Benítez-King G, Antón-Tay F
Instituto Mexicano de Psiquiatría, Departamento de Neurofarmacologia, Col. San Lorenzo Huipulco, México.
Experientia. 1993 Aug 15;49(8):635-41. doi: 10.1007/BF01923944.
In this article, we review the data concerning melatonin interactions with calmodulin. The kinetics of melatonin-calmodulin binding suggest that the hormone modulates cell activity through intracellular binding to the protein at physiological concentration ranges. Melatonin interaction with calmodulin may allow the hormone to modulate rhythmically many cellular functions. Melatonin's effect on tubulin polymerization, and cytoskeletal changes in MDCK and N1E-115 cells cultured with melatonin, suggest that at low concentrations (10(-9) M) cytoskeletal effects are mediated by its antagonism to Ca2+-calmodulin. At higher concentrations (10(-5)M) non-specific binding of melatonin to tubulin occurs thus overcoming the specific melatonin antagonism to Ca2+-calmodulin. Since the structures of melatonin and calmodulin are phylogenetically well preserved, calmodulin-melatonin interaction probably represents a major mechanism for regulation and synchronization of cell physiology.
在本文中，我们综述了有关褪黑素与钙调蛋白相互作用的数据。褪黑素与钙调蛋白结合的动力学表明，该激素在生理浓度范围内通过细胞内与该蛋白结合来调节细胞活性。褪黑素与钙调蛋白的相互作用可能使该激素有节律地调节多种细胞功能。褪黑素对微管蛋白聚合的影响，以及用褪黑素培养的MDCK和N1E - 115细胞中的细胞骨架变化表明，在低浓度（10⁻⁹ M）时，细胞骨架效应是由其对Ca²⁺ - 钙调蛋白的拮抗作用介导的。在较高浓度（10⁻⁵ M）时，褪黑素与微管蛋白发生非特异性结合，从而克服了褪黑素对Ca²⁺ - 钙调蛋白的特异性拮抗作用。由于褪黑素和钙调蛋白的结构在系统发育上保存良好，钙调蛋白 - 褪黑素相互作用可能是调节和同步细胞生理的主要机制。
