Kometini Z P, Dzhariashvili T Ia, Tsakadze L G
Biokhimiia. 1975 Sep-Oct;40(5):1039-46.
Effect of acetylcholine (ACh) on Na, K-ATPase system has a complex character. ACh concentration, as well as the type of membrane are responsible for the increase or decrease of Na, K-ATPase activity. The inhibition and activation capacity is not constant in different subcellular fractions. The maximal effect is observed in subcellular fractions rich in junctional complexes, whereas minimal effect is in microsomes. There is no effect in mitochondria and myelin at all. EGTA and EDTA removes the inhibition, but the activation remains unchanged. ACh is supposed to release from membrane structure Ca2+, which subsequently inhibits Na, K-ATPase. On the other hand, activation by ACh is the result of its direct effect. The inhibition prevails over the activation at high (2-10 mM) concentration of ACh, whereas at low (2mM) concentration it might be vice versa. Thus the effect of ACh on Na K-ATPase is the result of two different processes having opposite effects.
乙酰胆碱(ACh)对钠钾ATP酶系统的作用具有复杂的特性。ACh的浓度以及膜的类型决定了钠钾ATP酶活性的升高或降低。在不同的亚细胞组分中,其抑制和激活能力并非恒定不变。在富含连接复合体的亚细胞组分中观察到最大效应,而在微粒体中效应最小。在线粒体和髓磷脂中则完全没有作用。乙二醇双四乙酸(EGTA)和乙二胺四乙酸(EDTA)可消除抑制作用,但激活作用保持不变。据推测,ACh从膜结构中释放出钙离子,随后抑制钠钾ATP酶。另一方面,ACh的激活作用是其直接作用的结果。在高浓度(2 - 10 mM)的ACh下,抑制作用强于激活作用,而在低浓度(2 mM)时情况可能相反。因此,ACh对钠钾ATP酶的作用是两个具有相反效应的不同过程的结果。