitrostimulation of human and rabbit erythrocyte membrane Ca2+-ATPase activity by physiological concentrations of thyroid hormone has recently been described. To extend these observations to a nucleated cell model, Ca2+-ATPase activity in a membrane preparation obtained from rabbit myocardium has been studied. Activity of 5′-nucleotidase in the preparation was increased 26-fold over that of myocardial homogenate, consistent with enrichment by sarcolemma. Mean basal enzyme activity in membranes from nine animals was 20.8 ± 3.3 μmolPimg membrane protein−190 min−1, approximately 20-fold the activity described in rabbit red cell membranes. Exposure of heart membranesin vitrotol-thyroxine (T4) (10−10m) increased Ca2+-ATPase activity to 29.2 ± 3.8 μmolPi(P< 0.001). Dose-response studies conducted with T4showed that maximal stimulatory response was obtained at 10−10m. Hormonal stimulation was comparable forl-T4and triiodo-l-thyronine (T3) (10−10m). Tetraiodothyroacetic acid was without biological activity, whereas triiodothyroacetic acid andd-T4, each at 10−10m, significantly decreased enzyme activity compared to control (basal) levels. The action ofl-T4on myocardial membrane Ca2+-ATPase activity was inhibited by trifluoperazine (100 μm) and the naphthalenesulfonamide W-7 (50–100 μm), compounds that block actions of calmodulin, the protein activator of membrane-associated Ca2+-ATPase. Radioimmunoassay revealed the presence of calmodulin (1.4 μg mg membrane protein−1) in the myocardial membrane fraction and 0.35 μg mg−1in cytosol. Myocardial Ca2+-ATPase activity, apparently of sarcolemmal origin, is thus thyroid hormone stimulable. The hormonal responsiveness of this calcium pump-associated enzyme requires calmodulin.
兔心室肌球蛋白重链的两个分子变体的分离和表征。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Chizzonite,RA;Everett,AW;Clark,WA;Jakovcic,S;Rabinowitz,M;Zak,R
通讯作者：
Zak,R
轻度和重度原发性甲状腺功能减退症的心脏功能。
影响因子：
6.1
作者：
Ridgway,EC;Ladenson,PW;Cooper,DS;Daniels,GH;Francis,GS;Maloof,F
通讯作者：
Maloof,F
离体心脏肌浆网中钙调蛋白介导的钙转运调节和 (Ca2 Mg2 ) 激活的 ATP 酶活性。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Kirchberger,MA;Antonetz,T
通讯作者：
Antonetz,T