Protein kinase C modulates hormone secretion regulated by extracellular polycations in bovine parathyroid cells.
Protein kinase C modulates hormone secretion regulated by extracellular polycations in bovine parathyroid cells.
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蛋白激酶 C 调节牛甲状旁腺细胞中胞外聚阳离子调节的激素分泌。
DOI：
10.1113/jphysiol.1993.sp019765
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Nemeth,EF
中科院分区：
文献类型：
--
作者：
Racke,FK;Nemeth,EF
1. 在离解的牛甲状旁腺细胞中检查了蛋白激酶 C (PKC) 在甲状旁腺激素 (PTH) 分泌调节中的作用。 2.将细胞外Ca2+浓度从0.5 mM增加至2 mM可抑制PTH分泌60-80%。通过将细胞外 Mg2+ 浓度从 1 mM 增加至 7 mM 或添加 La3+（至 40 µM），可以获得类似的分泌抑制作用。 PKC 激活剂佛波醇肉豆蔻酸酯乙酸酯 (PMA) 在细胞外 Ca2+、Mg2+ 或 La3+ 浓度较低时抑制 PTH 分泌，在较高浓度时增强分泌。 PKC 对分泌的抑制作用与细胞外 Ca2+ 升高引起的抑制作用的大小呈正相关。 3. PKC激活剂对PTH分泌的刺激作用被完全逆转，而PKC抑制剂十字孢碱则部分逆转了抑制作用。星形孢菌素单独使用时不会影响低浓度 (0.5 mM) 或高浓度 (2 mM) 细胞外 Ca2+ 的分泌，但会抑制中等浓度（约 1 mM）细胞外 Ca2+ 的分泌。 4. PKC 激活剂对分泌的刺激作用通过增加细胞外 Ca2+（至 5 或 10 mM）或 La3+（至 100 microM）浓度来克服。相反，将细胞外 Mg2+ 浓度增加至 11 或 19 mM 并不能减轻 PKC 激活剂的增强作用。 Ca2+ 和 Mg2+ 获得的不同结果不能用它们对胞质 Ca2+ 的不同影响来解释，并且表明不同的阳离子可以具有不同程度的功效来激活与牛甲状旁腺细胞上的 Ca2+ 受体相关的功能反应。 5.异丙肾上腺素刺激的PTH分泌不受PKC激活剂或十字孢菌素的影响。同样，细胞外 ATP gamma S 对分泌的抑制作用不受 PKC 激活剂的影响。这些结果表明 PKC 激活剂特异性影响由细胞外聚阳离子调节的 PTH 分泌。 6. PKC 激活剂对分泌的刺激作用与其对 [Ca2+]i 和三磷酸肌醇形成的抑制作用平行，表明 PKC 削弱了与细胞外 Ca(2+) 诱导的分泌抑制相关的机制。这些作用的特异性表明 PKC 在甲状旁腺细胞中刺激分泌耦合的早期阶段发挥作用，特定于细胞外聚阳离子所使用的作用，并且可能涉及 Ca2+ 受体。
1. The role of protein kinase C (PKC) in the regulation of parathyroid hormone (PTH) secretion was examined in dissociated bovine parathyroid cells. 2. Increasing the concentration of extracellular Ca2+ from 0.5 to 2 mM inhibited PTH secretion by 60‐80%. Similar depressive effects on secretion were obtained by increasing the concentration of extracellular Mg2+ from 1 to 7 mM or by adding La3+ (to 40 microM). The PKC activator phorbol myristate acetate (PMA) depressed PTH secretion at the lower and potentiated secretion at the higher concentrations of extracellular Ca2+, Mg2+ or La3+. The inhibitory effect of PKC on secretion correlated positively with the magnitude of the inhibitory effect elicited by elevated extracellular Ca2+. 3. The stimulatory effects of PKC activators on PTH secretion were reversed completely and the inhibitory effects were reversed partially by the PKC inhibitor staurosporine. Staurosporine alone did not affect secretion at low (0.5 mM) or high (2 mM) concentrations of extracellular Ca2+ but it did depress secretion at intermediate concentrations (around 1 mM) of extracellular Ca2+. 4. The stimulatory effects of PKC activators on secretion were overcome by increases in the concentration of extracellular Ca2+ (to 5 or 10 mM) or La3+ (to 100 microM). In contrast, increasing the concentration of extracellular Mg2+ to 11 or 19 mM did not alleviate the potentiating effects of PKC activators. The different results obtained with Ca2+ and Mg2+ could not be explained by their different effects on cytosolic Ca2+ and suggests that different cations can have varying degrees of efficacy to activate functional responses linked to the Ca2+ receptor on bovine parathyroid cells. 5. PTH secretion stimulated by isoprenaline was not affected by PKC activators or staurosporine. Similarly, the inhibitory effects of extracellular ATP gamma S on secretion were unaffected by PKC activators. These results show that PKC activators affect specifically PTH secretion regulated by extracellular polycations. 6. The stimulatory effect of PKC activators on secretion parallels its inhibitory effects on [Ca2+]i and inositol trisphosphate formation, showing that PKC blunts the mechanisms associated with extracellular Ca(2+)‐induced inhibition of secretion. The specificity of these actions suggests that PKC acts at a very early step of stimulus‐secretion coupling in parathyroid cells, specific to that used by extracellular polycations and perhaps involving the Ca2+ receptor.
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